PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
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
15046863-3	2004	When rapid movement is inhibited by geldanamycin (GA), a specific inhibitor of the protein chaperone hsp90, the GFP-GR translocates slowly to the nucleus by diffusion.	geldanamycin	36-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
15046863-3	2004	When rapid movement is inhibited by geldanamycin (GA), a specific inhibitor of the protein chaperone hsp90, the GFP-GR translocates slowly to the nucleus by diffusion.	geldanamycin	50-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
15046863-5	2004	In neurites, movement by diffusion is not possible, and we show that movement of the GFP-GR from neurites is blocked by geldanamycin, suggesting that the hsp90-dependent movement machinery is required for retrograde movement.	geldanamycin	120-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
14726529-3	2004	In addition, it became apparent that Hsp90 protects HIF-1alpha from oxygen-independent degradation.	Oxygen	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
15031341-2	2004	We evaluated the efficacy of methylprednisolone and urokinase pulse therapy combined with cyclophosphamide for patients with HSPN of at least grade IVb.	Methylprednisolone	29-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-129
15031341-2	2004	We evaluated the efficacy of methylprednisolone and urokinase pulse therapy combined with cyclophosphamide for patients with HSPN of at least grade IVb.	Cyclophosphamide	90-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-129
15031341-9	2004	CONCLUSIONS: Our study suggests that methylprednisolone and urokinase pulse therapy combined with cyclophosphamide is useful for patients with severe HSPN.	Methylprednisolone	37-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-154
15031341-9	2004	CONCLUSIONS: Our study suggests that methylprednisolone and urokinase pulse therapy combined with cyclophosphamide is useful for patients with severe HSPN.	Cyclophosphamide	98-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-154
15081540-5	2004	Not surprisingly, Hsp90 inhibitors behave as immunosuppressants, and also cause an induction of superoxide production.	Superoxides	96-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
14711833-7	2004	Geldanamycin treatment, which disrupts the HSP90-FKBP52 complex, resulted in >22-fold increase in AAV transduction in heat-shock-treated cells compared with heat shock alone.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
14711833-8	2004	Deliberate overexpression of the human HSP90 gene resulted in a significant decrease in AAV-mediated transduction in tyrphostin 23-treated cells, whereas down-modulation of HSP90 levels led to a decrease in HSP90-FKBP52-AAV D-sequence complex formation, resulting in a significant increase in AAV transduction following pre-treatment with tyrphostin 23.	Tyrphostins	117-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
14711833-8	2004	Deliberate overexpression of the human HSP90 gene resulted in a significant decrease in AAV-mediated transduction in tyrphostin 23-treated cells, whereas down-modulation of HSP90 levels led to a decrease in HSP90-FKBP52-AAV D-sequence complex formation, resulting in a significant increase in AAV transduction following pre-treatment with tyrphostin 23.	Tyrphostins	339-349	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
14711833-8	2004	Deliberate overexpression of the human HSP90 gene resulted in a significant decrease in AAV-mediated transduction in tyrphostin 23-treated cells, whereas down-modulation of HSP90 levels led to a decrease in HSP90-FKBP52-AAV D-sequence complex formation, resulting in a significant increase in AAV transduction following pre-treatment with tyrphostin 23.	Tyrphostins	339-349	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
14711833-8	2004	Deliberate overexpression of the human HSP90 gene resulted in a significant decrease in AAV-mediated transduction in tyrphostin 23-treated cells, whereas down-modulation of HSP90 levels led to a decrease in HSP90-FKBP52-AAV D-sequence complex formation, resulting in a significant increase in AAV transduction following pre-treatment with tyrphostin 23.	Tyrphostins	339-349	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
15039704-6	2004	Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.	Arginine	181-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
15039704-6	2004	Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.	Adenosine Triphosphate	222-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
14967193-0	2004	Hsp90 inhibitors attenuate effect of dexamethasone on activated NF-kappaB and AP-1.	Dexamethasone	37-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14967193-2	2004	Hsp90 inhibitors geldanamycin (GA) and radicicol (Rad) have been studied as anti-inflammatory agents; however, their effects on glucocorticoid-mediated anti-inflammatory mechanism are not known.	geldanamycin	17-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14967193-2	2004	Hsp90 inhibitors geldanamycin (GA) and radicicol (Rad) have been studied as anti-inflammatory agents; however, their effects on glucocorticoid-mediated anti-inflammatory mechanism are not known.	geldanamycin	31-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14967193-2	2004	Hsp90 inhibitors geldanamycin (GA) and radicicol (Rad) have been studied as anti-inflammatory agents; however, their effects on glucocorticoid-mediated anti-inflammatory mechanism are not known.	monorden	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14967193-2	2004	Hsp90 inhibitors geldanamycin (GA) and radicicol (Rad) have been studied as anti-inflammatory agents; however, their effects on glucocorticoid-mediated anti-inflammatory mechanism are not known.	monorden	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14967193-4	2004	In cell-based reporter assay, Hsp90 inhibitors inhibited Dex-induced nuclear import and transcriptional activity of GR.	Dexamethasone	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
14967193-5	2004	Both tumor necrosis factor-alpha-activated NF-kappaB and phorbol ester-activated AP-1 were inhibited by Dex and Hsp90 inhibitors alone.	Phorbol Esters	57-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
14967193-6	2004	When the cells were treated with a combination of these drugs, the inhibitory effect of Dex was significantly attenuated by Hsp90 inhibitors.	Dexamethasone	88-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
14967193-10	2004	These results suggest that Hsp90 inhibitor itself inhibits the activation of NF-kappaB and AP-1, however, impedes Dex-induced inhibition of IL-1beta induction by attenuating Dex-mediated activation of GR and inhibition of the proinflammatory transcription factors.	Dexamethasone	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
14967193-10	2004	These results suggest that Hsp90 inhibitor itself inhibits the activation of NF-kappaB and AP-1, however, impedes Dex-induced inhibition of IL-1beta induction by attenuating Dex-mediated activation of GR and inhibition of the proinflammatory transcription factors.	Dexamethasone	174-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
14982777-0	2004	Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-47
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-94
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-94
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	Adenosine Diphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-94
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	Adenosine Diphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-94
14982777-1	2004	Geldanamycin (GA) is an antibiotic targeting the ADP/ATP binding site of heat shock protein 90 (Hsp90).	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
14668343-5	2004	However, pretreatment of the cells with the Hsp90 inhibitor geldanamycin, which leads to proteasome-mediated degradation of receptor interacting protein 1 (RIP1), reverts FKBP-FADD-induced necrosis to apoptosis.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
14668343-5	2004	However, pretreatment of the cells with the Hsp90 inhibitor geldanamycin, which leads to proteasome-mediated degradation of receptor interacting protein 1 (RIP1), reverts FKBP-FADD-induced necrosis to apoptosis.	fadd	176-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
15040939-5	2004	Analysis of the antibody response which occurs in patients with invasive candidiasis, being treated with amphotericin B, showed a close correlation between recovery and antibody to the immunodominant heat shock protein 90 (hsp90).	Amphotericin B	105-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-221
14670946-7	2004	Ligand-dependent nuclear translocation of the wild-type receptor and misfolding and aggregation of the K632A/K633A mutant are blocked by radicicol, an Hsp90 inhibitor.	monorden	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
15040939-5	2004	Analysis of the antibody response which occurs in patients with invasive candidiasis, being treated with amphotericin B, showed a close correlation between recovery and antibody to the immunodominant heat shock protein 90 (hsp90).	Amphotericin B	105-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
15040939-7	2004	Mycograb is a human recombinant antibody to hsp90 which shows intrinsic antifungal activity and synergy with amphotericin B both in vitro and in vivo.	Amphotericin B	109-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
14551138-3	2004	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of various hsp90-dependent kinases important in oncogenesis.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-122
14739935-6	2004	Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.	Arginine	181-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
14739935-6	2004	Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.	Adenosine Triphosphate	222-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
14551138-3	2004	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of various hsp90-dependent kinases important in oncogenesis.	benzoquinoid ansamycin	51-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
14638689-3	2004	Glutathione S-transferase pull-down assays and co-immunoprecipitation experiments indicated the formation of stable complexes between S100A1 and Hsp90, Hsp70, FKBP52, and CyP40 both in vitro and in mammalian cells.	Glutathione	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
14551138-3	2004	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of various hsp90-dependent kinases important in oncogenesis.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
14551138-3	2004	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of various hsp90-dependent kinases important in oncogenesis.	benzoquinoid ansamycin	51-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
14551138-3	2004	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of various hsp90-dependent kinases important in oncogenesis.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
14551138-3	2004	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of various hsp90-dependent kinases important in oncogenesis.	benzoquinoid ansamycin	51-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-122
14661033-5	2004	Pretreatment of cells with either 1 microg/ml geldanamycin (a specific inhibitor of Hsp90) or 500 nM wortmannin (a specific PI3 kinase inhibitor) suppressed hypoxia-stimulated Akt and eNOS phosphorylation and significantly attenuated hypoxia-stimulated Hsp90 binding to eNOS.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
14709723-8	2004	Geldanamycin, a specific inhibitor of Hsp90, reversibly blocks myofibril assembly and triggers accumulation of myosin folding intermediates.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
14583611-6	2004	In addition, Hsp90 suppression in NN plants compromises N-mediated resistance to tobacco mosaic virus.	Nitrogen	34-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
14555685-1	2004	This study examines the notion that heat shock protein (HSP) 90 binding to nitric oxide (NO), endothelial NO synthase (eNOS), and PI3K-Akt regulate angiopoietin (Ang)-1-induced angiogenesis in porcine coronary artery endothelial cells (PCAEC).	Nitric Oxide	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-63
15106614-2	2004	The first Hsp90 inhibitor to enter clinical trials--the geldanamycin derivative 17AAG--has recently demonstrated proof-of-concept for successful target modulation, with sighs of therapeutic benefit.	geldanamycin	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15106614-2	2004	The first Hsp90 inhibitor to enter clinical trials--the geldanamycin derivative 17AAG--has recently demonstrated proof-of-concept for successful target modulation, with sighs of therapeutic benefit.	tanespimycin	80-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15106614-5	2004	New research now shows that Hsp90 exists in cancer cells in a heightened, activated state that is highly susceptible to inhibition by 17AAG.	tanespimycin	134-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
14698151-0	2004	Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures.	Adenine	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
14698151-1	2004	Multiple co-crystal structures of an adenine-based series of inhibitors bound to the molecular chaperone Hsp90 have been determined.	Adenine	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
14698045-6	2004	When compared to a panel of known protein kinase inhibitors, CMV423 was found to share anti-HHV-6 characteristics with herbimycin A, which affects tyrosine kinase activity through heat shock protein 90 (Hsp90) inhibition.	herbimycin	119-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-201
14698045-6	2004	When compared to a panel of known protein kinase inhibitors, CMV423 was found to share anti-HHV-6 characteristics with herbimycin A, which affects tyrosine kinase activity through heat shock protein 90 (Hsp90) inhibition.	herbimycin	119-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
14661033-5	2004	Pretreatment of cells with either 1 microg/ml geldanamycin (a specific inhibitor of Hsp90) or 500 nM wortmannin (a specific PI3 kinase inhibitor) suppressed hypoxia-stimulated Akt and eNOS phosphorylation and significantly attenuated hypoxia-stimulated Hsp90 binding to eNOS.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	253-258
14661033-5	2004	Pretreatment of cells with either 1 microg/ml geldanamycin (a specific inhibitor of Hsp90) or 500 nM wortmannin (a specific PI3 kinase inhibitor) suppressed hypoxia-stimulated Akt and eNOS phosphorylation and significantly attenuated hypoxia-stimulated Hsp90 binding to eNOS.	Wortmannin	101-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	253-258
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	geldanamycin	32-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	monorden	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	monorden	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	Dexamethasone	142-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	Corticosterone	157-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-4	2004	Hsp90 inhibitors; geldanamycin (GA) and radicicol (Rad), significantly accelerated nuclear export of GR after withdrawal of ligands including dexamethasone, corticosterone and RU486.	Mifepristone	176-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15062560-7	2004	Only nuclear-targeted Hsp90 prolonged basal nuclear retention of GR after withdrawal of dexamethasone and corticosterone.	Dexamethasone	88-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
15062560-7	2004	Only nuclear-targeted Hsp90 prolonged basal nuclear retention of GR after withdrawal of dexamethasone and corticosterone.	Corticosterone	106-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
14557268-4	2003	GRK2 interaction with Hsp90 was confirmed by co-immunoprecipitation and was effectively disrupted by geldanamycin, an Hsp90-specific inhibitor.	geldanamycin	101-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
15319539-10	2004	Hypoxic accumulation of HIF-1alpha was delayed in a novel cell model deficient for HSP90beta as well as after treatment of wild-type cells with the HSP90 inhibitor geldanamycin, suggesting that HSP90 activity is involved in the rapid HIF-1alpha protein induction.	geldanamycin	164-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
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
14718169-4	2004	Dimeric p50(cdc37) binds to surfaces of the Hsp90 N-domain implicated in ATP-dependent N-terminal dimerization and association with the middle segment of the chaperone.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
14976405-0	2004	Heat shock protein 90 recognized as an iron-binding protein associated with the plasma membrane of HeLa cells.	Iron	39-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
14976405-3	2004	Employing an iron-binding assay and mass spectrometric analysis, we have identified human Hsp90 as an iron-binding protein in membrane protein preparations of human HeLa cells.	Iron	13-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
14976405-3	2004	Employing an iron-binding assay and mass spectrometric analysis, we have identified human Hsp90 as an iron-binding protein in membrane protein preparations of human HeLa cells.	Iron	102-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
14976405-5	2004	The iron-binding assay with purified human Hsp90 confirmed iron binding by Hsp90.	Iron	4-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
14976405-5	2004	The iron-binding assay with purified human Hsp90 confirmed iron binding by Hsp90.	Iron	4-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
14976405-5	2004	The iron-binding assay with purified human Hsp90 confirmed iron binding by Hsp90.	Iron	59-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
14976405-5	2004	The iron-binding assay with purified human Hsp90 confirmed iron binding by Hsp90.	Iron	59-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
14976405-6	2004	Thus we suggest that Hsp90 is an iron-binding protein associated with the plasma membrane.	Iron	33-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
15491060-5	2004	An indirect immunoperoxidase method was applied using polyclonal antibodies against HSP70 and HSP90 on formalin-fixed paraffin-embedded tissues.	Formaldehyde	103-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15491060-5	2004	An indirect immunoperoxidase method was applied using polyclonal antibodies against HSP70 and HSP90 on formalin-fixed paraffin-embedded tissues.	Paraffin	118-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
14740253-7	2004	It summarizes the current knowledge in the field, including the ATP-dependent regulation of the Hsp70/Hsp90 multichaperone cycle and elucidates the complex interplay and their synergistic interaction.	Adenosine Triphosphate	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
14557268-4	2003	GRK2 interaction with Hsp90 was confirmed by co-immunoprecipitation and was effectively disrupted by geldanamycin, an Hsp90-specific inhibitor.	geldanamycin	101-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
14668798-4	2003	Treatment of cells with either geldanamycin or novobiocin, two pharmacological inhibitors of Hsp90 causes the destabilization of LKB1.	geldanamycin	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
14570880-3	2003	Consistent with Chk1 being an Hsp90 client, we also found that Chk1 but not Chk2 is destabilized in cells treated with the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	139-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
14570880-3	2003	Consistent with Chk1 being an Hsp90 client, we also found that Chk1 but not Chk2 is destabilized in cells treated with the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	139-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
14570880-3	2003	Consistent with Chk1 being an Hsp90 client, we also found that Chk1 but not Chk2 is destabilized in cells treated with the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	179-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
14695217-1	2003	Ansamycin antibiotics inhibit function of the heat shock protein (HSP) 90, causing selective degradation of several intracellular proteins regulating such processes as proliferation, cell cycle regulation, and prosurvival signaling cascades.	Rifabutin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-73
14695217-3	2003	Therefore, we hypothesized that the ansamycin geldanamycin and its 17-allylamino-17-demethoxy analog (17-AAG), which inhibit HSP90, would enhance tumor cell susceptibility to the cytotoxicity of IR.	Rifabutin	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
14695217-3	2003	Therefore, we hypothesized that the ansamycin geldanamycin and its 17-allylamino-17-demethoxy analog (17-AAG), which inhibit HSP90, would enhance tumor cell susceptibility to the cytotoxicity of IR.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
14695217-3	2003	Therefore, we hypothesized that the ansamycin geldanamycin and its 17-allylamino-17-demethoxy analog (17-AAG), which inhibit HSP90, would enhance tumor cell susceptibility to the cytotoxicity of IR.	17-allylamino-17-demethoxy	67-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
14695217-3	2003	Therefore, we hypothesized that the ansamycin geldanamycin and its 17-allylamino-17-demethoxy analog (17-AAG), which inhibit HSP90, would enhance tumor cell susceptibility to the cytotoxicity of IR.	tanespimycin	102-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
14668798-4	2003	Treatment of cells with either geldanamycin or novobiocin, two pharmacological inhibitors of Hsp90 causes the destabilization of LKB1.	Novobiocin	47-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
14668798-6	2003	In addition, we found that a LKB1 point mutation identified in a sporadic testicular cancer, weakens the interaction of LKB1 with both Hsp90 and Cdc37/p50 and enhances its sensitivity to the destabilizing effect of geldanamycin.	geldanamycin	215-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
14668798-8	2003	Furthermore, these data draw attention to the possible adverse consequences of antitumor drugs that target Hsp90, such as antibiotics related to geldanamycin, which could disrupt LKB1 function and promote the development of polyps and carcinomatous lesions.	geldanamycin	145-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
12890735-4	2003	We used cross-immunoprecipitation experiments to confirm the tyrosine phosphorylation of HSP-86, a process that is not inhibited by the ansamycin antibiotic, geldanamycin.	geldanamycin	158-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-95
12890735-5	2003	The general significance of these findings was confirmed by studies in which HSP-90 was also found to be tyrosine phosphorylated in human and rat spermatozoa when incubated under conditions that support capacitation.	Tyrosine	105-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-83
14678981-2	2003	We show in tumor cells that hypericin targets the heat shock protein (Hsp) 90 chaperone but not Hsp70 (Hsc70) to enhanced ubiquitinylation.	hypericin	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-77
14679005-1	2003	Interactions between the histone deacetylase inhibitors (HDACIs) suberoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino-17-demethoxygeldanamycin (17-AAG) have been examined in human leukemia cells (U937).	Vorinostat	65-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
14679005-1	2003	Interactions between the histone deacetylase inhibitors (HDACIs) suberoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino-17-demethoxygeldanamycin (17-AAG) have been examined in human leukemia cells (U937).	Vorinostat	98-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
14679005-1	2003	Interactions between the histone deacetylase inhibitors (HDACIs) suberoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino-17-demethoxygeldanamycin (17-AAG) have been examined in human leukemia cells (U937).	Butyric Acid	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
14679005-1	2003	Interactions between the histone deacetylase inhibitors (HDACIs) suberoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino-17-demethoxygeldanamycin (17-AAG) have been examined in human leukemia cells (U937).	tanespimycin	176-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
14679005-1	2003	Interactions between the histone deacetylase inhibitors (HDACIs) suberoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino-17-demethoxygeldanamycin (17-AAG) have been examined in human leukemia cells (U937).	tanespimycin	216-222	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
14679005-9	2003	Together, these findings indicate that coadministration of SAHA or SB with the Hsp90 antagonist 17-AAG in human leukemia cells leads to multiple perturbations in signaling, cell cycle, and survival pathways that culminate in mitochondrial injury and apoptosis.	Vorinostat	59-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
14679005-9	2003	Together, these findings indicate that coadministration of SAHA or SB with the Hsp90 antagonist 17-AAG in human leukemia cells leads to multiple perturbations in signaling, cell cycle, and survival pathways that culminate in mitochondrial injury and apoptosis.	Butyric Acid	67-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
14679005-9	2003	Together, these findings indicate that coadministration of SAHA or SB with the Hsp90 antagonist 17-AAG in human leukemia cells leads to multiple perturbations in signaling, cell cycle, and survival pathways that culminate in mitochondrial injury and apoptosis.	tanespimycin	96-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
14713575-0	2003	Geldanamycin, an inhibitor of Hsp90, sensitizes human tumour cells to radiation.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
14713575-1	2003	PURPOSE: The effects of the heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA) were examined on the radiosensitivity and signal transduction pathways in human tumour cell lines.	geldanamycin	68-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
14713575-9	2003	CONCLUSION: Targeting Hsp90 with GA provides a promising experimental strategy for radiosensitization of carcinoma.	geldanamycin	33-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
14580201-5	2003	The Hsp90 antagonist molybdate was necessary to stabilize the interactions between isolated subdomains and Hsp90 or Cdc37, but the presence of both lobes of the kinases" catalytic domain generated a stable salt-resistant chaperone-client heterocomplex.	molybdate	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
12970348-3	2003	GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
12970348-5	2003	The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members.	Adenosine-5'-(N-ethylcarboxamide)	125-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-262
12970348-5	2003	The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members.	2-Chloro-2',3'-dideoxyadenosine	169-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-262
14580201-5	2003	The Hsp90 antagonist molybdate was necessary to stabilize the interactions between isolated subdomains and Hsp90 or Cdc37, but the presence of both lobes of the kinases" catalytic domain generated a stable salt-resistant chaperone-client heterocomplex.	molybdate	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
14596612-8	2003	Mutation of arginine residues in NPY13-36 to alanine abrogated binding to Hsp90.	Arginine	12-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
14596612-8	2003	Mutation of arginine residues in NPY13-36 to alanine abrogated binding to Hsp90.	Alanine	45-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
14600095-0	2003	Magnetic resonance spectroscopic pharmacodynamic markers of the heat shock protein 90 inhibitor 17-allylamino,17-demethoxygeldanamycin (17AAG) in human colon cancer models.	17-allylamino	96-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
14600095-0	2003	Magnetic resonance spectroscopic pharmacodynamic markers of the heat shock protein 90 inhibitor 17-allylamino,17-demethoxygeldanamycin (17AAG) in human colon cancer models.	17-demethoxygeldanamycin	110-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
14600095-1	2003	BACKGROUND: 17-allylamino,17-demethoxygeldanamycin (17AAG) is a novel anticancer drug that inhibits heat shock protein 90 (Hsp90), resulting in proteasomal degradation of several oncogenic proteins.	17-allylamino	12-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-121
14600095-1	2003	BACKGROUND: 17-allylamino,17-demethoxygeldanamycin (17AAG) is a novel anticancer drug that inhibits heat shock protein 90 (Hsp90), resulting in proteasomal degradation of several oncogenic proteins.	17-allylamino	12-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
14600095-1	2003	BACKGROUND: 17-allylamino,17-demethoxygeldanamycin (17AAG) is a novel anticancer drug that inhibits heat shock protein 90 (Hsp90), resulting in proteasomal degradation of several oncogenic proteins.	17-demethoxygeldanamycin	26-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-121
14600095-1	2003	BACKGROUND: 17-allylamino,17-demethoxygeldanamycin (17AAG) is a novel anticancer drug that inhibits heat shock protein 90 (Hsp90), resulting in proteasomal degradation of several oncogenic proteins.	17-demethoxygeldanamycin	26-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
14600095-1	2003	BACKGROUND: 17-allylamino,17-demethoxygeldanamycin (17AAG) is a novel anticancer drug that inhibits heat shock protein 90 (Hsp90), resulting in proteasomal degradation of several oncogenic proteins.	tanespimycin	52-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-121
14600095-1	2003	BACKGROUND: 17-allylamino,17-demethoxygeldanamycin (17AAG) is a novel anticancer drug that inhibits heat shock protein 90 (Hsp90), resulting in proteasomal degradation of several oncogenic proteins.	tanespimycin	52-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
14600095-12	2003	CONCLUSIONS: Inhibition of Hsp90 by 17AAG resulted in altered phospholipid metabolism in cultured tumor cells and in tumor xenografts.	tanespimycin	36-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
14600095-12	2003	CONCLUSIONS: Inhibition of Hsp90 by 17AAG resulted in altered phospholipid metabolism in cultured tumor cells and in tumor xenografts.	Phospholipids	62-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
14600095-13	2003	The increases observed in phosphocholine and phosphomonoester levels suggest that these metabolites may have the potential to act as noninvasive pharmacodynamic markers for analyzing tumor response to treatment with 17AAG or other Hsp90 inhibitors.	Phosphorylcholine	26-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-236
14624223-3	2003	One Hsp90 inhibitor, 17-AAG, has completed Phase I clinical trial, and several Phase II trials are in progress.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
14580201-7	2003	Cyp40 was a salt labile component of Hsp90 complexes formed with the full-length, catalytic domains, and N-terminal catalytic lobes of Lck and HRI.	Salts	12-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
14535799-6	2003	Other known oxidants gave an unusual azaquinone product 49. o-Quino-GA 55 binds Hsp90 with good affinity but is less cytotoxic compared to GA.	Gangamicin	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
12890735-0	2003	Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation.	Tyrosine	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-34
12890735-4	2003	We used cross-immunoprecipitation experiments to confirm the tyrosine phosphorylation of HSP-86, a process that is not inhibited by the ansamycin antibiotic, geldanamycin.	Tyrosine	61-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-95
12890735-4	2003	We used cross-immunoprecipitation experiments to confirm the tyrosine phosphorylation of HSP-86, a process that is not inhibited by the ansamycin antibiotic, geldanamycin.	Rifabutin	136-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-95
12709419-1	2003	ERBB2 increases the sensitivity of breast cancer cells to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	78-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
14578462-4	2003	LAQ824 also induced the acetylation of heat shock protein (hsp) 90, resulting in inhibition of its binding to ATP, which has been shown to impair the chaperone association of hsp 90 with its client proteins, Her-2, AKT, and c-Raf-1.	LAQ824	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-66
14578462-4	2003	LAQ824 also induced the acetylation of heat shock protein (hsp) 90, resulting in inhibition of its binding to ATP, which has been shown to impair the chaperone association of hsp 90 with its client proteins, Her-2, AKT, and c-Raf-1.	LAQ824	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-181
14578462-4	2003	LAQ824 also induced the acetylation of heat shock protein (hsp) 90, resulting in inhibition of its binding to ATP, which has been shown to impair the chaperone association of hsp 90 with its client proteins, Her-2, AKT, and c-Raf-1.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-66
14578462-4	2003	LAQ824 also induced the acetylation of heat shock protein (hsp) 90, resulting in inhibition of its binding to ATP, which has been shown to impair the chaperone association of hsp 90 with its client proteins, Her-2, AKT, and c-Raf-1.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-181
14578462-5	2003	Consistent with this, treatment with LAQ824 shifted the binding of Her-2 from hsp 90 to hsp 70, promoting proteasomal degradation of Her-2.	LAQ824	37-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-84
12869560-0	2003	Tyrosine phosphorylation of HSP90 within the P2X7 receptor complex negatively regulates P2X7 receptors.	Tyrosine	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
12869560-4	2003	We found that HSP90 was tyrosine-phosphorylated in association with the P2X7 receptor complex, but not in the cytosolic compartment.	Tyrosine	24-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12869560-5	2003	The HSP90 inhibitor geldanamycin decreased tyrosine phosphorylation of HSP90 and produced a 2-fold increase in the sensitivity of P2X7 receptors to agonist.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
12869560-5	2003	The HSP90 inhibitor geldanamycin decreased tyrosine phosphorylation of HSP90 and produced a 2-fold increase in the sensitivity of P2X7 receptors to agonist.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
12869560-5	2003	The HSP90 inhibitor geldanamycin decreased tyrosine phosphorylation of HSP90 and produced a 2-fold increase in the sensitivity of P2X7 receptors to agonist.	Tyrosine	43-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
12869560-5	2003	The HSP90 inhibitor geldanamycin decreased tyrosine phosphorylation of HSP90 and produced a 2-fold increase in the sensitivity of P2X7 receptors to agonist.	Tyrosine	43-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
12869560-8	2003	We conclude that selective tyrosine phosphorylation of P2X7 receptor-associated HSP90 may act as a negative regulator of P2X7 receptor complex formation and function.	Tyrosine	27-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
12941337-1	2003	Quinoline-5,8-dione-based compounds were designed from the structure of the geldanamycin-bound Hsp-90 active site.	6-amino-7-chloro-5,8-dioxoquinoline	0-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-101
12941337-1	2003	Quinoline-5,8-dione-based compounds were designed from the structure of the geldanamycin-bound Hsp-90 active site.	geldanamycin	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-101
12904022-1	2003	A new facile synthesis has been developed for nanomolar Hsp90 inhibitor, cycloproparadicicol (2).	cycloproparadicicol	73-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
12811834-3	2003	Geldanamycin (GA), a benzoquinone ansamycin antibiotic, binds to heat shock protein 90 (Hsp90) and interferes with its function.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-86
12811834-3	2003	Geldanamycin (GA), a benzoquinone ansamycin antibiotic, binds to heat shock protein 90 (Hsp90) and interferes with its function.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
12811834-3	2003	Geldanamycin (GA), a benzoquinone ansamycin antibiotic, binds to heat shock protein 90 (Hsp90) and interferes with its function.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-86
12811834-3	2003	Geldanamycin (GA), a benzoquinone ansamycin antibiotic, binds to heat shock protein 90 (Hsp90) and interferes with its function.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
12811834-3	2003	Geldanamycin (GA), a benzoquinone ansamycin antibiotic, binds to heat shock protein 90 (Hsp90) and interferes with its function.	benzoquinone ansamycin	21-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
12930845-0	2003	Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.	Serine	19-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
12930845-4	2003	Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle.	Serine	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
12930845-4	2003	Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle.	Serine	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
12930845-4	2003	Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle.	Glutamic Acid	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
12930845-4	2003	Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle.	Glutamic Acid	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
12930845-4	2003	Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle.	Adenosine Triphosphate	182-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
12930845-4	2003	Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle.	Adenosine Triphosphate	182-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
14555522-2	2003	EXPERIMENTAL DESIGN: The effects of the Hsp90-inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) on cell growth, expression of signal transduction kinases, apoptosis, FLT3 phosphorylation and interaction with Hsp90 was determined in FLT3(+) human leukemias.	tanespimycin	56-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
14555522-2	2003	EXPERIMENTAL DESIGN: The effects of the Hsp90-inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) on cell growth, expression of signal transduction kinases, apoptosis, FLT3 phosphorylation and interaction with Hsp90 was determined in FLT3(+) human leukemias.	tanespimycin	96-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
14555522-4	2003	17-AAG inhibited FLT3 phosphorylation and interaction with Hsp90.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
14555522-5	2003	FLT3(+) leukemias were significantly more sensitive to the Hsp90 inhibitors 17-AAG and Herbimycin A in cell growth assays than FLT3-negative leukemias.	tanespimycin	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
14555522-5	2003	FLT3(+) leukemias were significantly more sensitive to the Hsp90 inhibitors 17-AAG and Herbimycin A in cell growth assays than FLT3-negative leukemias.	herbimycin	87-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
14529382-6	2003	The "druggability" of Hsp90 was confirmed by the discovery that the natural products geldanamycin and radicicol, which have anticancer activity, exert their biological effects by inhibiting the essential ATPase activity associated with the N-terminal domain of the protein.	geldanamycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
14529382-6	2003	The "druggability" of Hsp90 was confirmed by the discovery that the natural products geldanamycin and radicicol, which have anticancer activity, exert their biological effects by inhibiting the essential ATPase activity associated with the N-terminal domain of the protein.	monorden	102-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
14529383-2	2003	The structure determination of the N-terminal domain of Hsp90/Hsp90beta, proof that it is an ATPase, that this activity is regulated and the identification of co-chaperones that facilitate Hsp90 function were landmarks towards understanding conformational changes in Hsp90 brought about by ATP, co-chaperones and client proteins.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
14529383-2	2003	The structure determination of the N-terminal domain of Hsp90/Hsp90beta, proof that it is an ATPase, that this activity is regulated and the identification of co-chaperones that facilitate Hsp90 function were landmarks towards understanding conformational changes in Hsp90 brought about by ATP, co-chaperones and client proteins.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
14529383-2	2003	The structure determination of the N-terminal domain of Hsp90/Hsp90beta, proof that it is an ATPase, that this activity is regulated and the identification of co-chaperones that facilitate Hsp90 function were landmarks towards understanding conformational changes in Hsp90 brought about by ATP, co-chaperones and client proteins.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
14529383-5	2003	The structure determination of the middle region of Hsp90 has shed further light on the complex ATP-cycle of Hsp90, identifying a catalytic loop, with key residues that are essential for ATP hydrolysis.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
14529383-5	2003	The structure determination of the middle region of Hsp90 has shed further light on the complex ATP-cycle of Hsp90, identifying a catalytic loop, with key residues that are essential for ATP hydrolysis.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
14529383-5	2003	The structure determination of the middle region of Hsp90 has shed further light on the complex ATP-cycle of Hsp90, identifying a catalytic loop, with key residues that are essential for ATP hydrolysis.	Adenosine Triphosphate	187-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
14529383-5	2003	The structure determination of the middle region of Hsp90 has shed further light on the complex ATP-cycle of Hsp90, identifying a catalytic loop, with key residues that are essential for ATP hydrolysis.	Adenosine Triphosphate	187-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
14529383-6	2003	These studies, together with biochemical ones, suggest that ATP hydrolysis, is dependent on a complex rate-limiting step, involving N-terminal dimerization and association of the middle region, and therefore the catalytic loop, of Hsp90 with the N-terminal domains.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-236
14529384-1	2003	The currently used Hsp90 inhibitors, geldanamycin, herbimycin A and radicicol, were isolated many years ago from Streptomyces and fungi originally for their antiprotozoal activity, herbicidal activity and antifungal activity, respectively.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
14529384-1	2003	The currently used Hsp90 inhibitors, geldanamycin, herbimycin A and radicicol, were isolated many years ago from Streptomyces and fungi originally for their antiprotozoal activity, herbicidal activity and antifungal activity, respectively.	herbimycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
14529384-1	2003	The currently used Hsp90 inhibitors, geldanamycin, herbimycin A and radicicol, were isolated many years ago from Streptomyces and fungi originally for their antiprotozoal activity, herbicidal activity and antifungal activity, respectively.	monorden	68-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
14529384-3	2003	In 1994, these ansamycins were found to bind to Hsp90 and to cause the degradation of client proteins including Src kinases; further efforts to develop anticancer drugs were made using geldanamycin analogs, and 17AAG was chosen as the best candidate for clinical trials.	Lactams, Macrocyclic	15-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
14529384-3	2003	In 1994, these ansamycins were found to bind to Hsp90 and to cause the degradation of client proteins including Src kinases; further efforts to develop anticancer drugs were made using geldanamycin analogs, and 17AAG was chosen as the best candidate for clinical trials.	tanespimycin	211-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
14529385-1	2003	HSP90 inhibitors such as 17AAG have the major therapeutic advantage that they exert downstream inhibitory effects on multiple oncogenic client proteins.	tanespimycin	25-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14529387-3	2003	In a study of mechanisms of action, it was revealed that radicicol depletes the Hsp90 client signaling molecules in cells, and thus inhibit the signal transduction pathway.	monorden	57-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
14529387-4	2003	In addition, direct binding of radicicol to the N-terminal ATP/ADP binding site of Hsp90 was shown, and thus radicicol has been recognized as a structurally unique antibiotic that binds and inhibits the molecular chaperone Hsp90.	monorden	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
14529387-4	2003	In addition, direct binding of radicicol to the N-terminal ATP/ADP binding site of Hsp90 was shown, and thus radicicol has been recognized as a structurally unique antibiotic that binds and inhibits the molecular chaperone Hsp90.	monorden	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
14529387-4	2003	In addition, direct binding of radicicol to the N-terminal ATP/ADP binding site of Hsp90 was shown, and thus radicicol has been recognized as a structurally unique antibiotic that binds and inhibits the molecular chaperone Hsp90.	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
14529387-4	2003	In addition, direct binding of radicicol to the N-terminal ATP/ADP binding site of Hsp90 was shown, and thus radicicol has been recognized as a structurally unique antibiotic that binds and inhibits the molecular chaperone Hsp90.	Adenosine Diphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
14529387-4	2003	In addition, direct binding of radicicol to the N-terminal ATP/ADP binding site of Hsp90 was shown, and thus radicicol has been recognized as a structurally unique antibiotic that binds and inhibits the molecular chaperone Hsp90.	monorden	109-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
14529387-4	2003	In addition, direct binding of radicicol to the N-terminal ATP/ADP binding site of Hsp90 was shown, and thus radicicol has been recognized as a structurally unique antibiotic that binds and inhibits the molecular chaperone Hsp90.	monorden	109-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
14529387-6	2003	Hsp90 client proteins were depleted and apoptosis was induced in the tumor specimen treated with radicicol oxime derivatives.	radicicol oxime	97-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
14529387-7	2003	Taken together, these results suggest that the antitumor activity of radicicol oxime derivatives is mediated by binding to Hsp90 and destabilization of Hsp90 client proteins in the tumor.	radicicol oxime	69-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
14529387-7	2003	Taken together, these results suggest that the antitumor activity of radicicol oxime derivatives is mediated by binding to Hsp90 and destabilization of Hsp90 client proteins in the tumor.	radicicol oxime	69-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
14529388-0	2003	Development of purine-scaffold small molecule inhibitors of Hsp90.	purine	15-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
14529388-3	2003	The ansamycins (geldanamycin and herbimycin) and the unrelated natural product radicicol were found to bind to the N-terminal pocket of Hsp90 and inhibit its function.	Lactams, Macrocyclic	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
14529388-3	2003	The ansamycins (geldanamycin and herbimycin) and the unrelated natural product radicicol were found to bind to the N-terminal pocket of Hsp90 and inhibit its function.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
14529388-3	2003	The ansamycins (geldanamycin and herbimycin) and the unrelated natural product radicicol were found to bind to the N-terminal pocket of Hsp90 and inhibit its function.	herbimycin	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
14529388-3	2003	The ansamycins (geldanamycin and herbimycin) and the unrelated natural product radicicol were found to bind to the N-terminal pocket of Hsp90 and inhibit its function.	monorden	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
14529388-9	2003	Here we present an overview of such efforts with focus on a new class of purine-scaffold Hsp90 inhibitors developed by rational design.	purine	73-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
14529389-1	2003	17-allylamino, 17-demethoxygeldanamycin (17AAG; NSC 330507) is the first modulator of heat shock protein 90 (Hsp90) to enter clinical trials.	17-allylamino	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-107
14529389-1	2003	17-allylamino, 17-demethoxygeldanamycin (17AAG; NSC 330507) is the first modulator of heat shock protein 90 (Hsp90) to enter clinical trials.	17-allylamino	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
14529389-1	2003	17-allylamino, 17-demethoxygeldanamycin (17AAG; NSC 330507) is the first modulator of heat shock protein 90 (Hsp90) to enter clinical trials.	17-demethoxygeldanamycin	15-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-107
14529389-1	2003	17-allylamino, 17-demethoxygeldanamycin (17AAG; NSC 330507) is the first modulator of heat shock protein 90 (Hsp90) to enter clinical trials.	17-demethoxygeldanamycin	15-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
14529389-1	2003	17-allylamino, 17-demethoxygeldanamycin (17AAG; NSC 330507) is the first modulator of heat shock protein 90 (Hsp90) to enter clinical trials.	tanespimycin	41-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-107
14529389-1	2003	17-allylamino, 17-demethoxygeldanamycin (17AAG; NSC 330507) is the first modulator of heat shock protein 90 (Hsp90) to enter clinical trials.	tanespimycin	41-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
14529390-6	2003	Phase I clinical studies with 17AAG have shown that the drug can be given at does that are well tolerated and that also achieve active pharmacokinetic exposures and elicit molecular signatures of gene and protein expression that are indicative of Hsp90 inhibition.	tanespimycin	30-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	247-252
12869591-0	2003	The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation.	Cisplatin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
12869591-2	2003	Cisplatin may also disrupt the function of some proteins, including heat shock protein 90 (Hsp90).	Cisplatin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
12869591-2	2003	Cisplatin may also disrupt the function of some proteins, including heat shock protein 90 (Hsp90).	Cisplatin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
12869591-8	2003	Immunoprecipitation revealed that cisplatin disrupts binding of GR to Hsp90.	Cisplatin	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
12869591-9	2003	Moreover, cisplatin-treated Hsp90 was unable to associate with untreated ligand binding domain of GR.	Cisplatin	10-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
14571418-7	2003	17-Allyamino-17-demethoxygeldanamycin (17-AAG) is an inhibitor of the Hsp90 chaperone protein.	17-allyamino-17-demethoxygeldanamycin	0-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
14986860-3	2003	Recent studies have proposed that the highly conserved chaperone Hsp90 could function as a "capacitor," or an "adaptively inducible canalizer," that masks silent phenotypic variation of either genetic or epigenetic origin.	capacitor	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
14559183-4	2003	The localized co-chaperones can harness the ATP-dependent mechanisms of Hsp70 and Hsp90 to do conformational work in diverse functional contexts, including vesicle secretion and recycling, protein transport and the regulated assembly and/or disassembly of protein complexes.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
12890756-6	2003	An inhibitor of Hsp90, geldanamycin, inhibited IKK"s kinase activity induced by vFLIP and killed PEL cells, suggesting that vFLIP activation of IKK contributes to PEL cell survival.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
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
12807878-2	2003	The first step in assembly is the ATP-dependent and hsp40 (YDJ-1)-dependent formation of a GR.hsp70 complex that primes the receptor for subsequent ATP-dependent activation by hsp90, Hop, and p23.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
12807878-2	2003	The first step in assembly is the ATP-dependent and hsp40 (YDJ-1)-dependent formation of a GR.hsp70 complex that primes the receptor for subsequent ATP-dependent activation by hsp90, Hop, and p23.	Adenosine Triphosphate	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
12842893-1	2003	Anti-Hsp90 ribozyme reveals a complex mechanism of Hsp90 inhibitors involving both superoxide- and Hsp90-dependent events.	Superoxides	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
12842893-1	2003	Anti-Hsp90 ribozyme reveals a complex mechanism of Hsp90 inhibitors involving both superoxide- and Hsp90-dependent events.	Superoxides	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
12842893-1	2003	Anti-Hsp90 ribozyme reveals a complex mechanism of Hsp90 inhibitors involving both superoxide- and Hsp90-dependent events.	Superoxides	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
12842893-4	2003	Inhibition of Hsp90 by geldanamycin, radicicol, cisplatin, and novobiocin induced a significant acceleration of detergent- and hypotonic shock-induced cell lysis.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12842893-4	2003	Inhibition of Hsp90 by geldanamycin, radicicol, cisplatin, and novobiocin induced a significant acceleration of detergent- and hypotonic shock-induced cell lysis.	monorden	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12842893-4	2003	Inhibition of Hsp90 by geldanamycin, radicicol, cisplatin, and novobiocin induced a significant acceleration of detergent- and hypotonic shock-induced cell lysis.	Cisplatin	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12842893-4	2003	Inhibition of Hsp90 by geldanamycin, radicicol, cisplatin, and novobiocin induced a significant acceleration of detergent- and hypotonic shock-induced cell lysis.	Novobiocin	63-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12842893-5	2003	The concentration and time dependence of cell lysis acceleration was in agreement with the Hsp90 inhibition characteristics of the N-terminal inhibitors, geldanamycin and radicicol.	geldanamycin	154-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
12842893-5	2003	The concentration and time dependence of cell lysis acceleration was in agreement with the Hsp90 inhibition characteristics of the N-terminal inhibitors, geldanamycin and radicicol.	monorden	171-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
12964162-0	2003	NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.	Adenosine Diphosphate	88-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12964162-0	2003	NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.	Adenylyl Imidodiphosphate	93-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12964162-0	2003	NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.	geldanamycin	102-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12964162-0	2003	NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.	monorden	120-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12964162-4	2003	Analysis of (1)H,(15)N correlation spectra showed a specific pattern of chemical shift perturbations at N210 (ATP binding domain of Hsp90, residues 1-210) upon ligand binding.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
12803546-0	2003	Hsp90 is a direct target of the anti-allergic drugs disodium cromoglycate and amlexanox.	Cromolyn Sodium	52-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12803546-0	2003	Hsp90 is a direct target of the anti-allergic drugs disodium cromoglycate and amlexanox.	amlexanox	78-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12803546-3	2003	In an effort to discover Hsp90 antagonists, we screened many drugs and found that the anti-allergic drugs DSCG (disodium cromoglycate) and amlexanox target Hsp90.	Cromolyn Sodium	106-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
12803546-3	2003	In an effort to discover Hsp90 antagonists, we screened many drugs and found that the anti-allergic drugs DSCG (disodium cromoglycate) and amlexanox target Hsp90.	Cromolyn Sodium	106-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
12803546-3	2003	In an effort to discover Hsp90 antagonists, we screened many drugs and found that the anti-allergic drugs DSCG (disodium cromoglycate) and amlexanox target Hsp90.	Cromolyn Sodium	112-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
12803546-3	2003	In an effort to discover Hsp90 antagonists, we screened many drugs and found that the anti-allergic drugs DSCG (disodium cromoglycate) and amlexanox target Hsp90.	Cromolyn Sodium	112-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
12803546-3	2003	In an effort to discover Hsp90 antagonists, we screened many drugs and found that the anti-allergic drugs DSCG (disodium cromoglycate) and amlexanox target Hsp90.	amlexanox	139-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
12803546-3	2003	In an effort to discover Hsp90 antagonists, we screened many drugs and found that the anti-allergic drugs DSCG (disodium cromoglycate) and amlexanox target Hsp90.	amlexanox	139-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
12803546-6	2003	Amlexanox suppressed C-terminal chaperone activity in vitro, but not N-terminal chaperone activity, and inhibited the association of cohort proteins, such as cyclophilin 40 and Hsp-organizing protein, to the C-terminal domain of Hsp90.	amlexanox	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	229-234
12803546-10	2003	DSCG and amlexanox may serve as useful tools for evaluating the physiological significance of Hsp90.	Cromolyn Sodium	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
12803546-10	2003	DSCG and amlexanox may serve as useful tools for evaluating the physiological significance of Hsp90.	amlexanox	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
12881371-3	2003	It represents a class of drugs, the benzoquinone ansamycin antibiotics, capable of binding and disrupting the function of Hsp90, leading to the depletion of multiple oncogenic client proteins.	benzoquinone ansamycin	36-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
12750378-3	2003	This process can be driven by geldanamycin, an irreversible blocker of Hsp90.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
12821470-2	2003	Antibody to HSP90 is closely associated with recovery in patients with invasive candidiasis who are receiving amphotericin B (AMB).	Amphotericin B	110-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
12821470-2	2003	Antibody to HSP90 is closely associated with recovery in patients with invasive candidiasis who are receiving amphotericin B (AMB).	Amphotericin B	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
12623837-1	2003	17-allylamino-demethoxy geldanamycin (17-AAG) inhibits the chaperone function of heat shock protein-90 (Hsp-90) and promotes the proteasomal degradation of its misfolded client proteins.	17-allylamino-demethoxy geldanamycin	0-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-102
12623837-1	2003	17-allylamino-demethoxy geldanamycin (17-AAG) inhibits the chaperone function of heat shock protein-90 (Hsp-90) and promotes the proteasomal degradation of its misfolded client proteins.	17-allylamino-demethoxy geldanamycin	0-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-110
12819933-12	2003	The first-in-class HSP90 inhibitor 17AAG exhibited good activity in animal models and is now showing evidence of molecular and clinical activity in ongoing clinical trials.	tanespimycin	35-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
12843186-0	2003	The heat shock protein 90-binding geldanamycin inhibits cancer cell proliferation, down-regulates oncoproteins, and inhibits epidermal growth factor-induced invasion in thyroid cancer cell lines.	geldanamycin	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
12843186-2	2003	Geldanamycin, a specific inhibitor of HSP90, is cytotoxic to several human cancer cell lines, but its effect in thyroid cancer is unknown.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
12775586-5	2003	The specific Hsp90 inhibitor geldanamycin prevents maturation and increases proteasomal degradation of hERG WT, while reducing hERG currents in heterologous expression systems.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
12724357-5	2003	In fact, our data show that incubation of PTHrP [67-86]-amide-treated cells with either antisense hsbp1-oligonucleotide or geldanamycin, an hsp90-inactivating antibiotic, results in downregulation of uPa and upregulation of MMP-1, and in a prominent inhibition of cell invasion in matrigel-containing Transwell chambers.	Amides	56-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
12724357-5	2003	In fact, our data show that incubation of PTHrP [67-86]-amide-treated cells with either antisense hsbp1-oligonucleotide or geldanamycin, an hsp90-inactivating antibiotic, results in downregulation of uPa and upregulation of MMP-1, and in a prominent inhibition of cell invasion in matrigel-containing Transwell chambers.	Oligonucleotides	104-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
12724357-5	2003	In fact, our data show that incubation of PTHrP [67-86]-amide-treated cells with either antisense hsbp1-oligonucleotide or geldanamycin, an hsp90-inactivating antibiotic, results in downregulation of uPa and upregulation of MMP-1, and in a prominent inhibition of cell invasion in matrigel-containing Transwell chambers.	geldanamycin	123-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
12729599-1	2003	A filter binding assay to measure affinity of [3H-allyl]17-allylamino geldanamycin ([3H]AAG) for the ATP binding site of the N-terminal domain of human Hsp90alpha (hHsp90alpha9-236) was developed.	[3h-allyl]17-allylamino geldanamycin	46-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-162
12729599-1	2003	A filter binding assay to measure affinity of [3H-allyl]17-allylamino geldanamycin ([3H]AAG) for the ATP binding site of the N-terminal domain of human Hsp90alpha (hHsp90alpha9-236) was developed.	[3h]aag	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-162
12729599-1	2003	A filter binding assay to measure affinity of [3H-allyl]17-allylamino geldanamycin ([3H]AAG) for the ATP binding site of the N-terminal domain of human Hsp90alpha (hHsp90alpha9-236) was developed.	Adenosine Triphosphate	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-162
12729599-2	2003	Diethylaminoethyl cellulose or glass fiber filters impregnated with polyethyleneimine were used to capture the [3H]AAG-Hsp90 complex, and conditions which washed >98% of free [3H]AAG from the filters were developed.	DEAE-Cellulose	0-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
12729599-2	2003	Diethylaminoethyl cellulose or glass fiber filters impregnated with polyethyleneimine were used to capture the [3H]AAG-Hsp90 complex, and conditions which washed >98% of free [3H]AAG from the filters were developed.	aziridine	68-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
12729599-2	2003	Diethylaminoethyl cellulose or glass fiber filters impregnated with polyethyleneimine were used to capture the [3H]AAG-Hsp90 complex, and conditions which washed >98% of free [3H]AAG from the filters were developed.	Tritium	112-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
12729599-2	2003	Diethylaminoethyl cellulose or glass fiber filters impregnated with polyethyleneimine were used to capture the [3H]AAG-Hsp90 complex, and conditions which washed >98% of free [3H]AAG from the filters were developed.	Adenosine Diphosphate Glucose	115-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
12729599-5	2003	[3H]AAG had similar affinities for full-length hHsp90alpha and for hHsp90alpha9-236 variants containing biotinylated N-terminal biotinylation signal sequences and N- or C-terminal His(6) tags.	Tritium	1-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-58
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	Adenosine Diphosphate	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	monorden	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	Tritium	98-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12729599-6	2003	Geldanamycin, ADP, ATP, and radicicol-all known to bind to the ATP domain of Hsp90-competed with [3H]AAG for binding to hHsp90alpha9-236, showing K(d) values in good agreement with reported values.	Adenosine Diphosphate Glucose	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
12755697-0	2003	Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
12755697-0	2003	Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site.	Adenosine Triphosphate	140-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
12755697-1	2003	The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that assists both in ATP-independent sequestration of damaged proteins, and in ATP-dependent folding of numerous targets, such as nuclear hormone receptors and protein kinases.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
12755697-1	2003	The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that assists both in ATP-independent sequestration of damaged proteins, and in ATP-dependent folding of numerous targets, such as nuclear hormone receptors and protein kinases.	Adenosine Triphosphate	142-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
12755697-12	2003	Our data provide additional evidence for the dynamic domain-domain interactions of Hsp90, give hints for the design of novel types of specific Hsp90 inhibitors, and raise the possibility that besides ATP, other small molecules might also interact with the C-terminal nucleotide binding site in vivo.	Adenosine Triphosphate	200-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
12755697-12	2003	Our data provide additional evidence for the dynamic domain-domain interactions of Hsp90, give hints for the design of novel types of specific Hsp90 inhibitors, and raise the possibility that besides ATP, other small molecules might also interact with the C-terminal nucleotide binding site in vivo.	Adenosine Triphosphate	200-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
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
12591925-3	2003	Mutation of serines 116 and 617 to alanine promoted a greater protein-protein interaction with hsp90 and Akt and greater phosphorylation on serine 1179, the major site for Akt phosphorylation.	Serine	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
14627195-2	2003	It appears to facilitate the adenosine triphosphate-driven cycle of Hsp90 binding to client proteins.	Adenosine Triphosphate	29-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
12727831-3	2003	17-allylamino-17-demethoxygeldanamycin (17-AGG) is an Hsp90 inhibitor currently in Phase I clinical trial.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
12727831-3	2003	17-allylamino-17-demethoxygeldanamycin (17-AGG) is an Hsp90 inhibitor currently in Phase I clinical trial.	17-agg	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
12678776-6	2003	Benzoquinone ansamycin binding to Hsp90 led to the identification of radicicol as an additional Hsp90 inhibitor.	benzoquinone ansamycin	0-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
12678776-6	2003	Benzoquinone ansamycin binding to Hsp90 led to the identification of radicicol as an additional Hsp90 inhibitor.	benzoquinone ansamycin	0-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
12678776-6	2003	Benzoquinone ansamycin binding to Hsp90 led to the identification of radicicol as an additional Hsp90 inhibitor.	monorden	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
12678776-6	2003	Benzoquinone ansamycin binding to Hsp90 led to the identification of radicicol as an additional Hsp90 inhibitor.	monorden	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
12678776-7	2003	Additional target-based screening uncovered novobiocin as a third structurally distinct small molecule with Hsp90 inhibitory properties.	Novobiocin	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
12853476-5	2003	Furthermore, unlike other co-chaperones, Tpr2 induces ATP-independent dissociation of Hsp90 but not of Hsp70 from chaperone-substrate complexes.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
12771028-1	2003	As it has been demonstrated that the heat shock protein 90 (HSP90) is required for the assembly and activation of telomerase in human cells, we investigated the effect exerted by the ansamycin antibiotics geldanamycin (GA) and 17-allylamino,17-demethoxygeldanamycin (17-AAG), two well-known inhibitors of the HSP90 chaperone function, on telomerase activity in JR8 human melanoma cells.	Rifabutin	183-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
12771028-1	2003	As it has been demonstrated that the heat shock protein 90 (HSP90) is required for the assembly and activation of telomerase in human cells, we investigated the effect exerted by the ansamycin antibiotics geldanamycin (GA) and 17-allylamino,17-demethoxygeldanamycin (17-AAG), two well-known inhibitors of the HSP90 chaperone function, on telomerase activity in JR8 human melanoma cells.	17-demethoxygeldanamycin	241-265	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-58
12771028-1	2003	As it has been demonstrated that the heat shock protein 90 (HSP90) is required for the assembly and activation of telomerase in human cells, we investigated the effect exerted by the ansamycin antibiotics geldanamycin (GA) and 17-allylamino,17-demethoxygeldanamycin (17-AAG), two well-known inhibitors of the HSP90 chaperone function, on telomerase activity in JR8 human melanoma cells.	17-demethoxygeldanamycin	241-265	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
12771028-1	2003	As it has been demonstrated that the heat shock protein 90 (HSP90) is required for the assembly and activation of telomerase in human cells, we investigated the effect exerted by the ansamycin antibiotics geldanamycin (GA) and 17-allylamino,17-demethoxygeldanamycin (17-AAG), two well-known inhibitors of the HSP90 chaperone function, on telomerase activity in JR8 human melanoma cells.	tanespimycin	267-273	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-58
12771028-1	2003	As it has been demonstrated that the heat shock protein 90 (HSP90) is required for the assembly and activation of telomerase in human cells, we investigated the effect exerted by the ansamycin antibiotics geldanamycin (GA) and 17-allylamino,17-demethoxygeldanamycin (17-AAG), two well-known inhibitors of the HSP90 chaperone function, on telomerase activity in JR8 human melanoma cells.	tanespimycin	267-273	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
12771028-3	2003	The results of TRAP (telomeric repeat amplification protocol) experiments carried out on HSP90 immunoprecipitates showed that exposure to 100 ng/ml GA and 17-AAG induced a significant (P < 0.01) inhibition of telomerase activity, which was observed at earlier time points than drug-induced inhibition of cell proliferation.	tanespimycin	155-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
12591925-3	2003	Mutation of serines 116 and 617 to alanine promoted a greater protein-protein interaction with hsp90 and Akt and greater phosphorylation on serine 1179, the major site for Akt phosphorylation.	Alanine	35-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
12591925-3	2003	Mutation of serines 116 and 617 to alanine promoted a greater protein-protein interaction with hsp90 and Akt and greater phosphorylation on serine 1179, the major site for Akt phosphorylation.	Serine	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
12684036-3	2003	Incubation of cPGES with Hsp90 resulted in a significant increase in PGES activity in vitro.	Prostaglandins E	15-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
12574167-4	2003	Hsp90 inhibitory ansamycin antibiotics such as geldanamycin (GA) induce rapid ubiquitinylation and down-regulation of ErbB2.	Rifabutin	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12574167-4	2003	Hsp90 inhibitory ansamycin antibiotics such as geldanamycin (GA) induce rapid ubiquitinylation and down-regulation of ErbB2.	geldanamycin	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12574167-4	2003	Hsp90 inhibitory ansamycin antibiotics such as geldanamycin (GA) induce rapid ubiquitinylation and down-regulation of ErbB2.	geldanamycin	61-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12574167-11	2003	Notably, CHIP H260Q induced a dramatic elevation of ErbB2 association with Hsp70 and prevented the 17-AAG-induced dissociation of Hsp90.	tanespimycin	99-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
12684036-4	2003	Association of cPGES with Hsp90 was increased in cells stimulated with A23187 or bradykinin, accompanied by concomitant increases in cPGES activity and PGE(2) production.	Calcimycin	71-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
12657742-0	2003	Trichloroethylene decreases heat shock protein 90 interactions with endothelial nitric oxide synthase: implications for endothelial cell proliferation.	Trichloroethylene	0-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
12820653-5	2003	The chaperone Hsp90 is found in a complex that coprecipitates with inactivated VEGFR2, and the association is increased by VEGF and decreased by geldanamycin, a specific inhibitor of Hsp90-mediated events.	geldanamycin	145-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12820653-5	2003	The chaperone Hsp90 is found in a complex that coprecipitates with inactivated VEGFR2, and the association is increased by VEGF and decreased by geldanamycin, a specific inhibitor of Hsp90-mediated events.	geldanamycin	145-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
12820659-1	2003	In all species studied to date, the function of heat shock protein 90 (Hsp90), a ubiquitous and evolutionarily conserved molecular chaperone, is inhibited selectively by the natural product drugs geldanamycin (GA) and radicicol.	geldanamycin	196-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
12820659-1	2003	In all species studied to date, the function of heat shock protein 90 (Hsp90), a ubiquitous and evolutionarily conserved molecular chaperone, is inhibited selectively by the natural product drugs geldanamycin (GA) and radicicol.	geldanamycin	196-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
12820659-1	2003	In all species studied to date, the function of heat shock protein 90 (Hsp90), a ubiquitous and evolutionarily conserved molecular chaperone, is inhibited selectively by the natural product drugs geldanamycin (GA) and radicicol.	geldanamycin	210-212	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
12820659-1	2003	In all species studied to date, the function of heat shock protein 90 (Hsp90), a ubiquitous and evolutionarily conserved molecular chaperone, is inhibited selectively by the natural product drugs geldanamycin (GA) and radicicol.	geldanamycin	210-212	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
12820659-1	2003	In all species studied to date, the function of heat shock protein 90 (Hsp90), a ubiquitous and evolutionarily conserved molecular chaperone, is inhibited selectively by the natural product drugs geldanamycin (GA) and radicicol.	monorden	218-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
12820659-1	2003	In all species studied to date, the function of heat shock protein 90 (Hsp90), a ubiquitous and evolutionarily conserved molecular chaperone, is inhibited selectively by the natural product drugs geldanamycin (GA) and radicicol.	monorden	218-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
12820659-2	2003	Crystal structures of the N-terminal region of yeast and human Hsp90 have revealed that these compounds interact with the chaperone in a Bergerat-type adenine nucleotide-binding fold shared throughout the gyrase, Hsp90, histidine kinase mutL (GHKL) superfamily of adenosine triphosphatases.	Adenine Nucleotides	151-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
12820659-2	2003	Crystal structures of the N-terminal region of yeast and human Hsp90 have revealed that these compounds interact with the chaperone in a Bergerat-type adenine nucleotide-binding fold shared throughout the gyrase, Hsp90, histidine kinase mutL (GHKL) superfamily of adenosine triphosphatases.	Adenine Nucleotides	151-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	213-218
12820659-7	2003	Further, affinity precipitation studies using chimeric worm-vertebrate fusion proteins or worm C-terminal truncations expressed in reticulocyte lysate revealed that the conserved nucleotide-binding fold of worm Hsp90 exhibits the novel ability to bind adenosine triphosphate but not GA.	Adenosine Triphosphate	252-274	heat shock protein 90 alpha family class A member 1	Homo sapiens	211-216
12820659-8	2003	Despite its unusual GA resistance, worm Hsp90 appeared fully functional when expressed in a vertebrate background.	geldanamycin	20-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
12820659-11	2003	These findings provide new insights into the nature of unusual N-terminal nucleotide-binding fold of Hsp90 and suggest that target-related drug resistance is unlikely to emerge in patients receiving GA-like chemotherapeutic agents.	geldanamycin	199-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
12684036-4	2003	Association of cPGES with Hsp90 was increased in cells stimulated with A23187 or bradykinin, accompanied by concomitant increases in cPGES activity and PGE(2) production.	Prostaglandins E	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
12684036-5	2003	Moreover, treatment of cells with Hsp90 inhibitors, which destabilized the cPGES/Hsp90 complex, reduced cPGES activity and PGE(2) production to basal levels.	Prostaglandins E	123-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
12519764-5	2003	This effect was abolished by the specific HSP90 inhibitor geldanamycin (GA) at both calcium concentrations.	geldanamycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
12519764-9	2003	At 100 nm Ca(2+), HSP90 promoted dose-dependent CaM binding to eNOS that was fully inhibitable by GA. At high calcium, HSP90 did not affect CaM binding to eNOS, but GA inhibited HSP90 binding to eNOS.	geldanamycin	98-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
12519764-10	2003	At high Ca(2+), HSP90 caused the V(max) of eNOS for l-arginine to increase by 2-fold, but the K(m) of eNOS was unchanged.	Arginine	52-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
12725864-0	2003	Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	44-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
12725864-2	2003	We describe the 1.75 A resolution crystal structure of human Hsp90 alpha (residues 9-236) complexed with 17-desmethoxy-17-N,N-dimethylaminoethylamino-geldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	105-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-72
12725864-2	2003	We describe the 1.75 A resolution crystal structure of human Hsp90 alpha (residues 9-236) complexed with 17-desmethoxy-17-N,N-dimethylaminoethylamino-geldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	164-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-72
12725864-4	2003	Targeted molecular dynamics simulations and energetic analysis indicate that geldanamycin undergoes two major conformational changes when it binds Hsp90, with the key step of the conversion being the trans to cis conformational change of the macrocycle amide bond.	geldanamycin	77-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
12725864-4	2003	Targeted molecular dynamics simulations and energetic analysis indicate that geldanamycin undergoes two major conformational changes when it binds Hsp90, with the key step of the conversion being the trans to cis conformational change of the macrocycle amide bond.	Amides	253-258	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
12725864-5	2003	We speculate that 17-DMAG analogs constrained to a cis-amide in the ground state could provide a significant increase in affinity for Hsp90.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
12725864-5	2003	We speculate that 17-DMAG analogs constrained to a cis-amide in the ground state could provide a significant increase in affinity for Hsp90.	cis-amide	51-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
12586360-4	2003	Treatment of cells with novobiocin, which blocks C-terminal interaction of HSP90, disrupted HSP90 binding to Akt, induced Akt dephosphorylation and significantly reduced telomerase activity.	Novobiocin	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
12586360-4	2003	Treatment of cells with novobiocin, which blocks C-terminal interaction of HSP90, disrupted HSP90 binding to Akt, induced Akt dephosphorylation and significantly reduced telomerase activity.	Novobiocin	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
12571865-2	2003	Geldanamycin (GD) is a benzoquinone ansamycin that inhibits the function of Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
12571865-2	2003	Geldanamycin (GD) is a benzoquinone ansamycin that inhibits the function of Hsp90.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
12571865-2	2003	Geldanamycin (GD) is a benzoquinone ansamycin that inhibits the function of Hsp90.	benzoquinone ansamycin	23-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
12678505-0	2003	Hsp90 binds CpG oligonucleotides directly: implications for hsp90 as a missing link in CpG signaling and recognition.	Oligonucleotides	16-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12678505-0	2003	Hsp90 binds CpG oligonucleotides directly: implications for hsp90 as a missing link in CpG signaling and recognition.	Oligonucleotides	16-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
12678505-4	2003	Hsp90 was characterized as a binder to oligodeoxynucleotides (ODNs) containing CpG motifs (CpG ODNs) after several purification steps from crude protein extracts of peripheral blood mononuclear cells.	Oligodeoxyribonucleotides	39-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
12563018-4	2003	In the 5 years since we last reviewed this subject, much has been learned about hsp90 structure, nucleotide-binding, and cochaperone interactions; the most important concept is that ATP hydrolysis by an intrinsic ATPase activity results in a conformational change in hsp90 that is required to induce conformational change in a substrate protein.	cochaperone	121-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	267-272
12563018-4	2003	In the 5 years since we last reviewed this subject, much has been learned about hsp90 structure, nucleotide-binding, and cochaperone interactions; the most important concept is that ATP hydrolysis by an intrinsic ATPase activity results in a conformational change in hsp90 that is required to induce conformational change in a substrate protein.	Adenosine Triphosphate	182-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
12563018-4	2003	In the 5 years since we last reviewed this subject, much has been learned about hsp90 structure, nucleotide-binding, and cochaperone interactions; the most important concept is that ATP hydrolysis by an intrinsic ATPase activity results in a conformational change in hsp90 that is required to induce conformational change in a substrate protein.	Adenosine Triphosphate	182-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	267-272
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
12563018-7	2003	An hsp90*Hop*hsp70*hsp40 complex opens the cleft in an ATP-dependent process to produce a receptor*hsp90 heterocomplex with hsp90 in its ATP-bound conformation, and p23 then interacts with the hsp90 to stabilize the complex.	Adenosine Triphosphate	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
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.	Adenosine Triphosphate	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	264-269
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
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.	Adenosine Triphosphate	240-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	264-269
12538799-7	2003	Finally, a new perspective on the regulation of NOS by hsp90-based chaperones is presented that involves facilitated heme insertion into the enzyme.	Heme	117-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
12519764-5	2003	This effect was abolished by the specific HSP90 inhibitor geldanamycin (GA) at both calcium concentrations.	geldanamycin	72-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
12519764-5	2003	This effect was abolished by the specific HSP90 inhibitor geldanamycin (GA) at both calcium concentrations.	Calcium	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
12519764-7	2003	HSP90 also significantly increased the rate of NADPH-dependent cytochrome c reduction by eNOS at both low and high Ca(2+) concentrations.	NADP	47-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12435747-2	2003	Unlike wild-type cells, cka2-13 cells were sensitive to the Hsp90-specific inhibitor geldanamycin, and this sensitivity was suppressed by overexpression of either Hsp90 or Cdc37.	geldanamycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
12471035-8	2003	Geldanamycin and radicicol, two chemically unrelated inhibitors of Hsp90, decreased the expression of EGFRvIII in glioblastoma cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
12471035-8	2003	Geldanamycin and radicicol, two chemically unrelated inhibitors of Hsp90, decreased the expression of EGFRvIII in glioblastoma cells.	monorden	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
12435747-2	2003	Unlike wild-type cells, cka2-13 cells were sensitive to the Hsp90-specific inhibitor geldanamycin, and this sensitivity was suppressed by overexpression of either Hsp90 or Cdc37.	geldanamycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
12559950-3	2003	Here we demonstrate that IL-6-induced gene expression was suppressed by a specific heat-shock protein 90 (Hsp90) inhibitor, geldanamycin (GA) in human hepatoma Hep3B cells.	geldanamycin	124-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
12559950-3	2003	Here we demonstrate that IL-6-induced gene expression was suppressed by a specific heat-shock protein 90 (Hsp90) inhibitor, geldanamycin (GA) in human hepatoma Hep3B cells.	geldanamycin	124-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
12559950-3	2003	Here we demonstrate that IL-6-induced gene expression was suppressed by a specific heat-shock protein 90 (Hsp90) inhibitor, geldanamycin (GA) in human hepatoma Hep3B cells.	geldanamycin	138-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
12559950-3	2003	Here we demonstrate that IL-6-induced gene expression was suppressed by a specific heat-shock protein 90 (Hsp90) inhibitor, geldanamycin (GA) in human hepatoma Hep3B cells.	geldanamycin	138-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
12559950-5	2003	This inhibitory effect of GA on STAT3 activation was reversed by overexpression of Hsp90.	geldanamycin	26-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
12559950-6	2003	Furthermore, Hsp90 directly bound to STAT3 via its N-terminal region, which interacted with GA. We provide evidence that the action of GA on IL-6 functions was due to the inhibition of direct physical interactions between STAT3 and Hsp90, which represents a novel role of Hsp90 in the IL-6 signaling pathways.	geldanamycin	92-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
12559950-6	2003	Furthermore, Hsp90 directly bound to STAT3 via its N-terminal region, which interacted with GA. We provide evidence that the action of GA on IL-6 functions was due to the inhibition of direct physical interactions between STAT3 and Hsp90, which represents a novel role of Hsp90 in the IL-6 signaling pathways.	geldanamycin	92-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
12559950-6	2003	Furthermore, Hsp90 directly bound to STAT3 via its N-terminal region, which interacted with GA. We provide evidence that the action of GA on IL-6 functions was due to the inhibition of direct physical interactions between STAT3 and Hsp90, which represents a novel role of Hsp90 in the IL-6 signaling pathways.	geldanamycin	92-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
12427754-7	2003	Inhibition of hsp90-p53 interaction by geldanamycin prevented p53 accumulation partially in ATM-wild type cells and completely in ATM-deficient cells.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
12504007-4	2002	The identification of these Hsp90 cochaperone activators adds to the complex roles of cochaperones in regulating the ATPase-coupled conformational changes of the Hsp90 chaperone cycle.	cochaperones	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
12617036-5	2003	HSP90 functions in an ATP-dependent manner with other molecular chaperones such as Cdc37 and FKBP52.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
12617036-6	2003	An HSP90 inhibitor, geldanamycin, binds the ATP-binding pocket of HSP90 and specifically inhibits the essential ATPase activity of HSP90.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
12617036-6	2003	An HSP90 inhibitor, geldanamycin, binds the ATP-binding pocket of HSP90 and specifically inhibits the essential ATPase activity of HSP90.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12617036-6	2003	An HSP90 inhibitor, geldanamycin, binds the ATP-binding pocket of HSP90 and specifically inhibits the essential ATPase activity of HSP90.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12617036-6	2003	An HSP90 inhibitor, geldanamycin, binds the ATP-binding pocket of HSP90 and specifically inhibits the essential ATPase activity of HSP90.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
12617036-6	2003	An HSP90 inhibitor, geldanamycin, binds the ATP-binding pocket of HSP90 and specifically inhibits the essential ATPase activity of HSP90.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12617036-6	2003	An HSP90 inhibitor, geldanamycin, binds the ATP-binding pocket of HSP90 and specifically inhibits the essential ATPase activity of HSP90.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
12617036-7	2003	Thus, treatment of cells with geldanamycin results in inactivation, destabilization, and degradation of HSP90 client proteins.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
12617036-8	2003	Because HSP90 client proteins play important roles in the regulation of the cell cycle, cell growth, cell survival, apoptosis, and oncogenesis, geldanamycin obstructs the proliferation of cultured cancer cells and shows anti-cancer activity in experimental animals.	geldanamycin	144-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
12504007-4	2002	The identification of these Hsp90 cochaperone activators adds to the complex roles of cochaperones in regulating the ATPase-coupled conformational changes of the Hsp90 chaperone cycle.	cochaperones	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
12235142-8	2002	Geldanamycin, an HSP90 inhibitor, markedly inhibited IL-6-stimulated STAT3 signaling in Hep3B hepatocytes cultured overnight at 39.5 degrees C as evaluated by DNA-shift assays, trafficking of PY-STAT3 to the nucleus, cross-precipitation of HSP90 by anti-STAT3 polyclonal antibody, and reporter/luciferase construct experiments.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
12446770-2	2002	The HSP90-binding drug geldanamycin interferes with this activity and promotes proteasome-dependent degradation of most HSP90 client proteins.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
12446770-2	2002	The HSP90-binding drug geldanamycin interferes with this activity and promotes proteasome-dependent degradation of most HSP90 client proteins.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
12446770-3	2002	Geldanamycin also binds to GRP94, the HSP90 paralog located in the endoplasmic reticulum (ER).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
12446770-6	2002	Both geldanamycin and the HSP90-specific inhibitor, 514, led to the dissociation of HSP90 from the kinases and a concomitant turnover of newly synthesized and existing pools of these proteins, demonstrating that the continued association of HSP90 with the kinases was required to maintain their stability.	geldanamycin	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
12446770-6	2002	Both geldanamycin and the HSP90-specific inhibitor, 514, led to the dissociation of HSP90 from the kinases and a concomitant turnover of newly synthesized and existing pools of these proteins, demonstrating that the continued association of HSP90 with the kinases was required to maintain their stability.	geldanamycin	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
12324468-0	2002	The influence of ATP and p23 on the conformation of hsp90.	Adenosine Triphosphate	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
12324468-1	2002	The chaperoning activity of the heat shock protein hsp90 is directed, in part, by the binding and hydrolysis of ATP and also by association with co-chaperone proteins.	Adenosine Triphosphate	112-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
12324468-2	2002	One co-chaperone, p23, binds to hsp90 only when hsp90 is in a conformation induced by the binding of ATP.	Adenosine Triphosphate	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
12324468-2	2002	One co-chaperone, p23, binds to hsp90 only when hsp90 is in a conformation induced by the binding of ATP.	Adenosine Triphosphate	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
12324468-3	2002	Once formed, the p23-hsp90 complex is very stable upon the removal of ATP and dissipates at 30 degrees with a half-life of about 45 min.	Adenosine Triphosphate	70-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
12324468-4	2002	This was shown to be due to the high stability of the ATP-induced state of hsp90, not to the rate of p23 dissociation.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
12324468-6	2002	This conformational state of hsp90 is correlated with the tight binding of ADP resulting from hydrolysis of bound ATP.	Adenosine Diphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
12324468-6	2002	This conformational state of hsp90 is correlated with the tight binding of ADP resulting from hydrolysis of bound ATP.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
12324468-7	2002	Both p23 and molybdate enhance and stabilize the nucleotide-bound state of hsp90, and this state is maximized by the presence of both agents.	molybdate	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
12324468-8	2002	These results can be explained in a model where the binding of ATP induces a conformational transition in hsp90 that traps the nucleotide and is committed to ATP hydrolysis.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
12324468-8	2002	These results can be explained in a model where the binding of ATP induces a conformational transition in hsp90 that traps the nucleotide and is committed to ATP hydrolysis.	Adenosine Triphosphate	158-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
12235160-2	2002	The function of Hsp90 has been shown to be dependent on its ability to hydrolyze ATP, and in vitro studies suggest that the dimeric nature of Hsp90 is critical for this activity.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
12235160-2	2002	The function of Hsp90 has been shown to be dependent on its ability to hydrolyze ATP, and in vitro studies suggest that the dimeric nature of Hsp90 is critical for this activity.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
12235160-3	2002	ATP binding occurs at the N-terminal domains of the Hsp90 dimer, whereas the main dimerization site resides in the very C-terminal domain.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
12235160-7	2002	We show that N-terminal deletion variants of Hsp90 are severely impaired in their ability to hydrolyze ATP.	Adenosine Triphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
12426384-3	2002	We find that the alphaGDI-chaperone complex is dissociated in response to Ca(2+)-induced neurotransmitter release, that chaperone complex dissociation is sensitive to the Hsp90 inhibitor geldanamycin (GA) and that GA inhibits the ability of alphaGDI to recycle Rab3A during neurotransmitter release.	geldanamycin	187-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
12426384-3	2002	We find that the alphaGDI-chaperone complex is dissociated in response to Ca(2+)-induced neurotransmitter release, that chaperone complex dissociation is sensitive to the Hsp90 inhibitor geldanamycin (GA) and that GA inhibits the ability of alphaGDI to recycle Rab3A during neurotransmitter release.	geldanamycin	201-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
12426384-3	2002	We find that the alphaGDI-chaperone complex is dissociated in response to Ca(2+)-induced neurotransmitter release, that chaperone complex dissociation is sensitive to the Hsp90 inhibitor geldanamycin (GA) and that GA inhibits the ability of alphaGDI to recycle Rab3A during neurotransmitter release.	geldanamycin	214-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
12235142-8	2002	Geldanamycin, an HSP90 inhibitor, markedly inhibited IL-6-stimulated STAT3 signaling in Hep3B hepatocytes cultured overnight at 39.5 degrees C as evaluated by DNA-shift assays, trafficking of PY-STAT3 to the nucleus, cross-precipitation of HSP90 by anti-STAT3 polyclonal antibody, and reporter/luciferase construct experiments.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
12232764-2	2002	We hypothesised that, when labelled appropriately, changes in choline kinetics could be used to assess geldanamycin pharmacodynamics, which involves inhibition of the HSP90 molecular chaperone-->Raf1-->Mitogenic Extracellular Kinase-->Extracellular Signal-Regulated Kinase 1 and 2 signal transduction pathway.	Choline	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
12391259-4	2002	Our results indicate that the 90-kDa heat-shock protein (Hsp90) inhibitor radicicol reduces the hypoxia-induced expression of both endogenous vascular endothelial growth factor (VEGF) and HRE-driven reporter plasmids.	monorden	74-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
12391259-7	2002	Our results, the first to show that radicicol specifically inhibits the interaction between the HIF-1alpha/Arnt heterodimer and HRE, suggest that Hsp90 modulates the conformation of the HIF-1alpha/Arnt heterodimer, making it suitable for interaction with HRE.	monorden	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
12161444-10	2002	Hop can inhibit the ATP binding and p23 binding activity of hsp90, yet this can be reversed if hsp70 is present in the complex.	Adenosine Triphosphate	20-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
12269819-2	2002	In this study, we investigated the influence of divalent cations Mg(2+) and Ca(2+) on the hydrodynamic properties and quaternary structure of Hsp90.	magnesium ion	65-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
12269819-3	2002	Using analytical ultracentrifugation, size-exclusion chromatography, and polyacrylamide gel electrophoresis, we showed that native Hsp90 was mostly dimeric.	polyacrylamide	73-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
12269819-5	2002	Using chemical cross-linking and analytical ultracentrifugation, we showed that Mg(2+) and Ca(2+) induced a tertiary conformational change of Hsp90, leading to a self-association process.	magnesium ion	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
12269819-8	2002	We previously showed that GA inhibits Hsp90 heat-induced oligomerization [Garnier, C., Protasevich, I., Gilli, R., Tsvetkov, P., Lobachov, V., Peyrot, V., Briand, C., and Makarov, A.	geldanamycin	26-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
12415202-5	2002	Benzoquinone ansamycins were the first group of compounds for which interference with Hsp90 function was shown to be the major mechanism of action.	benzoquinone ansamycins	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
12415202-9	2002	Recently, it became apparent that coumarin antibiotics, cisplatin and paclitaxel also bind to Hsp90.	coumarin	34-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
12415202-9	2002	Recently, it became apparent that coumarin antibiotics, cisplatin and paclitaxel also bind to Hsp90.	Cisplatin	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
12415202-9	2002	Recently, it became apparent that coumarin antibiotics, cisplatin and paclitaxel also bind to Hsp90.	Paclitaxel	70-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
12213470-0	2002	Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase.	purine	17-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
12213470-1	2002	The first published synthesis and characterization of a purine-scaffold library of hsp90 inhibitors is presented.	purine	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
12176997-2	2002	Natural products and synthetic small molecules that bind to the ATP-binding pocket in the amino-terminal domain of Hsp90 inhibit its function and cause the degradation of these client proteins.	Adenosine Triphosphate	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
12351420-0	2002	BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90.	Imatinib Mesylate	50-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-180
12323066-1	2002	Geldanamycin (GA), an antitumor Hsp90 inhibitor, was made for the first time by using an oxidative demethylation reaction as the final step.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
12323066-1	2002	Geldanamycin (GA), an antitumor Hsp90 inhibitor, was made for the first time by using an oxidative demethylation reaction as the final step.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
15989551-4	2002	One Hsp90 inhibitor, 17-allylamino-geldanamycin (17-AAG), is currently in Phase I clinical trials.	tanespimycin	21-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
12232764-2	2002	We hypothesised that, when labelled appropriately, changes in choline kinetics could be used to assess geldanamycin pharmacodynamics, which involves inhibition of the HSP90 molecular chaperone-->Raf1-->Mitogenic Extracellular Kinase-->Extracellular Signal-Regulated Kinase 1 and 2 signal transduction pathway.	geldanamycin	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
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
12093808-2	2002	The first step in assembly is the ATP-dependent and hsp40 (YDJ-1)-dependent binding of hsp70 to the GR, which primes the receptor for subsequent ATP-dependent activation by hsp90, Hop, and p23 (Morishima, Y., Murphy, P. J. M., Li, D. P., Sanchez, E. R., and Pratt, W. B.	Adenosine Triphosphate	145-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
12093808-9	2002	The rate-limiting step is the ATP-dependent opening of the steroid binding cleft after hsp90 binding.	Adenosine Triphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
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
12093808-10	2002	This activating step requires the N-terminal ATP-binding site of hsp90, but we cannot establish any role for a C-terminal ATP-binding site in steroid binding cleft opening.	Adenosine Triphosphate	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
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.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
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
12183065-0	2002	Volatile organic compounds cytotoxicity and expression of HSP72, HSP90 and GRP78 stress proteins in cultured human cells.	Organic Chemicals	9-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
12052835-5	2002	Geldanamycin (GA), an Hsp90 antagonist, promoted efficient ubiquitination and proteasome-mediated degradation of HIF-1 alpha in RCC in both normoxia and hypoxia.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
12052835-5	2002	Geldanamycin (GA), an Hsp90 antagonist, promoted efficient ubiquitination and proteasome-mediated degradation of HIF-1 alpha in RCC in both normoxia and hypoxia.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
12052835-8	2002	These findings demonstrate that disruption of Hsp90 function 1) promotes HIF-1 alpha degradation via a novel, oxygen-independent E3 ubiquitin ligase and 2) diminishes HIF-1 alpha transcriptional activity.	Oxygen	110-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
12117999-7	2002	Geldanamycin treatment, which specifically inhibits Hsp90, caused a partial loss of wild-type Galpha(12) and a complete loss of the Cys-11 mutant from the lipid rafts and the appearance of a higher molecular weight form of Galpha(12) in the soluble fractions.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
12117999-7	2002	Geldanamycin treatment, which specifically inhibits Hsp90, caused a partial loss of wild-type Galpha(12) and a complete loss of the Cys-11 mutant from the lipid rafts and the appearance of a higher molecular weight form of Galpha(12) in the soluble fractions.	cys-11	132-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
12530016-7	2002	CONCLUSION: Since geldanamycin and radicicol are specific inhibitors of the ATPase in HSP90, the present result implies that ATPase activity in HSP90 plays some role in this apoptosis.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
12530016-7	2002	CONCLUSION: Since geldanamycin and radicicol are specific inhibitors of the ATPase in HSP90, the present result implies that ATPase activity in HSP90 plays some role in this apoptosis.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
12530016-7	2002	CONCLUSION: Since geldanamycin and radicicol are specific inhibitors of the ATPase in HSP90, the present result implies that ATPase activity in HSP90 plays some role in this apoptosis.	monorden	35-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
12530016-7	2002	CONCLUSION: Since geldanamycin and radicicol are specific inhibitors of the ATPase in HSP90, the present result implies that ATPase activity in HSP90 plays some role in this apoptosis.	monorden	35-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
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
12093808-2	2002	The first step in assembly is the ATP-dependent and hsp40 (YDJ-1)-dependent binding of hsp70 to the GR, which primes the receptor for subsequent ATP-dependent activation by hsp90, Hop, and p23 (Morishima, Y., Murphy, P. J. M., Li, D. P., Sanchez, E. R., and Pratt, W. B.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
12375735-5	2002	There were epidermal dendritic cells as well as macrophage-like cells in the dermis, which expressed hsp 65 and hsp 90, in biopsies from metal salt-treated and control skin, while expression of hsp 72 in macrophage-like cells was found only in the dermis.	metal salt	137-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-118
12119343-4	2002	Geldanamycin, an inhibitor of hsp90, almost completely suppressed OVA antigen presentation in PA28alpha(-/-)/beta(-/-) lipopolysaccharide blasts, but not in wild-type cells, indicating that hsp90 compensates for the loss of PA28 and is essential in the PA28-independent pathway.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
12119132-0	2002	Expression of hsp 90 in the human kidney and in proximal tubule cells exposed to heat, sodium arsenite and cadmium chloride.	sodium arsenite	87-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-20
12119132-0	2002	Expression of hsp 90 in the human kidney and in proximal tubule cells exposed to heat, sodium arsenite and cadmium chloride.	Cadmium Chloride	107-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-20
12119343-4	2002	Geldanamycin, an inhibitor of hsp90, almost completely suppressed OVA antigen presentation in PA28alpha(-/-)/beta(-/-) lipopolysaccharide blasts, but not in wild-type cells, indicating that hsp90 compensates for the loss of PA28 and is essential in the PA28-independent pathway.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
12174876-0	2002	ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
12174876-5	2002	In cells overexpressing erbB2, the most notable effect on chemosensitivity was that of significantly increased (5-fold) sensitivity to the heat shock protein 90 (HSP90) molecular chaperone inhibitor geldanamycin.	geldanamycin	199-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-160
12174876-5	2002	In cells overexpressing erbB2, the most notable effect on chemosensitivity was that of significantly increased (5-fold) sensitivity to the heat shock protein 90 (HSP90) molecular chaperone inhibitor geldanamycin.	geldanamycin	199-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
12100037-7	2002	In normal IgG this autoreactivity could be adsorbed almost completely on F(ab")2 fragments from the same IgG preparation, coupled to Sepharose and could be inhibited by the effluent obtained after subjecting normal IgG to HSP90 affinity column.	Sepharose	133-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	222-227
12086682-10	2002	These data support the hypothesis that n-LDL increases O(2)(*-), which scavenges *NO, and suggest that n-LDL uncouples eNOS activity by decreasing the association of hsp90 as an initial step in signaling eNOS to generate O(2)(*-).	Nitrogen	39-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
12115584-5	2002	Levels of expression of heat shock protein 90 alpha (Hsp90 alpha) were found to be increased 20 min after the nicotine treatment, as analyzed by polymerase chain reaction-based mRNA differential display after Northern blotting analysis of mRNA amounts.	Nicotine	110-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-64
12115584-6	2002	Cellular contents of Hsp90 alpha were furthermore increased in the nicotine-treated RSa cells, as quantitated by Western immunoblot analysis.	Nicotine	67-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-32
12115584-7	2002	By contrast, in RSa cells treated with nicotine in combination with geldanamycin (GA), an inhibitor of Hsp90 alpha function, DNA fragmentation was not detected and caspase-3 protease activity levels were the same as those of mock-treated cells.	Nicotine	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-114
12115584-7	2002	By contrast, in RSa cells treated with nicotine in combination with geldanamycin (GA), an inhibitor of Hsp90 alpha function, DNA fragmentation was not detected and caspase-3 protease activity levels were the same as those of mock-treated cells.	geldanamycin	68-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-114
12115584-7	2002	By contrast, in RSa cells treated with nicotine in combination with geldanamycin (GA), an inhibitor of Hsp90 alpha function, DNA fragmentation was not detected and caspase-3 protease activity levels were the same as those of mock-treated cells.	geldanamycin	82-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-114
12115584-8	2002	Nicotine-induced caspase-3 activation and Hsp90 alpha expression, as well as suppression of the induction by GA, were also observed in a xeroderma pigmentosum patient-derived cell line, XP2OS cells.	Nicotine	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-53
12115584-9	2002	Thus, it was suggested that nicotine induces apoptosis, possibly via Hsp90 alpha expression, in human cells tested.	Nicotine	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-80
11916974-2	2002	For some client proteins the co-chaperone Sti1/Hop/p60 acts as a "scaffold," recruiting Hsp70 and the bound client to Hsp90 early in the cycle and suppressing ATP turnover by Hsp90 during the loading phase.	Adenosine Triphosphate	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
11916974-2	2002	For some client proteins the co-chaperone Sti1/Hop/p60 acts as a "scaffold," recruiting Hsp70 and the bound client to Hsp90 early in the cycle and suppressing ATP turnover by Hsp90 during the loading phase.	Adenosine Triphosphate	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
11916974-6	2002	However, unlike Sti1/Hop/p60, which can displace geldanamycin upon binding to Hsp90, Cdc37p/p50(cdc37) forms a stable complex with geldanamycin-bound Hsp90 and may be sequestered in geldanamycin-inhibited Hsp90 complexes in vivo.	geldanamycin	131-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
11916974-6	2002	However, unlike Sti1/Hop/p60, which can displace geldanamycin upon binding to Hsp90, Cdc37p/p50(cdc37) forms a stable complex with geldanamycin-bound Hsp90 and may be sequestered in geldanamycin-inhibited Hsp90 complexes in vivo.	geldanamycin	131-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
11916974-6	2002	However, unlike Sti1/Hop/p60, which can displace geldanamycin upon binding to Hsp90, Cdc37p/p50(cdc37) forms a stable complex with geldanamycin-bound Hsp90 and may be sequestered in geldanamycin-inhibited Hsp90 complexes in vivo.	geldanamycin	131-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
11916974-6	2002	However, unlike Sti1/Hop/p60, which can displace geldanamycin upon binding to Hsp90, Cdc37p/p50(cdc37) forms a stable complex with geldanamycin-bound Hsp90 and may be sequestered in geldanamycin-inhibited Hsp90 complexes in vivo.	geldanamycin	131-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
11923316-0	2002	hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90.	Heme	22-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11923316-0	2002	hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90.	geldanamycin	89-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11923316-2	2002	We have discovered that inhibition of hsp90 by radicicol or geldanamycin nearly prevents the heme-mediated activation and assembly of heme-deficient apo-nNOS in insect cells.	monorden	47-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
11923316-2	2002	We have discovered that inhibition of hsp90 by radicicol or geldanamycin nearly prevents the heme-mediated activation and assembly of heme-deficient apo-nNOS in insect cells.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
11923316-2	2002	We have discovered that inhibition of hsp90 by radicicol or geldanamycin nearly prevents the heme-mediated activation and assembly of heme-deficient apo-nNOS in insect cells.	Heme	93-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
11923316-5	2002	We propose that the hsp90-based chaperone machinery facilitates functional heme entry into apo-nNOS by the opening of the hydrophobic heme-binding cleft in the protein.	Heme	75-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11923316-5	2002	We propose that the hsp90-based chaperone machinery facilitates functional heme entry into apo-nNOS by the opening of the hydrophobic heme-binding cleft in the protein.	Heme	134-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11923316-6	2002	Previously, it has been reported that the hsp90 inhibitor geldanamycin uncouples endothelial NOS activity and increases endothelial NOS-dependent O(2)() production.	geldanamycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
11923316-6	2002	Previously, it has been reported that the hsp90 inhibitor geldanamycin uncouples endothelial NOS activity and increases endothelial NOS-dependent O(2)() production.	o(2)	146-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
12003772-3	2002	Incubation of PAEC with taxol (15 microM) for 2-4 h resulted in an increase in NO production, eNOS activity, and the amount of HSP90 binding to eNOS.	paec	14-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
12003772-3	2002	Incubation of PAEC with taxol (15 microM) for 2-4 h resulted in an increase in NO production, eNOS activity, and the amount of HSP90 binding to eNOS.	Paclitaxel	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
12003772-4	2002	Incubation of PAEC with nocodazole (50 microM) for 2-4 h induced a decrease in NO production, eNOS activity, and the amount of HSP90 binding to eNOS.	paec	14-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
12003772-4	2002	Incubation of PAEC with nocodazole (50 microM) for 2-4 h induced a decrease in NO production, eNOS activity, and the amount of HSP90 binding to eNOS.	Nocodazole	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
12003772-6	2002	Geldanamycin, a HSP90 inhibitor, prevented the taxol-induced increase in eNOS activity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
12003772-6	2002	Geldanamycin, a HSP90 inhibitor, prevented the taxol-induced increase in eNOS activity.	Paclitaxel	47-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
12036925-2	2002	Geldanamycin and its less toxic analogue, 17- (allylamino)-17-demethoxygeldanamycin (17-AAG) are ansamycin antibiotics that bind to a highly conserved pocket in the hsp 90 chaperone protein and inhibit its function.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-171
12036925-2	2002	Geldanamycin and its less toxic analogue, 17- (allylamino)-17-demethoxygeldanamycin (17-AAG) are ansamycin antibiotics that bind to a highly conserved pocket in the hsp 90 chaperone protein and inhibit its function.	tanespimycin	42-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-171
12036925-2	2002	Geldanamycin and its less toxic analogue, 17- (allylamino)-17-demethoxygeldanamycin (17-AAG) are ansamycin antibiotics that bind to a highly conserved pocket in the hsp 90 chaperone protein and inhibit its function.	Rifabutin	97-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-171
12022881-1	2002	The maturation and activation of newly synthesized molecules of the heme-regulated inhibitor of protein synthesis (HRI) in reticulocytes require their functional interaction with Hsp90.	Heme	68-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
11877417-3	2002	The TPR1 and TPR2A domains of the Hsp70/Hsp90 adapter protein p60/Hop specifically bind to short peptides corresponding to the C-terminal tails of Hsp70 and Hsp90, respectively, both of which contain the highly conserved sequence motif EEVD-COOH.	Carbonic Acid	241-245	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
11877417-3	2002	The TPR1 and TPR2A domains of the Hsp70/Hsp90 adapter protein p60/Hop specifically bind to short peptides corresponding to the C-terminal tails of Hsp70 and Hsp90, respectively, both of which contain the highly conserved sequence motif EEVD-COOH.	Carbonic Acid	241-245	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
11877417-12	2002	Ile-4 in Hsp70 and Met-4 in Hsp90 are most important in determining the specific binding of TPR1 and TPR2A, respectively.	Isoleucine	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
12022881-8	2002	Furthermore, the Hsp90 inhibitor geldanamycin negated the effects of phosphatase inhibitors on HRI maturation/activation.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
12006493-5	2002	The degradative pathway stimulated by TKIs appears to be chaperone mediated, and is common to the heat shock protein 90 (Hsp90) antagonist geldanamycin and a stress-induced mechanism.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
12006493-5	2002	The degradative pathway stimulated by TKIs appears to be chaperone mediated, and is common to the heat shock protein 90 (Hsp90) antagonist geldanamycin and a stress-induced mechanism.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
11980636-3	2002	Here, we show that treatment of prostate cancer PC-3 and LNCaP cells with the benzoquinone ansamycin geldanamycin, an Hsp90-specific inhibitor, induced degradation of HIF-1alpha protein in a dose- and time-dependent manner under both normoxia and hypoxia.	benzoquinone ansamycin geldanamycin	78-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
11983711-2	2002	The ansamycin antibiotic geldanamycin has frequently been used as an inhibitor of heat shock protein 90 (Hsp90), and this agent has been widely employed as a probe to examine the interactions of Hsp90 with endothelial nitric-oxide synthase.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-103
11983711-2	2002	The ansamycin antibiotic geldanamycin has frequently been used as an inhibitor of heat shock protein 90 (Hsp90), and this agent has been widely employed as a probe to examine the interactions of Hsp90 with endothelial nitric-oxide synthase.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
11983711-2	2002	The ansamycin antibiotic geldanamycin has frequently been used as an inhibitor of heat shock protein 90 (Hsp90), and this agent has been widely employed as a probe to examine the interactions of Hsp90 with endothelial nitric-oxide synthase.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
11983711-2	2002	The ansamycin antibiotic geldanamycin has frequently been used as an inhibitor of heat shock protein 90 (Hsp90), and this agent has been widely employed as a probe to examine the interactions of Hsp90 with endothelial nitric-oxide synthase.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-103
11983711-2	2002	The ansamycin antibiotic geldanamycin has frequently been used as an inhibitor of heat shock protein 90 (Hsp90), and this agent has been widely employed as a probe to examine the interactions of Hsp90 with endothelial nitric-oxide synthase.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
11983711-2	2002	The ansamycin antibiotic geldanamycin has frequently been used as an inhibitor of heat shock protein 90 (Hsp90), and this agent has been widely employed as a probe to examine the interactions of Hsp90 with endothelial nitric-oxide synthase.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
11983711-11	2002	In light of these findings, the studies using geldanamycin as an inhibitor of Hsp90 should be interpreted with caution.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
11969419-3	2002	From the study of glucocorticoid receptor (GR).hsp90.immunophilin complexes in mammalian cells, there is considerable evidence that both hsp90 and the FK506-binding immunophilin FKBP52 play a role in receptor movement from the cytoplasm to the nucleus.	Tacrolimus	151-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
11809754-2	2002	However, an in vitro chaperoning system consisting of five proteins (HSP40, HSP70, HOP, HSP90, and p23) with ATP is capable of restoring this function.	Adenosine Triphosphate	109-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
11823472-5	2002	Disruption of endogenous heat shock protein 90 (hsp90) function with geldanamycin abrogated BCR-induced cyclin D2 expression and proliferation.	geldanamycin	69-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-46
11823472-5	2002	Disruption of endogenous heat shock protein 90 (hsp90) function with geldanamycin abrogated BCR-induced cyclin D2 expression and proliferation.	geldanamycin	69-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
11895790-6	2002	In turn, Hsp90 modulated Bcl-2 expression, as shown by a complete blockage of VEGF-induced Bcl-2 expression and binding to Hsp90 by the Hsp90-specific inhibitor geldanamycin (GA).	geldanamycin	161-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
11895790-6	2002	In turn, Hsp90 modulated Bcl-2 expression, as shown by a complete blockage of VEGF-induced Bcl-2 expression and binding to Hsp90 by the Hsp90-specific inhibitor geldanamycin (GA).	geldanamycin	161-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
11895790-6	2002	In turn, Hsp90 modulated Bcl-2 expression, as shown by a complete blockage of VEGF-induced Bcl-2 expression and binding to Hsp90 by the Hsp90-specific inhibitor geldanamycin (GA).	geldanamycin	161-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
11895790-6	2002	In turn, Hsp90 modulated Bcl-2 expression, as shown by a complete blockage of VEGF-induced Bcl-2 expression and binding to Hsp90 by the Hsp90-specific inhibitor geldanamycin (GA).	geldanamycin	175-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
11895790-6	2002	In turn, Hsp90 modulated Bcl-2 expression, as shown by a complete blockage of VEGF-induced Bcl-2 expression and binding to Hsp90 by the Hsp90-specific inhibitor geldanamycin (GA).	geldanamycin	175-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
11895790-6	2002	In turn, Hsp90 modulated Bcl-2 expression, as shown by a complete blockage of VEGF-induced Bcl-2 expression and binding to Hsp90 by the Hsp90-specific inhibitor geldanamycin (GA).	geldanamycin	175-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
11895790-7	2002	GA also blocked the VEGF-induced Hsp90 binding to APAF-1 on leukemic cells, a mechanism shown to inhibit apoptosis.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
11929951-9	2002	FK228 treatment also inhibited the binding of mutant p53 and Raf-1 to Hsp90; this inhibition was associated with acetylation of Hsp90.	romidepsin	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
11929951-9	2002	FK228 treatment also inhibited the binding of mutant p53 and Raf-1 to Hsp90; this inhibition was associated with acetylation of Hsp90.	romidepsin	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
11929951-10	2002	CONCLUSIONS: FK228 depletes the levels of several oncoproteins that are normally stabilized by binding to Hsp90 in cancer cells.	romidepsin	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	herbimycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	herbimycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	monorden	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
11960322-1	2002	Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors.	monorden	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
11779851-2	2002	Screening of drugs that could interfere with the Akt signaling pathway revealed that Hsp90 inhibitors (e.g. geldanamycin, radicicol, and its analogues) induced Akt dephosphorylation, which resulted in Akt inactivation and apoptosis of the cells.	geldanamycin	108-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
11779866-8	2002	Inhibition of the ATP-dependent chaperone activity of HSP90 by novobiocin or geldanamycin prevented heat-induced as well as hypoxia-induced HIF-1alpha accumulation, indicating a common role of the HSP90 chaperone activity in HIF-1alpha stabilization by these two environmental parameters.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
11779866-8	2002	Inhibition of the ATP-dependent chaperone activity of HSP90 by novobiocin or geldanamycin prevented heat-induced as well as hypoxia-induced HIF-1alpha accumulation, indicating a common role of the HSP90 chaperone activity in HIF-1alpha stabilization by these two environmental parameters.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	197-202
11779866-8	2002	Inhibition of the ATP-dependent chaperone activity of HSP90 by novobiocin or geldanamycin prevented heat-induced as well as hypoxia-induced HIF-1alpha accumulation, indicating a common role of the HSP90 chaperone activity in HIF-1alpha stabilization by these two environmental parameters.	Novobiocin	63-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
11779866-8	2002	Inhibition of the ATP-dependent chaperone activity of HSP90 by novobiocin or geldanamycin prevented heat-induced as well as hypoxia-induced HIF-1alpha accumulation, indicating a common role of the HSP90 chaperone activity in HIF-1alpha stabilization by these two environmental parameters.	geldanamycin	77-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
11777905-8	2002	Another common ATP-dependent chaperone, Hsp90, was absent from all HDAC complexes tested, whereas Hsp60 associated with HDAC1 only.	Adenosine Triphosphate	15-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
11779851-2	2002	Screening of drugs that could interfere with the Akt signaling pathway revealed that Hsp90 inhibitors (e.g. geldanamycin, radicicol, and its analogues) induced Akt dephosphorylation, which resulted in Akt inactivation and apoptosis of the cells.	monorden	122-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
11751878-0	2002	A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
11751878-2	2002	In vivo function of the molecular chaperone Hsp90 is ATP-dependent and requires the full-length protein.	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
11751878-3	2002	Our earlier studies predicted a second C-terminal ATP-binding site in Hsp90.	Adenosine Triphosphate	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
11751878-5	2002	We identified an N-terminal gamma-phosphate-binding motif in the middle domain of Hsp90 similar to other GHKL family members.	gamma-phosphate	28-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
11751878-7	2002	Whereas novobiocin disrupts both C- and N-terminal nucleotide binding, we found a selective C-terminal nucleotide competitor, cisplatin, that strengthens the Hsp90-Hsp70 complex leaving the Hsp90-p23 complex intact.	Cisplatin	126-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
11751878-7	2002	Whereas novobiocin disrupts both C- and N-terminal nucleotide binding, we found a selective C-terminal nucleotide competitor, cisplatin, that strengthens the Hsp90-Hsp70 complex leaving the Hsp90-p23 complex intact.	Cisplatin	126-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
11751878-8	2002	Cisplatin may provide a pharmacological tool to dissect C- and N-terminal nucleotide binding of Hsp90.	Cisplatin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
11748067-2	2002	Studies have shown that the HSP90-specific inhibitor geldanamycin (GA) can cause attenuation of NO-mediated processes.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
11751892-3	2002	Chicken or human hsp90 hydrolyzed ATP with a k(cat) of 0.02 min(-1) and a K(m) greater than 300 microm.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
11911945-4	2002	Here, we report that radicicol, an Hsp90-specific inhibitor, repressed estrogen-dependent transactivation of the ER as measured by pS2 gene transcription and a reporter gene encoding an estrogen-responsive element.	monorden	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
11911945-7	2002	These results suggest that radicicol disrupts the ER-Hsp90 heterodimeric complex, thereby generating ERalpha that is susceptible to ubiquitin/proteasome-induced degradation.	monorden	27-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
11934275-1	2002	We purified a large quantity of HSP90 from porcine testis by hydroxylapatite (HA-HSP90) and SDS-PAGE/electroelution (eluted-HSP90) to explore the molecular mechanism of HSP90 phosphorylation affecting its metabolism.	Durapatite	61-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
11934275-1	2002	We purified a large quantity of HSP90 from porcine testis by hydroxylapatite (HA-HSP90) and SDS-PAGE/electroelution (eluted-HSP90) to explore the molecular mechanism of HSP90 phosphorylation affecting its metabolism.	Sodium Dodecyl Sulfate	92-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
11934275-5	2002	Incubation of the purified HSP90 or HSP90 immunoprecipitated from extracts of human A431 cells, Balb/c 3T3 fibroblasts, and porcine testis with [gamma-32P]ATP/Mg2+ resulted in phosphorylation of HSP90.	[gamma-32p]	144-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
11934275-5	2002	Incubation of the purified HSP90 or HSP90 immunoprecipitated from extracts of human A431 cells, Balb/c 3T3 fibroblasts, and porcine testis with [gamma-32P]ATP/Mg2+ resulted in phosphorylation of HSP90.	[gamma-32p]	144-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
11934275-5	2002	Incubation of the purified HSP90 or HSP90 immunoprecipitated from extracts of human A431 cells, Balb/c 3T3 fibroblasts, and porcine testis with [gamma-32P]ATP/Mg2+ resulted in phosphorylation of HSP90.	[gamma-32p]	144-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
11934275-5	2002	Incubation of the purified HSP90 or HSP90 immunoprecipitated from extracts of human A431 cells, Balb/c 3T3 fibroblasts, and porcine testis with [gamma-32P]ATP/Mg2+ resulted in phosphorylation of HSP90.	Adenosine Triphosphate	155-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
11934275-5	2002	Incubation of the purified HSP90 or HSP90 immunoprecipitated from extracts of human A431 cells, Balb/c 3T3 fibroblasts, and porcine testis with [gamma-32P]ATP/Mg2+ resulted in phosphorylation of HSP90.	magnesium ion	159-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
11934275-6	2002	However, the eluted-HSP90 lost its phosphorylation ability when incubated with [gamma-32P]ATP x Mg2+ alone but could be phosphorylated by various protein kinases, including PKA, CKII, kinase FA/GSK-3 alpha, and AK.	[gamma-32p]atp	79-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11934275-6	2002	However, the eluted-HSP90 lost its phosphorylation ability when incubated with [gamma-32P]ATP x Mg2+ alone but could be phosphorylated by various protein kinases, including PKA, CKII, kinase FA/GSK-3 alpha, and AK.	magnesium ion	96-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11894840-5	2002	GA selectively binds to Hsp90 and inhibits its activity, leading to the loss of steroid receptor activity, and frequently, its degradation.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
11839685-11	2002	We also demonstrate that the Hsp90 inhibitor geldanamycin, which also affects c-Met, reduced the growth and viability of four of four SCLC cell lines by 25% to 85%, over a 72-h time period.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
11839685-12	2002	Geldanamycin caused apoptosis of SCLC cells, as well as led to increased levels of Hsp70 but not Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
11773412-3	2002	The titer of vaccinia intracellular mature virions (IMV) was reduced by 2 orders of magnitude in RK13 cells treated with geldanamycin (GA), which blocks the ATPase activity of Hsp90.	geldanamycin	121-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
11773412-3	2002	The titer of vaccinia intracellular mature virions (IMV) was reduced by 2 orders of magnitude in RK13 cells treated with geldanamycin (GA), which blocks the ATPase activity of Hsp90.	geldanamycin	135-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
11812147-4	2002	It is known that ATP binding and hydrolysis are essential for Hsp90 function in vivo and in vitro.	Adenosine Triphosphate	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
11812147-7	2002	Human Hsp90 is a very weak ATPase, its activity is significantly lower than that of the yeast homologue, and it has a half-life of ATP hydrolysis of eight minutes at 37 degrees C. Using a physiological substrate of Hsp90, the ligand-binding domain of the glucocorticoid receptor, we show that this "client" protein can stimulate the ATPase activity up to 200-fold.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
12127946-0	2002	Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation.	Novobiocin	18-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-84
12127946-0	2002	Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation.	Novobiocin	18-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
12127946-0	2002	Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-84
12127946-0	2002	Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
12127946-6	2002	The N-terminal domain of Hsp90 has been shown to contain an unusual ATP-binding site.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
12127946-7	2002	A well-known inhibitor of Hsp90 function is geldanamycin binding to the N-terminal ATP-binding site with high affinity.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
12127946-7	2002	A well-known inhibitor of Hsp90 function is geldanamycin binding to the N-terminal ATP-binding site with high affinity.	Adenosine Triphosphate	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
12127946-8	2002	Recently it was shown that Hsp90 possesses a second ATP-binding site in the C-terminal region, which can be competed with novobiocin.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
12127946-8	2002	Recently it was shown that Hsp90 possesses a second ATP-binding site in the C-terminal region, which can be competed with novobiocin.	Novobiocin	122-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
11748067-2	2002	Studies have shown that the HSP90-specific inhibitor geldanamycin (GA) can cause attenuation of NO-mediated processes.	geldanamycin	67-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
11748067-10	2002	The results show that GA can attenuate NO-mediated dilation in human skin, suggesting a potential role for HSP90 in activation of eNOS in the microcirculation.	geldanamycin	22-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
12127946-9	2002	Autophosphorylation of Hsp90 was analysed by incubation with gamma(32)P-ATP.	gamma(32)p-atp	61-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
11927289-4	2002	One Hsp90 inhibitor, 17-allylaminogeldanamycin (17AAG), is currently in phase I clinical trial.	tanespimycin	21-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
12127946-11	2002	These results suggest that the C-terminal ATP-binding site is required for autophosphorylation of Hsp90.	Adenosine Triphosphate	42-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
11772336-3	2002	The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11772336-3	2002	The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
11772336-3	2002	The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
11772336-3	2002	The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway.	monorden	54-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11772336-3	2002	The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway.	monorden	54-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
11772336-3	2002	The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway.	monorden	54-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
11927289-4	2002	One Hsp90 inhibitor, 17-allylaminogeldanamycin (17AAG), is currently in phase I clinical trial.	tanespimycin	48-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
11698240-1	2001	Recent studies showed that heat shock protein 90 (HSP90) enhances nitric oxide (NO) synthesis from endothelial and neuronal NO synthase (eNOS and nNOS, respectively).	Nitric Oxide	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-48
11698240-1	2001	Recent studies showed that heat shock protein 90 (HSP90) enhances nitric oxide (NO) synthesis from endothelial and neuronal NO synthase (eNOS and nNOS, respectively).	Nitric Oxide	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
11698240-3	2001	Moreover, although our previous studies showed that the action of HSP90 involves increased Ca(2+)/calmodulin (Ca(2+)/CaM) binding, quantitative measurements of the effect of HSP90 on CaM binding to nNOS have been lacking.	cafestol palmitate	117-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
11698240-6	2001	Tryptophan fluorescence-quenching measurements revealed that HSP90 markedly reduced the K(d) of CaM to nNOS (0.5 +/- 0.1 nM vs. 9.4 +/- 1.8 nM in the presence and absence of HSP90, P < 0.01).	Tryptophan	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
11698240-7	2001	Ca(2+) ionophore triggered strong NO production from nNOS-transfected cells, and this was significantly reduced by the HSP90 inhibitor geldanamycin.	geldanamycin	135-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
11698240-9	2001	The effect of HSP90 is mediated by the enhancement of CaM binding to nNOS.	cafestol palmitate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11800023-15	2001	CONCLUSIONS: These results suggest that inhibition of hsp90 function, which causes depletion of hsp90 client proteins in tumor, contributes to the antitumor activity of KF58333, and that the stereochemistry of the oxime moiety is important for the biological activity of radicicol oxime derivatives.	Oximes	214-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
11800023-1	2001	PURPOSE: Radicicol is a novel hsp90 antagonist, distinct from the chemically unrelated benzoquinone ansamycin compounds, geldanamycin and herbimycin.	monorden	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
11800023-2	2001	Both geldanamycin and radicicol bind in the aminoterminal nucleotide-binding pocket of hsp90, destabilizing the hsp90 client proteins, many of which are essential for tumor cell growth.	geldanamycin	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
11800023-2	2001	Both geldanamycin and radicicol bind in the aminoterminal nucleotide-binding pocket of hsp90, destabilizing the hsp90 client proteins, many of which are essential for tumor cell growth.	geldanamycin	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
11800023-2	2001	Both geldanamycin and radicicol bind in the aminoterminal nucleotide-binding pocket of hsp90, destabilizing the hsp90 client proteins, many of which are essential for tumor cell growth.	monorden	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
11800023-2	2001	Both geldanamycin and radicicol bind in the aminoterminal nucleotide-binding pocket of hsp90, destabilizing the hsp90 client proteins, many of which are essential for tumor cell growth.	monorden	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
11800023-7	2001	Direct binding activity to hsp90 was assessed by hsp90-binding assays using geldanamycin or radicicol beads.	geldanamycin	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
11800023-7	2001	Direct binding activity to hsp90 was assessed by hsp90-binding assays using geldanamycin or radicicol beads.	geldanamycin	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
11800023-7	2001	Direct binding activity to hsp90 was assessed by hsp90-binding assays using geldanamycin or radicicol beads.	monorden	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
11800023-7	2001	Direct binding activity to hsp90 was assessed by hsp90-binding assays using geldanamycin or radicicol beads.	monorden	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
11800023-12	2001	These results are consistent with the ability of KF58333 to deplete hsp90 client proteins and the induction of apoptosis in KPL-4 cells in vitro.	KF58333	49-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
11800023-15	2001	CONCLUSIONS: These results suggest that inhibition of hsp90 function, which causes depletion of hsp90 client proteins in tumor, contributes to the antitumor activity of KF58333, and that the stereochemistry of the oxime moiety is important for the biological activity of radicicol oxime derivatives.	KF58333	169-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
11800023-15	2001	CONCLUSIONS: These results suggest that inhibition of hsp90 function, which causes depletion of hsp90 client proteins in tumor, contributes to the antitumor activity of KF58333, and that the stereochemistry of the oxime moiety is important for the biological activity of radicicol oxime derivatives.	KF58333	169-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
11749701-1	2001	A novel oxime derivative of radicicol, KF58333, binds to the heat shock protein 90 (Hsp90) and destabilizes its associated signaling molecules.	Oximes	8-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-82
11749701-1	2001	A novel oxime derivative of radicicol, KF58333, binds to the heat shock protein 90 (Hsp90) and destabilizes its associated signaling molecules.	Oximes	8-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
11749701-1	2001	A novel oxime derivative of radicicol, KF58333, binds to the heat shock protein 90 (Hsp90) and destabilizes its associated signaling molecules.	monorden	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-82
11749701-1	2001	A novel oxime derivative of radicicol, KF58333, binds to the heat shock protein 90 (Hsp90) and destabilizes its associated signaling molecules.	monorden	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
11749701-1	2001	A novel oxime derivative of radicicol, KF58333, binds to the heat shock protein 90 (Hsp90) and destabilizes its associated signaling molecules.	KF58333	39-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-82
11749701-1	2001	A novel oxime derivative of radicicol, KF58333, binds to the heat shock protein 90 (Hsp90) and destabilizes its associated signaling molecules.	KF58333	39-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
11800023-15	2001	CONCLUSIONS: These results suggest that inhibition of hsp90 function, which causes depletion of hsp90 client proteins in tumor, contributes to the antitumor activity of KF58333, and that the stereochemistry of the oxime moiety is important for the biological activity of radicicol oxime derivatives.	radicicol oxime	271-286	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
11763165-2	2001	Only recently was it discovered that they bind with high specificity within the ADP/ATP binding pocket of the Hsp90 molecular chaperone, thereby inhibiting the function of Hsp90.	Adenosine Diphosphate	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
11707594-3	2001	Geldanamycin and radicicol, ATP-competitive inhibitors of the chaperone HSP90, also inhibit the cleavage of in vitro-synthesized NS2/3.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
11707594-3	2001	Geldanamycin and radicicol, ATP-competitive inhibitors of the chaperone HSP90, also inhibit the cleavage of in vitro-synthesized NS2/3.	monorden	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
11707594-3	2001	Geldanamycin and radicicol, ATP-competitive inhibitors of the chaperone HSP90, also inhibit the cleavage of in vitro-synthesized NS2/3.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
11707401-4	2001	The conformational mutant p53R175H can form a stable heterocomplex with Hsp90 only in the presence of Hsc70, Hsp40, Hop and ATP.	Adenosine Triphosphate	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
11686693-1	2001	Radicicol (1) exhibits potent anticancer properties in vitro, which are likely to be mediated through its high affinity (20 nM) for the molecular chaperone Hsp90.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
11507088-6	2001	Release of MDM2 from the p53-hsp90 complex after DNA damage restores MDM2 but not p53 turnover, whereas dissociation of hsp90 by geldanamycin increases the degradation of both MDM2 and mutant p53.	geldanamycin	129-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
11763165-2	2001	Only recently was it discovered that they bind with high specificity within the ADP/ATP binding pocket of the Hsp90 molecular chaperone, thereby inhibiting the function of Hsp90.	Adenosine Diphosphate	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
11763165-2	2001	Only recently was it discovered that they bind with high specificity within the ADP/ATP binding pocket of the Hsp90 molecular chaperone, thereby inhibiting the function of Hsp90.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
11763165-2	2001	Only recently was it discovered that they bind with high specificity within the ADP/ATP binding pocket of the Hsp90 molecular chaperone, thereby inhibiting the function of Hsp90.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
11763165-6	2001	Hsp90 inhibitors are, therefore, now attracting considerable attention as potential antitumor agents; one geldanamycin derivative is already in phase I trials as an anticancer drug.	geldanamycin	106-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11795466-0	2001	The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor.	Adenosine Triphosphate	15-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
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
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
11795466-2	2001	Hsp90 was either immunoadsorbed to BF4 antibody-Sepharose or GST-Hsp90 fusion protein (GST.90) was adsorbed to glutathione-Sepharose.	Sepharose	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11553774-8	2001	Secondly, the antitumor ATP-mimetic agent geldanamycin, which inhibits the ATPase activity of Hsp-90, did not affect JFC1 ATPase.	Adenosine Triphosphate	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-100
11795466-4	2001	When cells were treated with estradiol and the hormone treatment was maintained during cell homogenization, binding, and washing steps, GST.90 still interacted efficiently with ER, suggesting that ER may form complexes with Hsp90 even after its activation by hormone and salt extraction from nuclei.	Estradiol	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
11795466-5	2001	The GST.90-ER interaction was consistently reduced in the presence of increasing concentrations of potassium chloride or when cytosolic ER-Hsp90 complexes were previously stabilized by molybdate, indicating that GST.90-ER complexes behave like cytosolic Hsp90-ER complexes.	Potassium Chloride	99-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	254-259
11795466-5	2001	The GST.90-ER interaction was consistently reduced in the presence of increasing concentrations of potassium chloride or when cytosolic ER-Hsp90 complexes were previously stabilized by molybdate, indicating that GST.90-ER complexes behave like cytosolic Hsp90-ER complexes.	molybdate	185-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
11795466-8	2001	The N-terminal fragment 1-334, devoid of the dimeric GST moiety, was also able to interact with ER, pointing to the monomeric N-terminal adenosine triphosphate binding region of Hsp90 (1-224) as the region necessary and sufficient for interaction.	Adenosine Triphosphate	137-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
11562278-11	2001	17-Allylaminogeldanamycin targets the Hsp-90 (heat shock protein-90) family of cellular chaperones regulating the function of signaling proteins.	tanespimycin	0-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-44
11562278-11	2001	17-Allylaminogeldanamycin targets the Hsp-90 (heat shock protein-90) family of cellular chaperones regulating the function of signaling proteins.	tanespimycin	0-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
11677264-6	2001	Levels of the stress heat-shock proteins HSP70 and HSP90, and of the anti-apoptotic protein Bcl-2, were increased in neurons exposed to IAA.	Iodoacetic Acid	136-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
11587211-0	2001	The Hsp90 inhibitor geldanamycin selectively sensitizes Bcr-Abl-expressing leukemia cells to cytotoxic chemotherapy.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
11587211-2	2001	Geldanamycin (GA), a drug which destabilizes Hsp90-associated proteins, depletes cells of Bcr-Abl, an Hsp90 client, but not of Abl.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
11587211-2	2001	Geldanamycin (GA), a drug which destabilizes Hsp90-associated proteins, depletes cells of Bcr-Abl, an Hsp90 client, but not of Abl.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
11587211-2	2001	Geldanamycin (GA), a drug which destabilizes Hsp90-associated proteins, depletes cells of Bcr-Abl, an Hsp90 client, but not of Abl.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
11587211-2	2001	Geldanamycin (GA), a drug which destabilizes Hsp90-associated proteins, depletes cells of Bcr-Abl, an Hsp90 client, but not of Abl.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
11553774-8	2001	Secondly, the antitumor ATP-mimetic agent geldanamycin, which inhibits the ATPase activity of Hsp-90, did not affect JFC1 ATPase.	geldanamycin	42-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-100
11441008-0	2001	Coordinated ATP hydrolysis by the Hsp90 dimer.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
11593383-8	2001	Depletion of the dephosphorylated HIF-1alpha, by using the Hsp90 inhibitor geldanamycin A that had little effect on the phosphorylated HIF-1alpha expression, suppressed p53 induction and subsequent apoptosis.	geldanamycin a	75-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
11425855-7	2001	Further experiments in transfected COS cells expressing either wild-type or S1177A mutant eNOS led us to identify the serine 1177 as the critical residue for the hsp90-dependent Akt-mediated activation of eNOS.	Serine	118-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
16200774-1	2001	OBJECTIVE: Using GA (geldanamycine), which specifically binding to HSP90, to induce the imbalance of HSP90/GR in function (low ratio) and analyzing the effect of low HSP90/GR ratio on T lymphocytes apoptosis induced by Dex from asthmatic patients.	Gallium	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
16200774-1	2001	OBJECTIVE: Using GA (geldanamycine), which specifically binding to HSP90, to induce the imbalance of HSP90/GR in function (low ratio) and analyzing the effect of low HSP90/GR ratio on T lymphocytes apoptosis induced by Dex from asthmatic patients.	Gallium	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16200774-1	2001	OBJECTIVE: Using GA (geldanamycine), which specifically binding to HSP90, to induce the imbalance of HSP90/GR in function (low ratio) and analyzing the effect of low HSP90/GR ratio on T lymphocytes apoptosis induced by Dex from asthmatic patients.	Gallium	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16200774-1	2001	OBJECTIVE: Using GA (geldanamycine), which specifically binding to HSP90, to induce the imbalance of HSP90/GR in function (low ratio) and analyzing the effect of low HSP90/GR ratio on T lymphocytes apoptosis induced by Dex from asthmatic patients.	geldanamycine	21-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
16200774-1	2001	OBJECTIVE: Using GA (geldanamycine), which specifically binding to HSP90, to induce the imbalance of HSP90/GR in function (low ratio) and analyzing the effect of low HSP90/GR ratio on T lymphocytes apoptosis induced by Dex from asthmatic patients.	geldanamycine	21-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16200774-1	2001	OBJECTIVE: Using GA (geldanamycine), which specifically binding to HSP90, to induce the imbalance of HSP90/GR in function (low ratio) and analyzing the effect of low HSP90/GR ratio on T lymphocytes apoptosis induced by Dex from asthmatic patients.	geldanamycine	21-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16200774-10	2001	Dex inhibited the expression of HSP90 and GR mRNA of T lymphocytes from asthmatic patients (1.23 +/- 0.16 vs 1.68 +/- 0.38 and 0.42 +/- 0.06 vs 0.54 +/- 0.07, respectively, P all < 0.05).	Dextromethorphan	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
16200774-11	2001	GA could interrupt the inhibiting effect of Dex on the expression of HSP90 and GR mRNA but had no effect on it.	Dextromethorphan	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
16200774-12	2001	CONCLUSION: The low ratio of HSP90/GR could reduce the inducing apoptosis effect of Dex.	Dextromethorphan	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
16200774-13	2001	Dex could down-regulate the mRNA expression of HSP90 and GR and GA could interrupt the inhibiting effect of Dex.	Dextromethorphan	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
16200774-13	2001	Dex could down-regulate the mRNA expression of HSP90 and GR and GA could interrupt the inhibiting effect of Dex.	Dextromethorphan	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
11473354-1	2001	Hsp90 is an ATP dependent molecular chaperone involved in the folding and activation of an unknown number of substrate proteins.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11473354-6	2001	Large ATP-dependent conformational changes of Hsp90 occur during the hydrolysis reaction and these changes are thought to drive the chaperone cycle.	Adenosine Triphosphate	6-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
11473354-7	2001	Natural inhibitors of the ATPase activity, like geldanamycin and radicicol, block the processing of Hsp90 substrate proteins.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
11473354-7	2001	Natural inhibitors of the ATPase activity, like geldanamycin and radicicol, block the processing of Hsp90 substrate proteins.	monorden	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
12580116-0	2001	[Advances in antitumor activity of the hsp90 inhibitor geldanamycin].	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
11504706-2	2001	Inhibition of Hsp90 with geldanamycin suppressed the ability of bacterial lipopolysaccharide to enhance the cell adhesion properties of macrophages, a phenomenon most likely explained by the reduced expression and activity of Hck in macrophages lacking Hsp90 function.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11504706-2	2001	Inhibition of Hsp90 with geldanamycin suppressed the ability of bacterial lipopolysaccharide to enhance the cell adhesion properties of macrophages, a phenomenon most likely explained by the reduced expression and activity of Hck in macrophages lacking Hsp90 function.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	253-258
11489788-1	2001	Commentary re: P. Munster et al., Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner.	Lactams, Macrocyclic	66-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
11489796-0	2001	Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner.	Lactams, Macrocyclic	32-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11489796-3	2001	17-allyl-aminogeldanamycin (17-AAG) is an ansamycin antibiotic that binds to a highly conserved pocket in the Hsp90 chaperone protein and inhibits its function.	tanespimycin	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
11489796-3	2001	17-allyl-aminogeldanamycin (17-AAG) is an ansamycin antibiotic that binds to a highly conserved pocket in the Hsp90 chaperone protein and inhibits its function.	Rifabutin	42-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
11441008-1	2001	The Hsp90 dimer is a molecular chaperone with an unusual N-terminal ATP binding site.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
11441008-4	2001	Here we set out to investigate the correlation between dimerization and ATP hydrolysis by Hsp90.	Adenosine Triphosphate	72-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
11441008-6	2001	Heterodimers of WT Hsp90 with fragments lacking the ATP binding domain form readily and exhibit dimerization constants similar to full-length Hsp90.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
11441008-11	2001	Together, these results suggest a mechanism for coupling the hydrolysis of ATP to the opening-closing movement of the Hsp90 molecular chaperone.	Adenosine Triphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
11447118-4	2001	In mammalian cells, inhibition of Hsp90 function with geldanamycin (GA) during de novo synthesis of PKR also interferes with its accumulation and activity.	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
11447118-4	2001	In mammalian cells, inhibition of Hsp90 function with geldanamycin (GA) during de novo synthesis of PKR also interferes with its accumulation and activity.	geldanamycin	68-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
11447118-7	2001	A short-term exposure of cells to the Hsp90 inhibitors GA or radicicol not only derepresses PKR, but also activates the Raf-MAPK pathway.	monorden	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
11448926-5	2001	We found that interaction of the Hsp90-binding drugs geldanamycin and radicicol with the chaperone destabilizes these hormone receptors in a ligand-independent manner, leading to profound and prolonged depletion of their levels in breast cancer cells cultured in vitro.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
11448926-5	2001	We found that interaction of the Hsp90-binding drugs geldanamycin and radicicol with the chaperone destabilizes these hormone receptors in a ligand-independent manner, leading to profound and prolonged depletion of their levels in breast cancer cells cultured in vitro.	monorden	70-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
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
11394871-0	2001	The protective role of HSP90 against 3-hydroxykynurenine-induced neuronal apoptosis.	3-hydroxykynurenine	37-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
11394871-7	2001	Our results show that the protective effect was abolished by HSP90 anti-sense oligonucleotides while not by HSP27 and HSP70 anti-sense oligonucleotides.	Oligonucleotides	78-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
11278794-4	2001	Treatment of cells with geldanamycin, an HSP90-specific inhibitor, rapidly decreased the protein level of MOK, and the decrease was attributed to enhanced degradation of MOK through proteasome-dependent pathways.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
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
11358819-4	2001	Geldanamycin (GA) is a benzoquinone ansamycin antibiotic that disrupts Hsp90-protein interactions.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
11399505-2	2001	Specifically, our studies addressed whether cortisol exposure modified heat shock protein 90 (HSP90) mRNA expression in rainbow trout (Oncorhynchus mykiss) hepatocytes maintained in primary culture.	Hydrocortisone	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
11399505-8	2001	Our results suggest that elevated plasma cortisol levels modulate the cellular stress response by affecting the transcription of HSP90 in fish.	Hydrocortisone	41-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
11406612-2	2001	Geldanamycin is a benzoquinone ansamycin that binds to the heat shock protein Hsp90 and activates a heat shock response in mammalian cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
11406612-2	2001	Geldanamycin is a benzoquinone ansamycin that binds to the heat shock protein Hsp90 and activates a heat shock response in mammalian cells.	benzoquinone ansamycin	18-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
11406612-3	2001	In this study, we show by using a filter retardation assay and immunofluorescence microscopy that treatment of mammalian cells with geldanamycin at nanomolar concentrations induces the expression of Hsp40, Hsp70 and Hsp90 and inhibits HD exon 1 protein aggregation in a dose-dependent manner.	geldanamycin	132-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	216-221
11358819-4	2001	Geldanamycin (GA) is a benzoquinone ansamycin antibiotic that disrupts Hsp90-protein interactions.	benzoquinone ansamycin	23-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
11351325-7	2001	Inhibition of NOS activity in these ascidian larvae with L-NAME increased the frequency of metamorphosis, consistent with a putative interaction of NOS and HSP90.	NG-Nitroarginine Methyl Ester	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
11360191-7	2001	In addition, UCS15A appeared to differ from src-destabilizing agents such as herbimycin and radicicol that destabilize src by interfering with Hsp90.	herbimycin	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
11360191-7	2001	In addition, UCS15A appeared to differ from src-destabilizing agents such as herbimycin and radicicol that destabilize src by interfering with Hsp90.	monorden	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
11152473-3	2001	When cultured cells expressing recombinant GC-A were treated with geldanamycin, an inhibitor of hsp90 function, the ANP-stimulated production of cyclic GMP was inhibited.	geldanamycin	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
11294389-1	2001	Several LY294002-GM heterodimers were synthesized with the intent of modulating their activity in the presence of hsp90 and thereby creating selective inhibitors of PI3K and PI3K-related family.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	8-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
11399505-0	2001	Cortisol modulates HSP90 mRNA expression in primary cultures of trout hepatocytes.	Hydrocortisone	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
11426058-5	2001	However, in situ labelling experiments along with Western blots revealed that high concentration of hemin (50 microM) reduced the level of protein synthesis in general and of beta-tubulin in particular with a concomitant induction of hsp90, and induced consequent morphological changes that are observed during in situ transformation of promastigotes in mammalian macrophages.	Hemin	100-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
11358818-0	2001	Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis.	tanespimycin	57-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
11358818-1	2001	17-Allylamino-17-demethoxygeldanamycin (17AAG) is a first-in-class heat shock protein 90 (Hsp90) molecular chaperone inhibitor to enter clinical trials.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-88
11237709-4	2001	The Hsp90-specific inhibitor geldanamycin (GA) induced a rapid degradation of Pim-1 and reduced its kinase activity.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
11358818-1	2001	17-Allylamino-17-demethoxygeldanamycin (17AAG) is a first-in-class heat shock protein 90 (Hsp90) molecular chaperone inhibitor to enter clinical trials.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
11358818-1	2001	17-Allylamino-17-demethoxygeldanamycin (17AAG) is a first-in-class heat shock protein 90 (Hsp90) molecular chaperone inhibitor to enter clinical trials.	tanespimycin	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-88
11358818-1	2001	17-Allylamino-17-demethoxygeldanamycin (17AAG) is a first-in-class heat shock protein 90 (Hsp90) molecular chaperone inhibitor to enter clinical trials.	tanespimycin	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
11358819-0	2001	Disruption of the EF-2 kinase/Hsp90 protein complex: a possible mechanism to inhibit glioblastoma by geldanamycin.	geldanamycin	101-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
11358819-4	2001	Geldanamycin (GA) is a benzoquinone ansamycin antibiotic that disrupts Hsp90-protein interactions.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
11237709-4	2001	The Hsp90-specific inhibitor geldanamycin (GA) induced a rapid degradation of Pim-1 and reduced its kinase activity.	geldanamycin	43-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
11347901-1	2001	Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as proto-oncogenic kinases and nuclear receptors.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-134
11347901-1	2001	Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as proto-oncogenic kinases and nuclear receptors.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
11347901-1	2001	Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as proto-oncogenic kinases and nuclear receptors.	benzoquinone ansamycin geldanamycin	24-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-134
11347901-1	2001	Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as proto-oncogenic kinases and nuclear receptors.	benzoquinone ansamycin geldanamycin	24-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
11347901-1	2001	Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as proto-oncogenic kinases and nuclear receptors.	geldanamycin	61-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-134
11347901-1	2001	Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as proto-oncogenic kinases and nuclear receptors.	geldanamycin	61-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
11306353-0	2001	A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells.	Adenine Nucleotides	41-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
11280726-5	2001	By binding and inhibiting Hsp90, GA or 17-AAG treatment shifted the binding of Bcr-Abl from Hsp90 to Hsp70 and induced the proteasomal degradation of Bcr-Abl, because cotreatment with proteasome inhibitor PSC341 reduced both GA (or 17-AAG)-mediated down-regulation of Bcr-Abl levels and inhibited apoptosis of HL-60/Bcr-Abl and K562 cells.	tanespimycin	39-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
11280726-5	2001	By binding and inhibiting Hsp90, GA or 17-AAG treatment shifted the binding of Bcr-Abl from Hsp90 to Hsp70 and induced the proteasomal degradation of Bcr-Abl, because cotreatment with proteasome inhibitor PSC341 reduced both GA (or 17-AAG)-mediated down-regulation of Bcr-Abl levels and inhibited apoptosis of HL-60/Bcr-Abl and K562 cells.	tanespimycin	232-238	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
11306472-1	2001	17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) is an ansamycin antibiotic that binds to a conserved pocket in Hsp90 and induces the degradation of proteins that require this chaperone for conformational maturation.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
11306472-1	2001	17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) is an ansamycin antibiotic that binds to a conserved pocket in Hsp90 and induces the degradation of proteins that require this chaperone for conformational maturation.	Rifabutin	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
11306353-1	2001	BACKGROUND: The Hsp90s contain a conserved pocket that binds ATP/ADP and plays an important role in the regulation of chaperone function.	Adenosine Diphosphate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
11306353-2	2001	Occupancy of this pocket by several natural products (geldanamycin (GM) and radicicol) alters Hsp90 function and results in the degradation of a subset of proteins (i.e. steroid receptors, Her2, Raf).	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
11306353-2	2001	Occupancy of this pocket by several natural products (geldanamycin (GM) and radicicol) alters Hsp90 function and results in the degradation of a subset of proteins (i.e. steroid receptors, Her2, Raf).	geldanamycin	68-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
11306353-2	2001	Occupancy of this pocket by several natural products (geldanamycin (GM) and radicicol) alters Hsp90 function and results in the degradation of a subset of proteins (i.e. steroid receptors, Her2, Raf).	monorden	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
11306353-4	2001	RESULTS: The designed small molecule PU3 competes with GM for Hsp90 binding with a relative affinity of 15-20 microM.	9-BUTYL-8-(3,4,5-TRIMETHOXYBENZYL)-9H-PURIN-6-AMINE	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
11306353-4	2001	RESULTS: The designed small molecule PU3 competes with GM for Hsp90 binding with a relative affinity of 15-20 microM.	geldanamycin	55-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
11306353-7	2001	CONCLUSIONS: PU3 is representative of a novel class of synthetic compounds that binds to Hsp90 and inhibits the proliferation of cancer cells.	9-BUTYL-8-(3,4,5-TRIMETHOXYBENZYL)-9H-PURIN-6-AMINE	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
11306353-1	2001	BACKGROUND: The Hsp90s contain a conserved pocket that binds ATP/ADP and plays an important role in the regulation of chaperone function.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
11071886-12	2001	Hsp90 co-immunoprecipitated with all ErbB2 constructs that were sensitive to GA, but not with ErbB2/DK or ErbB1.	geldanamycin	77-79	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	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
11170435-2	2001	The first event in assembly is the ATP-dependent and hsp40 (YDJ-1)-dependent binding of hsp70 to the GR, which primes the receptor for subsequent ATP-dependent activation by hsp90 [Morishima, Y., Murphy, P. J. M., Li, D. P., Sanchez, E. R., and Pratt, W. B.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
11170435-2	2001	The first event in assembly is the ATP-dependent and hsp40 (YDJ-1)-dependent binding of hsp70 to the GR, which primes the receptor for subsequent ATP-dependent activation by hsp90 [Morishima, Y., Murphy, P. J. M., Li, D. P., Sanchez, E. R., and Pratt, W. B.	Adenosine Triphosphate	146-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
11170435-7	2001	In the second step, hsp90, which is provided in the non-nucleotide-bound state, is converted to GR-bound hsp90 in the ATP-dependent conformation.	Adenosine Triphosphate	118-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
11170435-7	2001	In the second step, hsp90, which is provided in the non-nucleotide-bound state, is converted to GR-bound hsp90 in the ATP-dependent conformation.	Adenosine Triphosphate	118-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
11170435-9	2001	Surprisingly, the subsequent hsp90-dependent step, which is rate-limiting for receptor activation, is also potassium-dependent.	Potassium	107-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
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
11036079-7	2001	The Hsp90-specific inhibitor geldanamycin disrupted the ability of both Hsp90 and p50(cdc37) to bind HRI and promote its activation, but did not disrupt the native association of p50(cdc37) with Hsp90.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
11036079-7	2001	The Hsp90-specific inhibitor geldanamycin disrupted the ability of both Hsp90 and p50(cdc37) to bind HRI and promote its activation, but did not disrupt the native association of p50(cdc37) with Hsp90.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
11036079-7	2001	The Hsp90-specific inhibitor geldanamycin disrupted the ability of both Hsp90 and p50(cdc37) to bind HRI and promote its activation, but did not disrupt the native association of p50(cdc37) with Hsp90.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
11123263-8	2001	HSP90 redistributes in cardiac myocytes after treatment with 17beta-estradiol or progesterone.	Estradiol	61-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11123263-8	2001	HSP90 redistributes in cardiac myocytes after treatment with 17beta-estradiol or progesterone.	Progesterone	81-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11123263-11	2001	Geldanamycin, which inactivates HSP90 and prevents it from binding to receptors, activates HSF-1 and stimulates HSP72 synthesis.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
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
11146632-3	2001	Disruption of Hsp90 heterocomplexes by the Hsp90 inhibitor geldanamycin leads to substrate degradation through the ubiquitin-proteasome pathway, implicating this system in protein triage decisions.	geldanamycin	59-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11146632-3	2001	Disruption of Hsp90 heterocomplexes by the Hsp90 inhibitor geldanamycin leads to substrate degradation through the ubiquitin-proteasome pathway, implicating this system in protein triage decisions.	geldanamycin	59-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
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
11071886-0	2001	Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90.	geldanamycin	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
11071886-3	2001	Although ErbB2 and ErbB1 are highly homologous, they respond quite differently to geldanamycin (GA), an antibiotic that is a specific inhibitor of the chaperone protein Hsp90.	geldanamycin	82-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
11071886-3	2001	Although ErbB2 and ErbB1 are highly homologous, they respond quite differently to geldanamycin (GA), an antibiotic that is a specific inhibitor of the chaperone protein Hsp90.	geldanamycin	96-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
10945979-4	2000	We recently demonstrated that the gyrase inhibitor novobiocin also interacts with Hsp90, altering the affinity of the chaperone for geldanamycin and radicicol and causing in vitro and in vivo depletion of key regulatory Hsp90-dependent kinases including v-Src, Raf-1, and p185(ErbB2).	monorden	149-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
11147836-0	2000	Reactive cysteines of the 90-kDa heat shock protein, Hsp90.	reactive cysteines	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
11147836-2	2000	Its cysteine groups participate in the interactions of Hsp90 with the heme-regulated eIF-2alpha kinase and molybdate, a stabilizer of Hsp90-protein complexes.	Cysteine	4-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
11147836-2	2000	Its cysteine groups participate in the interactions of Hsp90 with the heme-regulated eIF-2alpha kinase and molybdate, a stabilizer of Hsp90-protein complexes.	Cysteine	4-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
11147836-2	2000	Its cysteine groups participate in the interactions of Hsp90 with the heme-regulated eIF-2alpha kinase and molybdate, a stabilizer of Hsp90-protein complexes.	molybdate	107-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
11147836-2	2000	Its cysteine groups participate in the interactions of Hsp90 with the heme-regulated eIF-2alpha kinase and molybdate, a stabilizer of Hsp90-protein complexes.	molybdate	107-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
11147836-4	2000	Our data indicate that Hsp90 as well as two Hsp90 peptides containing Cys-521 and Cys-589/590 are able to reduce cytochrome c.	Peptides	50-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
11147836-4	2000	Our data indicate that Hsp90 as well as two Hsp90 peptides containing Cys-521 and Cys-589/590 are able to reduce cytochrome c.	Cysteine	70-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
11147836-4	2000	Our data indicate that Hsp90 as well as two Hsp90 peptides containing Cys-521 and Cys-589/590 are able to reduce cytochrome c.	Cysteine	70-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
11147836-4	2000	Our data indicate that Hsp90 as well as two Hsp90 peptides containing Cys-521 and Cys-589/590 are able to reduce cytochrome c.	Cysteine	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
11147836-4	2000	Our data indicate that Hsp90 as well as two Hsp90 peptides containing Cys-521 and Cys-589/590 are able to reduce cytochrome c.	Cysteine	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
11147836-5	2000	The effect of Hsp90 can be blocked by sulfhydryl reagents including arsenite and cadmium, which indicates the involvement of the vicinal cysteines Cys589/590 in the reduction of cytochrome c.	arsenite	68-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11147836-5	2000	The effect of Hsp90 can be blocked by sulfhydryl reagents including arsenite and cadmium, which indicates the involvement of the vicinal cysteines Cys589/590 in the reduction of cytochrome c.	Cadmium	81-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11147836-5	2000	The effect of Hsp90 can be blocked by sulfhydryl reagents including arsenite and cadmium, which indicates the involvement of the vicinal cysteines Cys589/590 in the reduction of cytochrome c.	Cysteine	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
11147836-6	2000	Hsp90 neither reduces the disulfide bonds of insulin nor possesses a NADPH:quinone oxidoreductase activity.	NADP	69-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11147836-8	2000	The high and specific reactivity of Hsp90 cysteine groups toward cytochrome c may indicate a role of this chaperone in modulation of the redox status of the cytosol in resting and apoptotic cells.	Cysteine	42-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10945979-0	2000	The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone.	Novobiocin	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
10945979-0	2000	The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
10945979-2	2000	The amino terminus of Hsp90 contains a non-conventional nucleotide-binding site, related to the ATP-binding motif of bacterial DNA gyrase.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
10945979-5	2000	In the present study we used deletion/mutation analysis to identify the site of interaction of novobiocin with Hsp90, and we demonstrate that the novobiocin-binding site resides in the carboxyl terminus of the chaperone.	Novobiocin	95-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
10945979-3	2000	The anti-tumor agents geldanamycin and radicicol bind specifically at this site and induce destabilization of Hsp90-dependent client proteins.	geldanamycin	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
10945979-3	2000	The anti-tumor agents geldanamycin and radicicol bind specifically at this site and induce destabilization of Hsp90-dependent client proteins.	monorden	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
10945979-6	2000	Surprisingly, this motif also recognizes ATP, and ATP and novobiocin efficiently compete with each other for binding to this region of Hsp90.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
10945979-4	2000	We recently demonstrated that the gyrase inhibitor novobiocin also interacts with Hsp90, altering the affinity of the chaperone for geldanamycin and radicicol and causing in vitro and in vivo depletion of key regulatory Hsp90-dependent kinases including v-Src, Raf-1, and p185(ErbB2).	Novobiocin	51-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
10945979-4	2000	We recently demonstrated that the gyrase inhibitor novobiocin also interacts with Hsp90, altering the affinity of the chaperone for geldanamycin and radicicol and causing in vitro and in vivo depletion of key regulatory Hsp90-dependent kinases including v-Src, Raf-1, and p185(ErbB2).	Novobiocin	51-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
10945979-6	2000	Surprisingly, this motif also recognizes ATP, and ATP and novobiocin efficiently compete with each other for binding to this region of Hsp90.	Adenosine Triphosphate	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
10945979-4	2000	We recently demonstrated that the gyrase inhibitor novobiocin also interacts with Hsp90, altering the affinity of the chaperone for geldanamycin and radicicol and causing in vitro and in vivo depletion of key regulatory Hsp90-dependent kinases including v-Src, Raf-1, and p185(ErbB2).	geldanamycin	132-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
10945979-6	2000	Surprisingly, this motif also recognizes ATP, and ATP and novobiocin efficiently compete with each other for binding to this region of Hsp90.	Novobiocin	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
10945979-7	2000	Novobiocin interferes with association of the co-chaperones Hsc70 and p23 with Hsp90.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
11054293-1	2000	Hsp90 is an abundant molecular chaperone that functions in an ATP-dependent manner in vivo.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
11050175-1	2000	Heat shock protein (hsp)90 functions in a complex chaperoning pathway where its activity is modulated by ATP and by interaction with several co-chaperones.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-26
11050175-2	2000	One co-chaperone, p23, binds selectively to the ATP-bound state of hsp90.	Adenosine Triphosphate	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
11050175-3	2000	However, the isolated ATP-binding domain of hsp90 does not bind p23.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
11054293-2	2000	The ATP-binding site is located in the N-terminal domain of Hsp90.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
11054293-4	2000	We find that Hsp90 binds ATP with a two-step mechanism.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
11054293-7	2000	In the isolated ATP-binding domain of Hsp90, however, the bound ATP was not committed and the turnover numbers were markedly reduced.	Adenosine Triphosphate	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
11054293-7	2000	In the isolated ATP-binding domain of Hsp90, however, the bound ATP was not committed and the turnover numbers were markedly reduced.	Adenosine Triphosphate	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
11054293-8	2000	Analysis of a series of truncation mutants of Hsp90 showed that C-terminal regions far apart in sequence from the ATP-binding domain are essential for trapping the bound ATP and for maximum hydrolysis rates.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
11054293-8	2000	Analysis of a series of truncation mutants of Hsp90 showed that C-terminal regions far apart in sequence from the ATP-binding domain are essential for trapping the bound ATP and for maximum hydrolysis rates.	Adenosine Triphosphate	170-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
11054293-9	2000	Our results suggest that ATP binding and hydrolysis drive conformational changes that involve the entire molecule and lead to repositioning of the N and C-terminal domains of Hsp90.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
11060043-0	2000	Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
11205268-9	2000	The inhibition of hsp90 expression was not found eiyher at 50 mM or 100 mM of quercetin exposure.	Quercetin	78-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
11060043-1	2000	The molecular chaperone Hsp90 binds and hydrolyses ATP, but how this ATPase activity regulates the interaction of Hsp90 with a polypeptide substrate is not yet understood.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
11060043-1	2000	The molecular chaperone Hsp90 binds and hydrolyses ATP, but how this ATPase activity regulates the interaction of Hsp90 with a polypeptide substrate is not yet understood.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
11060043-2	2000	Using the glucocorticoid receptor ligand binding domain as a substrate, we show that dissociation of Hsp90 from bound polypeptide depends on the Hsp90 ATPase and is blocked by geldanamycin, a specific ATPase inhibitor.	geldanamycin	176-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
11060043-2	2000	Using the glucocorticoid receptor ligand binding domain as a substrate, we show that dissociation of Hsp90 from bound polypeptide depends on the Hsp90 ATPase and is blocked by geldanamycin, a specific ATPase inhibitor.	geldanamycin	176-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
11060043-3	2000	The co-chaperone p23 greatly stimulates Hsp90 substrate release with ATP, but not with the non-hydrolysable nucleotides ATPgammaS or AMP-PNP.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
11060043-4	2000	Point mutants of Hsp90 with progressively lower ATPase rates are progressively slower in ATP-dependent substrate release but are still regulated by p23.	Adenosine Triphosphate	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
11060043-6	2000	These results outline an ATP-driven cycle of substrate binding and release for Hsp90 which differs from that of other ATP-driven chaperones.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
11060043-6	2000	These results outline an ATP-driven cycle of substrate binding and release for Hsp90 which differs from that of other ATP-driven chaperones.	Adenosine Triphosphate	118-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
11060043-7	2000	Conversion of the ATP state of Hsp90 to the ADP state through hydrolysis is required for efficient release of substrate polypeptide.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
11060043-7	2000	Conversion of the ATP state of Hsp90 to the ADP state through hydrolysis is required for efficient release of substrate polypeptide.	Adenosine Diphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
10944121-3	2000	C-terminal truncation mutants lacking inherent dimerization displayed reduced ATPase activity, but dimerized in the presence of 5"-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted association of N-termini in intact Hsp90 dimers was demonstrated.	Adenylyl Imidodiphosphate	170-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
10913161-3	2000	This interaction was sensitive to the hsp90 inhibitor, geldanamycin, and also ATP, suggesting that the chaperone activity of hsp90 is required for interaction with EPRS.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
10913161-3	2000	This interaction was sensitive to the hsp90 inhibitor, geldanamycin, and also ATP, suggesting that the chaperone activity of hsp90 is required for interaction with EPRS.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
10913161-3	2000	This interaction was sensitive to the hsp90 inhibitor, geldanamycin, and also ATP, suggesting that the chaperone activity of hsp90 is required for interaction with EPRS.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
10913161-3	2000	This interaction was sensitive to the hsp90 inhibitor, geldanamycin, and also ATP, suggesting that the chaperone activity of hsp90 is required for interaction with EPRS.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
10979978-0	2000	Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex.	Oximes	6-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
10979978-0	2000	Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex.	monorden	27-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
10979978-2	2000	Radicicol, a macrocyclic antifungal antibiotic, binds to the N-terminal of heat shock protein 90 (Hsp90) and destabilizes Hsp90-associated proteins such as Raf-1.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
10979978-2	2000	Radicicol, a macrocyclic antifungal antibiotic, binds to the N-terminal of heat shock protein 90 (Hsp90) and destabilizes Hsp90-associated proteins such as Raf-1.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
10979978-2	2000	Radicicol, a macrocyclic antifungal antibiotic, binds to the N-terminal of heat shock protein 90 (Hsp90) and destabilizes Hsp90-associated proteins such as Raf-1.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
10979978-8	2000	Immunoprecipitation analysis showed that p210(Bcr-Abl) formed multiple complexes with Hsp90, some containing p23 and others Hsp70; KF58333 treatment dissociated p210(Bcr-Abl) from Hsp90/p23 chaperone complexes.	KF58333	131-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
10979978-8	2000	Immunoprecipitation analysis showed that p210(Bcr-Abl) formed multiple complexes with Hsp90, some containing p23 and others Hsp70; KF58333 treatment dissociated p210(Bcr-Abl) from Hsp90/p23 chaperone complexes.	KF58333	131-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
10983853-1	2000	When tested on Suc-Leu-Leu-Val-Tyr-MCA as substrate, purified full-length hsp90 displays a low "chymotrypsin-like" peptidase activity which is activated by Ca++ and Mg++ ions.	Suc-Leu-Leu-Val-Tyr	15-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
10983853-1	2000	When tested on Suc-Leu-Leu-Val-Tyr-MCA as substrate, purified full-length hsp90 displays a low "chymotrypsin-like" peptidase activity which is activated by Ca++ and Mg++ ions.	Magnesium	165-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
11074940-4	2000	Polyacrylamide gel electrophoresis of [(35)S]methionine-labeled proteins showed transient induction of hsp47 within 4 h, and increased synthesis of hsp90 and GRP78 and other unidentified proteins at 24 h, but no change in hsp70.	polyacrylamide	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
11074940-4	2000	Polyacrylamide gel electrophoresis of [(35)S]methionine-labeled proteins showed transient induction of hsp47 within 4 h, and increased synthesis of hsp90 and GRP78 and other unidentified proteins at 24 h, but no change in hsp70.	Methionine	45-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
10962573-0	2000	Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone.	tanespimycin	101-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
10962573-2	2000	One of these is the novel agent 17-allylamino-17-demethoxygeldanamycin that acts to inhibit the hsp90 molecular chaperone.	tanespimycin	32-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
10816561-0	2000	Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94.	adenosine nucleotide	27-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
10983842-4	2000	We also show that Hsp90 and HSJ1b transfer alpha-lactalbumin to each other in an ATP-dependent manner.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
10919839-6	2000	HSP90 contributes critically to the maturation of steroid hormone receptors and may thus be a critical determinant of the aldosterone sensitivity of specific renal epithelial cells.	Aldosterone	122-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
10946823-7	2000	Hsp 90 as well as hsp 72 might be involved in the proliferation of human PBMC to mercuric chloride.	Mercuric Chloride	81-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-6
10816560-0	2000	Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94.	adenosine nucleotide	27-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	adenosine nucleotide	72-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	adenosine nucleotide	72-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
10816561-3	2000	X-ray crystallographic studies of the N-terminal domain of Hsp90 have identified an unconventional ATP binding fold, thereby inferring a role for ATP in the regulation of the Hsp90 activity.	Adenosine Triphosphate	99-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	geldanamycin	170-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10816561-3	2000	X-ray crystallographic studies of the N-terminal domain of Hsp90 have identified an unconventional ATP binding fold, thereby inferring a role for ATP in the regulation of the Hsp90 activity.	Adenosine Triphosphate	99-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	geldanamycin	170-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
10816561-3	2000	X-ray crystallographic studies of the N-terminal domain of Hsp90 have identified an unconventional ATP binding fold, thereby inferring a role for ATP in the regulation of the Hsp90 activity.	Adenosine Triphosphate	146-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	monorden	187-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10816561-3	2000	X-ray crystallographic studies of the N-terminal domain of Hsp90 have identified an unconventional ATP binding fold, thereby inferring a role for ATP in the regulation of the Hsp90 activity.	Adenosine Triphosphate	146-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	monorden	187-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
10816560-4	2000	Although this domain is essential for Hsp90 function, the molecular basis for adenosine nucleotide-dependent regulation of GRP94, the endoplasmic reticulum paralog of Hsp90, remains to be established.	adenosine nucleotide	78-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
10816561-4	2000	In this report, N-ethylcarboxamidoadenosine (NECA) was used to investigate the nucleotide binding properties of GRP94, the endoplasmic reticulum paralog of Hsp90.	Adenosine-5'-(N-ethylcarboxamide)	16-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
10816561-4	2000	In this report, N-ethylcarboxamidoadenosine (NECA) was used to investigate the nucleotide binding properties of GRP94, the endoplasmic reticulum paralog of Hsp90.	Adenosine-5'-(N-ethylcarboxamide)	45-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
10858314-5	2000	The hsp90 inhibitor geldanamycin does not directly disrupt the native association of hsp90 with p50(cdc37) per se, but does result in the formation of salt-labile hsp90-kinase heterocomplexes which lack the p50(cdc37) cohort.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
10919672-0	2000	Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent G1 arrest.	Lactams, Macrocyclic	32-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	herbimycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	herbimycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	herbimycin	41-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	herbimycin	41-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	geldanamycin	63-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
10919672-1	2000	The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90) and alter the function of this chaperone protein.	geldanamycin	63-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
10811633-8	2000	Geldanamycin had no effect on the reconstituted activity but partially reduced the stimulated activity of the reconstituted telomerase by the TIG3 cell extract, suggesting that Hsp90 may contribute to the stimulatory effect of the cellular components.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
10898951-6	2000	Geldanamycin, a specific inhibitor of hsp90, inhibited the degradation of microsomal CYP2E1 by the cytosol fraction.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
10898951-14	2000	The sensitivity to geldanamycin and molybdate and the immunodepletion experiments suggest that hsp90 is one of these factors that interact with CYP2E1 and/or with the proteasome to promote the degradation of this microsomal P450.	geldanamycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
10898951-14	2000	The sensitivity to geldanamycin and molybdate and the immunodepletion experiments suggest that hsp90 is one of these factors that interact with CYP2E1 and/or with the proteasome to promote the degradation of this microsomal P450.	molybdate	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
10939589-3	2000	Benzoquinone ansamycins also bind to and inhibit the activity of Hsp90.	benzoquinone ansamycins	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
10939589-5	2000	Brief exposure to the benzoquinone ansamycin Hsp90 inhibitor geldanamycin (GA) decreases the association of p210bcr-abl with Hsp90 and p23 and increases its association with the chaperones Hsp70 and p60Hop.	benzoquinone ansamycin	22-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
10939589-5	2000	Brief exposure to the benzoquinone ansamycin Hsp90 inhibitor geldanamycin (GA) decreases the association of p210bcr-abl with Hsp90 and p23 and increases its association with the chaperones Hsp70 and p60Hop.	benzoquinone ansamycin	22-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
10939589-5	2000	Brief exposure to the benzoquinone ansamycin Hsp90 inhibitor geldanamycin (GA) decreases the association of p210bcr-abl with Hsp90 and p23 and increases its association with the chaperones Hsp70 and p60Hop.	geldanamycin	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
10939589-5	2000	Brief exposure to the benzoquinone ansamycin Hsp90 inhibitor geldanamycin (GA) decreases the association of p210bcr-abl with Hsp90 and p23 and increases its association with the chaperones Hsp70 and p60Hop.	geldanamycin	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
10939589-5	2000	Brief exposure to the benzoquinone ansamycin Hsp90 inhibitor geldanamycin (GA) decreases the association of p210bcr-abl with Hsp90 and p23 and increases its association with the chaperones Hsp70 and p60Hop.	geldanamycin	75-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
10939589-5	2000	Brief exposure to the benzoquinone ansamycin Hsp90 inhibitor geldanamycin (GA) decreases the association of p210bcr-abl with Hsp90 and p23 and increases its association with the chaperones Hsp70 and p60Hop.	geldanamycin	75-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
10939589-6	2000	GA has a similar effect on chaperone association with v-src, another Hsp90-dependent oncogenic kinase.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
10939589-7	2000	Loss of Hsp90/p23 association and acquisition of Hsp70/p60Hop association of both p210bcr-abl and v-src precede GA-induced degradation of these kinases.	geldanamycin	112-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
10858314-5	2000	The hsp90 inhibitor geldanamycin does not directly disrupt the native association of hsp90 with p50(cdc37) per se, but does result in the formation of salt-labile hsp90-kinase heterocomplexes which lack the p50(cdc37) cohort.	Salts	151-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
10751404-4	2000	Mutation of Glu-729, Glu-730, and Asp-732 at the C terminus of hsp90 interfered with binding of all three TPR proteins.	Glutamic Acid	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
10751385-1	2000	It is established that suicide inactivation of neuronal nitric-oxide synthase (nNOS) with guanidine compounds, or inhibition of the hsp90-based chaperone system with geldanamycin, leads to the enhanced proteolytic degradation of nNOS.	geldanamycin	166-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
10751404-4	2000	Mutation of Glu-729, Glu-730, and Asp-732 at the C terminus of hsp90 interfered with binding of all three TPR proteins.	Glutamic Acid	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
10751404-4	2000	Mutation of Glu-729, Glu-730, and Asp-732 at the C terminus of hsp90 interfered with binding of all three TPR proteins.	Aspartic Acid	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
10751404-6	2000	Mutation of Glu-651 and Asp-653 did not affect binding of FKBP52 or PP5 but inhibited both Hop binding and hsp90 chaperone activity.	Glutamic Acid	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
10751404-6	2000	Mutation of Glu-651 and Asp-653 did not affect binding of FKBP52 or PP5 but inhibited both Hop binding and hsp90 chaperone activity.	Aspartic Acid	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
10751404-7	2000	We also found that a conserved Lys residue required for PP5 binding to hsp90 was critical for the binding of FKBP52 but not for the binding of Hop to hsp90.	Lysine	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
10835326-7	2000	Incubation of PAEC with a specific inhibitor of HSP90 (geldanamycin) mimicked the hypoxic decrease of eNOS activity.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
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.	Adenosine Triphosphate	91-94	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.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
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
10764743-8	2000	hsp90 is required for opening of the steroid binding pocket and is converted to its ATP-dependent conformation during this second step.	Adenosine Triphosphate	84-87	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.	Adenosine Triphosphate	186-189	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
10744744-5	2000	Here we report that RIP is a novel Hsp90-associated kinase and that disruption of Hsp90 function by its specific inhibitor, geldanamycin (GA), selectively causes RIP degradation and the subsequent inhibition of TNF-mediated IkappaB kinase and NF-kappaB activation.	geldanamycin	124-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
10938455-6	2000	In lymphocytes isolated from individuals receiving antioxidant supplements and subjected to a heat shock in the presence of the free radical generator 2, 2"-azobis-(2-amidinopropane)-dihydrochloride, enhanced synthesis of heat shock proteins hsp 105, hsp 90, hsp 70, and hsp 40 by contrast with decreased synthesis of heme oxygenase HO-1 (hsp 32) were noted.	Free Radicals	128-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	251-257
10938455-6	2000	In lymphocytes isolated from individuals receiving antioxidant supplements and subjected to a heat shock in the presence of the free radical generator 2, 2"-azobis-(2-amidinopropane)-dihydrochloride, enhanced synthesis of heat shock proteins hsp 105, hsp 90, hsp 70, and hsp 40 by contrast with decreased synthesis of heme oxygenase HO-1 (hsp 32) were noted.	2,2'-azobis(2-amidinopropane)	151-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	251-257
10793137-4	2000	Using specific inhibitors of Hsp90, geldanamycin and radicicol, we found that functional Hsp90 is essential for the stability of newly synthesized, but not mature, Lck.	geldanamycin	36-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
10793137-4	2000	Using specific inhibitors of Hsp90, geldanamycin and radicicol, we found that functional Hsp90 is essential for the stability of newly synthesized, but not mature, Lck.	monorden	53-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
10793137-6	2000	In contrast, LckY505F and LckDeltaSH2, constitutively active Lck mutants lacking the C-terminal regulatory tyrosine or the entire Src homology 2 domain, respectively, required Hsp90 activity to stabilize the mature proteins.	Tyrosine	107-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
10938586-6	2000	The results obtained show that the 41 degrees C stress leads to formation of intermolecular disulfide bonds between apo-GR and associated heat shock proteins (Hsp90, Hsp70).	Disulfides	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
10744744-5	2000	Here we report that RIP is a novel Hsp90-associated kinase and that disruption of Hsp90 function by its specific inhibitor, geldanamycin (GA), selectively causes RIP degradation and the subsequent inhibition of TNF-mediated IkappaB kinase and NF-kappaB activation.	geldanamycin	124-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
10744744-5	2000	Here we report that RIP is a novel Hsp90-associated kinase and that disruption of Hsp90 function by its specific inhibitor, geldanamycin (GA), selectively causes RIP degradation and the subsequent inhibition of TNF-mediated IkappaB kinase and NF-kappaB activation.	geldanamycin	138-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
10744744-5	2000	Here we report that RIP is a novel Hsp90-associated kinase and that disruption of Hsp90 function by its specific inhibitor, geldanamycin (GA), selectively causes RIP degradation and the subsequent inhibition of TNF-mediated IkappaB kinase and NF-kappaB activation.	geldanamycin	138-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
10822011-5	2000	To analyze the role of mammalian Hsp90, we synthesized the human ER in rabbit reticulocyte lysates containing geldanamycin, an Hsp90 inhibitor.	geldanamycin	110-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
10851302-8	2000	CONCLUSION: Hydrogen peroxide-induced renal cell death involves increased lipid peroxidation and partial degradation of Hsp90.	Hydrogen Peroxide	12-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
10851302-9	2000	Both pyruvate and NAC are capable of detoxifying H(2)O(2) to maintain cell viability and Hsp90 integrity.	Pyruvic Acid	5-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
10851302-9	2000	Both pyruvate and NAC are capable of detoxifying H(2)O(2) to maintain cell viability and Hsp90 integrity.	Acetylcysteine	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
10851302-9	2000	Both pyruvate and NAC are capable of detoxifying H(2)O(2) to maintain cell viability and Hsp90 integrity.	Hydrogen Peroxide	49-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
10716925-5	2000	Disruption of Hsp90 function by mutations in the Drosophila gene or treatment of mammalian cells with the Hsp90 inhibitor geldanamycin, results in abnormal centrosome separation and maturation, aberrant spindles and impaired chromosome segregation.	geldanamycin	122-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
10706677-1	2000	The benzoquinoid ansamycins geldanamycin (GA), herbimycin, and their derivatives are emerging as novel therapeutic agents that act by inhibiting the 90-kDa heat-shock protein hsp90.	benzoquinoid ansamycins	4-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
10706677-1	2000	The benzoquinoid ansamycins geldanamycin (GA), herbimycin, and their derivatives are emerging as novel therapeutic agents that act by inhibiting the 90-kDa heat-shock protein hsp90.	geldanamycin	28-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
10706677-1	2000	The benzoquinoid ansamycins geldanamycin (GA), herbimycin, and their derivatives are emerging as novel therapeutic agents that act by inhibiting the 90-kDa heat-shock protein hsp90.	geldanamycin	42-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
10798494-0	2000	The decline of porcine sperm motility by geldanamycin, a specific inhibitor of heat-shock protein 90 (HSP90).	geldanamycin	41-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
10706677-1	2000	The benzoquinoid ansamycins geldanamycin (GA), herbimycin, and their derivatives are emerging as novel therapeutic agents that act by inhibiting the 90-kDa heat-shock protein hsp90.	herbimycin	47-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
10798494-6	2000	An HSP90-specific inhibitor, geldanamycin (GA), was added to diluted semen at 0.5, 1.0, 2.5 or 5.0 microg/mL and the semen was then incubated at 37 degrees C for 15, 30, 45 or 60 min.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
10798494-6	2000	An HSP90-specific inhibitor, geldanamycin (GA), was added to diluted semen at 0.5, 1.0, 2.5 or 5.0 microg/mL and the semen was then incubated at 37 degrees C for 15, 30, 45 or 60 min.	geldanamycin	43-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
10723140-7	2000	LT-HSP90 complexes can be reconstituted from purified HSP90 and unfolded-LT in vitro in an ATP-independent manner but not from HSP90 and native LT, suggesting that non-mature conformation of LT is required for the efficient association with HSP90.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
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
10877126-0	2000	Exposure of human keratinocytes and fibroblasts in vitro to nickel sulphate ions induces synthesis of stress proteins Hsp72 and Hsp90.	nickel sulfate	60-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
10723140-8	2000	Moreover, geldanamycin, an anti-tumor drug that specifically binds and inhibits HSP90, reduced the intracellular concentration of LT by destabilizing newly synthesized LT.	geldanamycin	10-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
10671543-6	2000	These benzoquinone ansamycins are potent inhibitors of Hsp90 function, which has recently been shown to play a role in stimulus-dependent eNOS activation.	benzoquinone ansamycins	6-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
10652318-8	2000	However, TRAP1 is sufficiently conserved with hsp90 such that it bound ATP, and this binding was sensitive to the hsp90 inhibitor geldanamycin.	Adenosine Triphosphate	71-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
10652318-8	2000	However, TRAP1 is sufficiently conserved with hsp90 such that it bound ATP, and this binding was sensitive to the hsp90 inhibitor geldanamycin.	geldanamycin	130-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
10642522-6	2000	Dynamics of hsp90-p60 complex formation is modulated by ATP through changes in the co-operativity of interaction.	Adenosine Triphosphate	56-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
10746741-0	2000	Trichostatin A modulates expression of p21waf1/cip1, Bcl-xL, ID1, ID2, ID3, CRAB2, GATA-2, hsp86 and TFIID/TAFII31 mRNA in human lung adenocarcinoma cells.	trichostatin A	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
10640428-8	2000	Inhibitors of the intracellular signaling molecules, phosphatidylinositol 3-kinase with wortmannin, hsp90-dependent kinases with geldanamycin, and calpain with calpeptin, but not MAPKK with PD98059, reduced the high spontaneous adhesion and migration of the M21 cells to BSP, consistent with the constitutive activation of the receptor on these tumor cells.	geldanamycin	129-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
10634927-2	2000	It was observed that HSP 90, HSP 72 and HSP 27 are significantly over-expressed after exposure to cadmium chloride for 24 h. Low cadmium concentrations (i.e. from 1 to 10 microM) also triggered a slight accumulation of glutathione, whereas this compound was depleted after exposure to higher cadmium concentrations (25-100 microM).	Cadmium Chloride	98-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-27
10718371-3	2000	We found that HSP90 showed remarkably high expression in undifferentiated human embryonal carcinoma (EC) cells, which were subsequently dramatically down-regulated during in vitro cellular differentiation, following retinoic acid (RA) treatment, at the protein level.	Tretinoin	216-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
10718371-3	2000	We found that HSP90 showed remarkably high expression in undifferentiated human embryonal carcinoma (EC) cells, which were subsequently dramatically down-regulated during in vitro cellular differentiation, following retinoic acid (RA) treatment, at the protein level.	Tretinoin	231-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
10718371-8	2000	We showed that the RA-induced differentiation of EC cells into a neural cell lineage was inhibited by overexpression of the HSP90alpha or -beta isoform via the gene transfer method.	Tretinoin	19-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-134
10744763-6	2000	Geldanamycin, an inhibitor of HSP90 blocked tyrosine phosphorylation of FAK, assembly of focal adhesions, actin reorganization, and cell migration, all of which were reversed by overexpressing HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
10744763-6	2000	Geldanamycin, an inhibitor of HSP90 blocked tyrosine phosphorylation of FAK, assembly of focal adhesions, actin reorganization, and cell migration, all of which were reversed by overexpressing HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
10744763-6	2000	Geldanamycin, an inhibitor of HSP90 blocked tyrosine phosphorylation of FAK, assembly of focal adhesions, actin reorganization, and cell migration, all of which were reversed by overexpressing HSP90.	Tyrosine	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
10744763-6	2000	Geldanamycin, an inhibitor of HSP90 blocked tyrosine phosphorylation of FAK, assembly of focal adhesions, actin reorganization, and cell migration, all of which were reversed by overexpressing HSP90.	Tyrosine	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
10645006-7	2000	In addition, both Cys483/Cyr487 and Cys496/Cys498 kinases became resistant to in vitro inactivation by herbimycin A, which directly inactivates v-Src in addition to its effect on HSP90.	herbimycin	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
10634927-2	2000	It was observed that HSP 90, HSP 72 and HSP 27 are significantly over-expressed after exposure to cadmium chloride for 24 h. Low cadmium concentrations (i.e. from 1 to 10 microM) also triggered a slight accumulation of glutathione, whereas this compound was depleted after exposure to higher cadmium concentrations (25-100 microM).	Cadmium	98-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-27
10634927-2	2000	It was observed that HSP 90, HSP 72 and HSP 27 are significantly over-expressed after exposure to cadmium chloride for 24 h. Low cadmium concentrations (i.e. from 1 to 10 microM) also triggered a slight accumulation of glutathione, whereas this compound was depleted after exposure to higher cadmium concentrations (25-100 microM).	Glutathione	219-230	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-27
10634927-2	2000	It was observed that HSP 90, HSP 72 and HSP 27 are significantly over-expressed after exposure to cadmium chloride for 24 h. Low cadmium concentrations (i.e. from 1 to 10 microM) also triggered a slight accumulation of glutathione, whereas this compound was depleted after exposure to higher cadmium concentrations (25-100 microM).	Cadmium	129-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-27
10634927-3	2000	When 50 microM diethyl-maleate, which traps glutathione, was added together with cadmium, the over-expression of HSP 72 and HSP 90 was much stronger.	diethyl maleate	15-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-130
10634927-3	2000	When 50 microM diethyl-maleate, which traps glutathione, was added together with cadmium, the over-expression of HSP 72 and HSP 90 was much stronger.	Glutathione	44-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-130
10634927-3	2000	When 50 microM diethyl-maleate, which traps glutathione, was added together with cadmium, the over-expression of HSP 72 and HSP 90 was much stronger.	Cadmium	81-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-130
15687592-1	2000	Several natural product antibiotics, including herbimycin, geldanamycin, and radicicol, bind to an amino terminal nucleotide binding pocket in the heat shock protein Hsp90.	herbimycin	47-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
10617616-8	2000	Pharmacological inactivation of Hsp90/Cdc37 function by geldanamycin revealed an essential role for the chaperone-Cdk9 complexes in generation of Cdk9/cyclin T1.	geldanamycin	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
10617616-9	2000	Our data suggest a previously unrecognized chaperone-dependent pathway involving the sequential actions of Hsp70 and Hsp90/Cdc37 in the stabilization/folding of Cdk9 as well as the assembly of an active Cdk9/cyclin T1 complex responsible for P-TEFb-mediated Tat transactivation.	Phosphorus	242-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
15687592-1	2000	Several natural product antibiotics, including herbimycin, geldanamycin, and radicicol, bind to an amino terminal nucleotide binding pocket in the heat shock protein Hsp90.	geldanamycin	59-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
15687592-1	2000	Several natural product antibiotics, including herbimycin, geldanamycin, and radicicol, bind to an amino terminal nucleotide binding pocket in the heat shock protein Hsp90.	monorden	77-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
10731632-8	2000	Short treatment of cells with the hsp90 inhibitor geldanamycin (GA) did not prevent nuclear translocation of GR.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
10701840-0	2000	The Hsp90-specific inhibitor geldanamycin selectively disrupts kinase-mediated signaling events of T-lymphocyte activation.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
10701840-3	2000	Improper function of these proteins can be induced by selective disruption of their complexes with Hsp90 using the benzoquinonoid ansamycin geldanamycin.	benzoquinonoid ansamycin geldanamycin	115-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
10701840-8	2000	Through demonstrating the selective inhibition of kinase-related T-lymphocyte responses by geldanamycin, our results emphasize the substantial role of Hsp90-kinase complexes in T-cell activation.	geldanamycin	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
10731632-10	2000	The GA-induced transcriptional shutdown was also observed for other nuclear receptors which do not interact stably with hsp90.	geldanamycin	4-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
10574997-1	1999	It has been reported that immunosuppressant cyclosporin A or FK506 binds to immunophilins in the cell and that these immunophilins make a complex with molecular chaperones HSP70 or HSP90.	Cyclosporine	44-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
10574997-1	1999	It has been reported that immunosuppressant cyclosporin A or FK506 binds to immunophilins in the cell and that these immunophilins make a complex with molecular chaperones HSP70 or HSP90.	Tacrolimus	61-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
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
10581266-9	1999	Hsp90 complexes are required for CDK regulation; the synergy found between the excess of Wos2 and a deficiency in Hsp90 activity suggests that Wos2 could specifically interfere with the Hsp90-dependent regulation of Cdc2.	wos2	143-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
10581266-9	1999	Hsp90 complexes are required for CDK regulation; the synergy found between the excess of Wos2 and a deficiency in Hsp90 activity suggests that Wos2 could specifically interfere with the Hsp90-dependent regulation of Cdc2.	wos2	143-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
10581266-9	1999	Hsp90 complexes are required for CDK regulation; the synergy found between the excess of Wos2 and a deficiency in Hsp90 activity suggests that Wos2 could specifically interfere with the Hsp90-dependent regulation of Cdc2.	wos2	143-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
10543959-2	1999	p23 binds to Hsp90 in its ATP-bound state and, on its own, interacts specifically with non-native proteins.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
10564678-0	1999	DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90.	17-allylamino	55-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
10564678-0	1999	DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90.	17-demethoxygeldanamycin	70-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
10564678-1	1999	BACKGROUND: To our knowledge, 17-allylamino,17-demethoxygeldanamycin (17AAG) is the first inhibitor of heat shock protein 90 (Hsp90) to enter a phase I clinical trial in cancer.	17-allylamino	30-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-124
10564678-1	1999	BACKGROUND: To our knowledge, 17-allylamino,17-demethoxygeldanamycin (17AAG) is the first inhibitor of heat shock protein 90 (Hsp90) to enter a phase I clinical trial in cancer.	17-allylamino	30-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
10564678-1	1999	BACKGROUND: To our knowledge, 17-allylamino,17-demethoxygeldanamycin (17AAG) is the first inhibitor of heat shock protein 90 (Hsp90) to enter a phase I clinical trial in cancer.	17-demethoxygeldanamycin	44-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-124
10564678-1	1999	BACKGROUND: To our knowledge, 17-allylamino,17-demethoxygeldanamycin (17AAG) is the first inhibitor of heat shock protein 90 (Hsp90) to enter a phase I clinical trial in cancer.	17-demethoxygeldanamycin	44-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
10564678-1	1999	BACKGROUND: To our knowledge, 17-allylamino,17-demethoxygeldanamycin (17AAG) is the first inhibitor of heat shock protein 90 (Hsp90) to enter a phase I clinical trial in cancer.	tanespimycin	70-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-124
10564678-1	1999	BACKGROUND: To our knowledge, 17-allylamino,17-demethoxygeldanamycin (17AAG) is the first inhibitor of heat shock protein 90 (Hsp90) to enter a phase I clinical trial in cancer.	tanespimycin	70-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
10513983-4	1999	Ligand-inducible gene expression was inhibited when the HSP90 expression vector was cotransfected with a TCDD-responsive reporter plasmid.	Polychlorinated Dibenzodioxins	105-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
10632574-2	1999	Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
10557093-7	1999	Second, geldanamycin also induced mt p53 destabilization through the dissociation of the protein from hsp90 but not through the restoration of wt p53 function.	geldanamycin	8-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
10632574-2	1999	Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
10632574-2	1999	Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
10632574-2	1999	Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
10632574-2	1999	Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins.	benzoquinone ansamycin	21-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
10632574-2	1999	Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins.	benzoquinone ansamycin	21-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
10632574-3	1999	Thus, GA has been used as a specific inhibitor of HSP90.	geldanamycin	6-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
10632574-10	1999	These results indicate that the functional inactivation of HSP90 by GA potentially stimulates the expression of heat shock proteins through activation of HSF1.	geldanamycin	68-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
10478836-2	1999	Radicicol, an antifungal antibiotic that inhibits various signal transduction proteins such as v-src, ras, Raf-1, and mos, was found to bind to Hsp90, thus making it the prototype of a second class of Hsp90 inhibitors, distinct from the chemically unrelated benzoquinone ansamycins.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
10478836-2	1999	Radicicol, an antifungal antibiotic that inhibits various signal transduction proteins such as v-src, ras, Raf-1, and mos, was found to bind to Hsp90, thus making it the prototype of a second class of Hsp90 inhibitors, distinct from the chemically unrelated benzoquinone ansamycins.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
10478836-2	1999	Radicicol, an antifungal antibiotic that inhibits various signal transduction proteins such as v-src, ras, Raf-1, and mos, was found to bind to Hsp90, thus making it the prototype of a second class of Hsp90 inhibitors, distinct from the chemically unrelated benzoquinone ansamycins.	benzoquinone ansamycins	258-281	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
10478836-2	1999	Radicicol, an antifungal antibiotic that inhibits various signal transduction proteins such as v-src, ras, Raf-1, and mos, was found to bind to Hsp90, thus making it the prototype of a second class of Hsp90 inhibitors, distinct from the chemically unrelated benzoquinone ansamycins.	benzoquinone ansamycins	258-281	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
10478836-6	1999	Radicicol binds more strongly to Hsp90 than to Grp94, the Hsp90 homolog that resides in the endoplasmic reticulum.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
10478836-6	1999	Radicicol binds more strongly to Hsp90 than to Grp94, the Hsp90 homolog that resides in the endoplasmic reticulum.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
10478836-9	1999	Thus, the radicicol-binding site appears to be specific to and is conserved in all members of the Hsp90 family of molecular chaperones from bacteria to mammals, but is not present in other molecular chaperones with nucleotide-binding domains.	monorden	10-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
10461545-5	1999	It may also be possible to exploit the structure of geldanamycin to develop a new class of hsp-90-binding compounds for use in nerve regeneration.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-97
10463587-3	1999	One of them, the benzoquinone ansamycin geldanamycin (GA) Mr-90,000 heat-shock protein (hsp90)-binding antibiotic, is known to disrupt signaling pathways by inducing destabilization of the enzyme complexes and degradation of signaling intermediates involving the proteasome.	benzoquinone ansamycin geldanamycin	17-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
10463587-3	1999	One of them, the benzoquinone ansamycin geldanamycin (GA) Mr-90,000 heat-shock protein (hsp90)-binding antibiotic, is known to disrupt signaling pathways by inducing destabilization of the enzyme complexes and degradation of signaling intermediates involving the proteasome.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
10409767-4	1999	Treatment of the nuclear receptor with dioxin induces dimerization with Arnt to form an active transcription factor complex, while in stark contrast, treatment with the hsp90 ligand geldanamycin results in rapid degradation of the receptor.	geldanamycin	182-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
10409742-5	1999	Treatment of cells with geldanamycin, an inhibitor of HSP90, decreases the half-life of KSR, suggesting that HSPs may serve to stabilize KSR.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
10403788-9	1999	However, geldanamycin, an hsp90 inhibitor, reduced 1alpha,25-dihydroxyvitamin D(3)-mediated gene activation in osteoblasts.	geldanamycin	9-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
10454292-6	1999	Disruption of the Raf-1-HSP 90 multimolecular complex by geldanamycin lead to a considerable decrease in melanocyte cell count.	geldanamycin	57-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-30
10400612-8	1999	Lys-97 and Arg-101 were absolutely required for hsp90 binding, while mutation of Arg-74 diminished, but did not abrogate, hsp90 binding.	Lysine	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
10400612-9	1999	Mutation of Lys-32, another conserved basic residue in the binding groove, also blocked hsp90 binding.	Lysine	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
10403816-3	1999	HSP-90 (75 or 100 nM) significantly increased calcineurin V(max) in the presence of calmodulin, while maximal stimulation by HSP-70 occurred at 50 nM.	calcineurin v	46-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-6
10403788-9	1999	However, geldanamycin, an hsp90 inhibitor, reduced 1alpha,25-dihydroxyvitamin D(3)-mediated gene activation in osteoblasts.	Calcitriol	51-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
10370241-2	1999	Results from recent studies have shed light on the structure of Hsp90 and have demonstrated that it can bind to and hydrolyse ATP.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
10375396-0	1999	The 650-kDa 12(S)-hydroxyeicosatetraenoic acid binding complex: occurrence in human platelets, identification of hsp90 as a constituent, and binding properties of its 50-kDa subunit.	650-kda 12	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
10375396-0	1999	The 650-kDa 12(S)-hydroxyeicosatetraenoic acid binding complex: occurrence in human platelets, identification of hsp90 as a constituent, and binding properties of its 50-kDa subunit.	Hydroxyeicosatetraenoic Acids	14-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
10383157-0	1999	KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules.	KF 25706	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
10364185-0	1999	The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
10364185-1	1999	The chaperone hsp90 is capable of binding and hydrolyzing ATP.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
10364185-2	1999	Using information on a related ATPase, DNA gyrase B, we selected three conserved residues in hsp90"s ATP-binding domain for mutation.	Adenosine Triphosphate	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
10383157-0	1999	KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules.	monorden	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
10383157-1	1999	Radicicol, a macrocyclic antifungal antibiotic, has been shown to bind to the heat shock protein 90 (Hsp90) chaperone, interfering with its function.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
10383157-1	1999	Radicicol, a macrocyclic antifungal antibiotic, has been shown to bind to the heat shock protein 90 (Hsp90) chaperone, interfering with its function.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
10383157-5	1999	In addition, Hsp90 family chaperone-associated proteins, such as p185erbB2, Raf-1, cyclin-dependent kinase 4, and mutant p53, were depleted by KF25706 at a dose comparable to that required for antiproliferative activity.	KF 25706	143-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
10383157-6	1999	KF25706 was also shown to compete with geldanamycin for binding to Hsp90.	KF 25706	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
10366587-5	1999	Upon exposure of cells to heat shock, the heavy metal cadmium, or the amino acid analogue azetidine, transcription at the hsp90alpha and hsp70 gene loci is strongly induced, and both hsp transcription sites become associated with speckles in >90% of the cells.	Metals	48-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-132
10383157-6	1999	KF25706 was also shown to compete with geldanamycin for binding to Hsp90.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
10366587-5	1999	Upon exposure of cells to heat shock, the heavy metal cadmium, or the amino acid analogue azetidine, transcription at the hsp90alpha and hsp70 gene loci is strongly induced, and both hsp transcription sites become associated with speckles in >90% of the cells.	Cadmium	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-132
10383157-7	1999	KF29163, which is an inactive derivative of radicicol, was less potent both in p185erbB2 depletion and Hsp90 binding.	kf29163	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
10366587-5	1999	Upon exposure of cells to heat shock, the heavy metal cadmium, or the amino acid analogue azetidine, transcription at the hsp90alpha and hsp70 gene loci is strongly induced, and both hsp transcription sites become associated with speckles in >90% of the cells.	azetidine	90-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-132
10383157-12	1999	In agreement with in vivo antitumor activity, KF25706 depleted Hsp90-associated molecules in vivo, whereas KF29163 and radicicol did not show this activity in vivo.	KF 25706	46-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
10383157-13	1999	Taken together, these results suggest that antitumor activity of KF25706 may be mediated, at least in part, by binding to Hsp90 family proteins and destabilization of Hsp90-associated signaling molecules.	KF 25706	65-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
10383157-13	1999	Taken together, these results suggest that antitumor activity of KF25706 may be mediated, at least in part, by binding to Hsp90 family proteins and destabilization of Hsp90-associated signaling molecules.	KF 25706	65-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
10224120-8	1999	Ligand dependence was reconstituted in the presence of molybdate, a transition metal ion known to stabilize the interaction between the molecular chaperone hsp90 and p23.	molybdate	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
10347177-4	1999	When okadaic acid is present during hormone withdrawal, GR that is recycled to the cytoplasm becomes complexed with hsp90 and binds steroid, but it does not undergo the normal agonist-dependent dissociation from hsp90 upon retreatment with steroid.	Okadaic Acid	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
10347177-5	1999	However, when the cytoskeleton is disrupted by colcemid, the GR in okadaic acid-treated cells recycles from the cytoplasm to the nucleus in an agonist-dependent manner without dissociating from hsp90.	Okadaic Acid	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
10225814-12	1999	A significant correlation was demonstrated between IgGs to HSP 90 kDa and two other serological markers for RA, rheumatoid factor, and anti-Sa antibody; there were no correlations with antikeratin antibody, antiperinuclear factor, or anti-RA 33.	2-chloro-10-(4'(N-beta-hydroxyethyl)piperazinyl-1')acetylphenothiazine	140-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-65
10364185-7	1999	While hsp90 is capable of participating in this process in a nucleotide-independent manner, the ability to hydrolyze ATP markedly potentiates hsp90"s effect.	Adenosine Triphosphate	117-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
10322418-0	1999	Hsp90 & Co. - a holding for folding.	Adenosine Monophosphate	7-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
10331966-9	1999	Since HSP90 could preserve F-actin structure during stresses, quercetin might affect the interaction between HSP90 and F-actin without influencing HSP90 expression.	Quercetin	62-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
10331966-9	1999	Since HSP90 could preserve F-actin structure during stresses, quercetin might affect the interaction between HSP90 and F-actin without influencing HSP90 expression.	Quercetin	62-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
10322418-4	1999	Structural studies have identified the ATP-binding site in the N-terminal domain of Hsp90, which can be blocked by high-affinity inhibitors.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
10090774-0	1999	Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
10090774-1	1999	To examine the biochemical mechanism by which hsp90 exerts its essential positive function on certain signal transduction proteins, we characterized the effects of molybdate and geldanamycin on hsp90 function and structure.	molybdate	164-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
10090774-1	1999	To examine the biochemical mechanism by which hsp90 exerts its essential positive function on certain signal transduction proteins, we characterized the effects of molybdate and geldanamycin on hsp90 function and structure.	molybdate	164-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
10090774-1	1999	To examine the biochemical mechanism by which hsp90 exerts its essential positive function on certain signal transduction proteins, we characterized the effects of molybdate and geldanamycin on hsp90 function and structure.	geldanamycin	178-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
10066374-2	1999	The search for the amino acid sequence(s) in Hsp90 involved in interaction with the human GR has been carried out by mutational deletion analysis in whole cells, studying the effects of interaction on the nucleocytoplasmic distributions of transiently expressed Hsp90 and GR derivatives in COS-7 cells.	carbonyl sulfide	290-293	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
10467105-3	1999	Recently, GA has been shown to bind tightly to Hsp90, thereby implicating Hsp90 as a possible chaperone for those signaling molecules adversely affected by the benzoquinoid ansamycins.	benzoquinoid ansamycins	160-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
10467105-3	1999	Recently, GA has been shown to bind tightly to Hsp90, thereby implicating Hsp90 as a possible chaperone for those signaling molecules adversely affected by the benzoquinoid ansamycins.	benzoquinoid ansamycins	160-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
9990042-0	1999	The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.	glucocorticosteroid	72-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
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
9990042-4	1999	Here, by increasing the Hsp90/GR ratio in the nuclear compartment, we found an attenuation of the response to glucocorticosteroids that was not due to a nonspecific or toxic effect of the Hsp90 modified by nuclear targeting.	glucocorticosteroids	110-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
9990042-4	1999	Here, by increasing the Hsp90/GR ratio in the nuclear compartment, we found an attenuation of the response to glucocorticosteroids that was not due to a nonspecific or toxic effect of the Hsp90 modified by nuclear targeting.	glucocorticosteroids	110-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
9933607-9	1999	ATP and geldanamycin, both known to bind to the same pocket of Hsp90, are inhibitors of this process, whereas molybdate, vanadate, and Nonidet P-40, which are thought to increase surface hydrophobicity of the protein, are activators.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
9933607-9	1999	ATP and geldanamycin, both known to bind to the same pocket of Hsp90, are inhibitors of this process, whereas molybdate, vanadate, and Nonidet P-40, which are thought to increase surface hydrophobicity of the protein, are activators.	geldanamycin	8-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
9933607-9	1999	ATP and geldanamycin, both known to bind to the same pocket of Hsp90, are inhibitors of this process, whereas molybdate, vanadate, and Nonidet P-40, which are thought to increase surface hydrophobicity of the protein, are activators.	molybdate	110-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
9933607-9	1999	ATP and geldanamycin, both known to bind to the same pocket of Hsp90, are inhibitors of this process, whereas molybdate, vanadate, and Nonidet P-40, which are thought to increase surface hydrophobicity of the protein, are activators.	Vanadates	121-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
9933607-10	1999	Thus, oligomerization of Hsp90 at high temperatures may be mediated through hydrophobic interactions that are hindered by ligands and favored by transition metal oxyanions.	Metals	156-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
9925731-0	1999	Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.	monorden	94-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
9890555-3	1999	We also compared the effects of AG957 with those of geldanamycin, which can disrupt tyrosine kinase signaling through binding to heat shock protein (hsp90), and two geldanamycin analogs, 17-amino-17-demethoxygeldanamycin (17AG) and 17-allylamino-17-demethoxygeldanamycin (17AAG).	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
9925731-0	1999	Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.	geldanamycin	108-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
9925731-1	1999	The cellular activity of several regulatory and signal transduction proteins, which depend on the Hsp90 molecular chaperone for folding, is markedly decreased by geldanamycin and by radicicol (monorden).	geldanamycin	162-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
9925731-1	1999	The cellular activity of several regulatory and signal transduction proteins, which depend on the Hsp90 molecular chaperone for folding, is markedly decreased by geldanamycin and by radicicol (monorden).	monorden	182-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
9925731-2	1999	We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo.	Adenosine Triphosphate	71-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
9925731-2	1999	We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo.	Adenosine Triphosphate	71-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
9925731-2	1999	We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo.	Adenosine Diphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
9925731-2	1999	We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo.	monorden	109-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
9925731-2	1999	We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo.	monorden	109-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
9925731-3	1999	Crystal structure determinations of Hsp90 N-terminal domain complexes with geldanamycin and radicicol identify key aspects of their nucleotide mimicry and suggest a rational basis for the design of novel antichaperone drugs.	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10090774-1	1999	To examine the biochemical mechanism by which hsp90 exerts its essential positive function on certain signal transduction proteins, we characterized the effects of molybdate and geldanamycin on hsp90 function and structure.	geldanamycin	178-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
9925731-3	1999	Crystal structure determinations of Hsp90 N-terminal domain complexes with geldanamycin and radicicol identify key aspects of their nucleotide mimicry and suggest a rational basis for the design of novel antichaperone drugs.	monorden	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10090774-2	1999	Molybdate inhibited hsp90-mediated p56lck biogenesis and luciferase renaturation while enforcing salt-stable interactions with these substrates.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	47-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
10090774-3	1999	Molybdate also reduced the amount of free hsp90 present in cell lysates, inhibited hsp90"s ability to bind geldanamycin, and induced resistance to proteolysis at a specific region within the C-terminal domain of hsp90.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
10090774-3	1999	Molybdate also reduced the amount of free hsp90 present in cell lysates, inhibited hsp90"s ability to bind geldanamycin, and induced resistance to proteolysis at a specific region within the C-terminal domain of hsp90.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
10090774-3	1999	Molybdate also reduced the amount of free hsp90 present in cell lysates, inhibited hsp90"s ability to bind geldanamycin, and induced resistance to proteolysis at a specific region within the C-terminal domain of hsp90.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
10090774-3	1999	Molybdate also reduced the amount of free hsp90 present in cell lysates, inhibited hsp90"s ability to bind geldanamycin, and induced resistance to proteolysis at a specific region within the C-terminal domain of hsp90.	geldanamycin	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
10090774-3	1999	Molybdate also reduced the amount of free hsp90 present in cell lysates, inhibited hsp90"s ability to bind geldanamycin, and induced resistance to proteolysis at a specific region within the C-terminal domain of hsp90.	geldanamycin	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
10090774-4	1999	In contrast, the hsp90 inhibitor geldanamycin prevented hsp90 from assuming natural or molybdate-induced conformations that allow salt-stable interactions with substrates.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
10090774-4	1999	In contrast, the hsp90 inhibitor geldanamycin prevented hsp90 from assuming natural or molybdate-induced conformations that allow salt-stable interactions with substrates.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
10090774-4	1999	In contrast, the hsp90 inhibitor geldanamycin prevented hsp90 from assuming natural or molybdate-induced conformations that allow salt-stable interactions with substrates.	molybdate	87-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
10090774-4	1999	In contrast, the hsp90 inhibitor geldanamycin prevented hsp90 from assuming natural or molybdate-induced conformations that allow salt-stable interactions with substrates.	molybdate	87-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
10090774-4	1999	In contrast, the hsp90 inhibitor geldanamycin prevented hsp90 from assuming natural or molybdate-induced conformations that allow salt-stable interactions with substrates.	Salts	130-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
10090774-4	1999	In contrast, the hsp90 inhibitor geldanamycin prevented hsp90 from assuming natural or molybdate-induced conformations that allow salt-stable interactions with substrates.	Salts	130-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
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	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.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
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
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	302-307
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	302-307
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	302-307
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9880522-10	1999	We propose that, in vivo, where access by free heme is limited, the complete hsp90-based chaperone machinery is required for sustained opening of the heme binding cleft and nNOS activation, but in the heme-containing cell-free nNOS-activating system transient opening of the heme binding cleft without hsp90 is sufficient to facilitate heme binding.	Heme	150-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	302-307
9887258-5	1999	Treatment of HSP90 at elevated temperatures or with ATP at room temperature, though not with ADP, induces molecular transformation of the linear HSP90 dimer into an O-ring-shaped structure.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
10597896-10	1999	Histones and positively charged peptides modulated the Hsp90-associated kinase activity.	Peptides	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
9887258-5	1999	Treatment of HSP90 at elevated temperatures or with ATP at room temperature, though not with ADP, induces molecular transformation of the linear HSP90 dimer into an O-ring-shaped structure.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
10759403-3	1999	The benzoquinone ansamycin geldanamycin has been shown to bind to Hsp90 and to specifically inhibit this chaperone"s function, resulting in client protein destabilization.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
10759403-3	1999	The benzoquinone ansamycin geldanamycin has been shown to bind to Hsp90 and to specifically inhibit this chaperone"s function, resulting in client protein destabilization.	geldanamycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
10759403-4	1999	Its ability to simultaneously stimulate depletion of multiple oncogenic proteins suggests that geldanamycin, or other molecules capable of targeting Hsp90 in cancer cells, may be of clinical benefit.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
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
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
9875240-2	1998	Previously, we had shown that the immunosuppressant 15-deoxyspergualin (DSG) specifically interacted with Hsc70, as well as the Hsp90 family of proteins.	gusperimus	52-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
9875240-2	1998	Previously, we had shown that the immunosuppressant 15-deoxyspergualin (DSG) specifically interacted with Hsc70, as well as the Hsp90 family of proteins.	gusperimus	72-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
9830049-9	1998	ATP was required for the functioning of both hsp70 and hsp90.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
9830049-10	1998	The binding of hsp70 to the receptor requires hsp40 and about 10 microM ATP; however, hsp90 binding appears to occur subsequent to hsp70 binding and is optimal with 1 mM ATP.	Adenosine Triphosphate	170-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
9843494-3	1998	We show that the ansamysin drugs, geldanamycin and herbimycin A, which inhibit the assembly of some signaling molecules by binding to specific sites on Hsp90 in the cytosol or Grp94 in the ER lumen, block the maturation of nascent CFTR and accelerate its degradation.	geldanamycin	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
9843494-3	1998	We show that the ansamysin drugs, geldanamycin and herbimycin A, which inhibit the assembly of some signaling molecules by binding to specific sites on Hsp90 in the cytosol or Grp94 in the ER lumen, block the maturation of nascent CFTR and accelerate its degradation.	herbimycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
9843494-4	1998	The immature CFTR molecule was detected in association with Hsp90 but not with Grp94, and geldanamycin prevented the Hsp90 association.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
9843494-6	1998	Therefore, consistent with other examples of countervailing effects of Hsp90 and the proteasome, it would seem that this chaperone may normally contribute to CFTR folding and, when this function is interfered with by an ansamycin, there is a further shift to proteolytic degradation.	Rifabutin	220-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
9792703-2	1998	Herbimycin A, a drug that binds to Hsp90, induces the destruction of tyrosine kinases and causes the down-regulation of cyclin D and an Rb-dependent growth arrest in the G1 phase of the cell cycle.	herbimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
9817749-7	1998	Based on a new crystal structure of the NH2-terminal domain of human Hsp90 with bound ADP-Mg and on the structural homology of this domain with the ATPase domain of Escherichia coli DNA gyrase, the residues of Hsp90 critical in ATP binding (D93) and ATP hydrolysis (E47) were identified.	Adenosine Diphosphate	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
9817749-7	1998	Based on a new crystal structure of the NH2-terminal domain of human Hsp90 with bound ADP-Mg and on the structural homology of this domain with the ATPase domain of Escherichia coli DNA gyrase, the residues of Hsp90 critical in ATP binding (D93) and ATP hydrolysis (E47) were identified.	Adenosine Triphosphate	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
9817749-7	1998	Based on a new crystal structure of the NH2-terminal domain of human Hsp90 with bound ADP-Mg and on the structural homology of this domain with the ATPase domain of Escherichia coli DNA gyrase, the residues of Hsp90 critical in ATP binding (D93) and ATP hydrolysis (E47) were identified.	Adenosine Triphosphate	228-231	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
9751071-8	1998	Recently, Hsp90 was shown to be the unique target for geldanamycin, a potent new anti-tumor drug that blocks cell proliferation.	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
9727490-3	1998	In a novel in vitro system, in which human HSF1 can be activated by nonnative protein, heat, and geldanamycin, addition of Hsp90 inhibits activation.	geldanamycin	97-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
9727490-5	1998	In vivo, geldanamycin activates HSF1 under conditions in which it is an Hsp90-specific reagent.	geldanamycin	9-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
9705856-0	1998	The two-state process of the heat shock protein 90 thermal denaturation: effect of calcium and magnesium.	Calcium	83-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
9705856-0	1998	The two-state process of the heat shock protein 90 thermal denaturation: effect of calcium and magnesium.	Magnesium	95-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
9705856-2	1998	The calorimetric curve of the hsp90 dimer consists of two transitions centered at 53.8 and 63.1 degrees C. Using specific ligand geldanamycin, we have found that N-terminal domains in the hsp90 dimer are melted independently in the lower-temperature peak, while the higher-temperature one comprises unfolding of two non-interacting parts of the middle domains and dimerization region.	geldanamycin	129-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
9705856-2	1998	The calorimetric curve of the hsp90 dimer consists of two transitions centered at 53.8 and 63.1 degrees C. Using specific ligand geldanamycin, we have found that N-terminal domains in the hsp90 dimer are melted independently in the lower-temperature peak, while the higher-temperature one comprises unfolding of two non-interacting parts of the middle domains and dimerization region.	geldanamycin	129-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
9705856-4	1998	Calcium and magnesium strongly decrease the hsp90 thermostability and thereby cause oligomerization at lower temperature.	Calcium	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
9705856-4	1998	Calcium and magnesium strongly decrease the hsp90 thermostability and thereby cause oligomerization at lower temperature.	Magnesium	12-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
9705856-5	1998	We suggest that calcium affects the hsp90 oligomerization, known to be important for its chaperone activity, by shifting the unfolding temperature of the hsp90 N-terminal domain close to the heat shock temperature range.	Calcium	16-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
9705856-5	1998	We suggest that calcium affects the hsp90 oligomerization, known to be important for its chaperone activity, by shifting the unfolding temperature of the hsp90 N-terminal domain close to the heat shock temperature range.	Calcium	16-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
9738900-7	1998	Here we provide direct evidence for the binding of vanadate and molybdate to Hsp90 by demonstrating that surface-plasmon-resonance measurements indicate binding of various vanadate oligomers to Hsp90.	Vanadates	51-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9738900-7	1998	Here we provide direct evidence for the binding of vanadate and molybdate to Hsp90 by demonstrating that surface-plasmon-resonance measurements indicate binding of various vanadate oligomers to Hsp90.	Vanadates	51-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
9738900-7	1998	Here we provide direct evidence for the binding of vanadate and molybdate to Hsp90 by demonstrating that surface-plasmon-resonance measurements indicate binding of various vanadate oligomers to Hsp90.	molybdate	64-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9738900-7	1998	Here we provide direct evidence for the binding of vanadate and molybdate to Hsp90 by demonstrating that surface-plasmon-resonance measurements indicate binding of various vanadate oligomers to Hsp90.	molybdate	64-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
9738900-7	1998	Here we provide direct evidence for the binding of vanadate and molybdate to Hsp90 by demonstrating that surface-plasmon-resonance measurements indicate binding of various vanadate oligomers to Hsp90.	Vanadates	172-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9738900-7	1998	Here we provide direct evidence for the binding of vanadate and molybdate to Hsp90 by demonstrating that surface-plasmon-resonance measurements indicate binding of various vanadate oligomers to Hsp90.	Vanadates	172-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
9738900-8	1998	51V-NMR measurements show an extensive interaction of decavanadate with the chaperone, and permolybdate treatment of Hsp90 induces a marked mobility shift of the protein and its tryptic fragments.	permolybdate	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
9738900-9	1998	Our results indicate the flexibility of molybdate/vanadate-binding sites of Hsp90, which are able to accommodate various species of these transition metal anions.	molybdate	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
9738900-9	1998	Our results indicate the flexibility of molybdate/vanadate-binding sites of Hsp90, which are able to accommodate various species of these transition metal anions.	Vanadates	50-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
9738900-9	1998	Our results indicate the flexibility of molybdate/vanadate-binding sites of Hsp90, which are able to accommodate various species of these transition metal anions.	Metals	149-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
9688848-4	1998	We have investigated the ability of deoxyspergualin (DSG), a compound known to compete effectively for binding with HSP70 and HSP90, to promote trafficking of DeltaF508-CFTR to the cell membrane.	gusperimus	36-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
9658403-12	1998	The nuclear 9S-[3H]Org2058-PR resulting from cells exposed to Rap, contained, in addition to the heat shock proteins of 90 kDa and 70 kDa (hsp90 and hsp70), the FK506-binding immunophilin FKBP52 but not FKBP51, although the latter was part of unliganded PR heterocomplex associated with hsp90.	Tritium	16-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
9658403-12	1998	The nuclear 9S-[3H]Org2058-PR resulting from cells exposed to Rap, contained, in addition to the heat shock proteins of 90 kDa and 70 kDa (hsp90 and hsp70), the FK506-binding immunophilin FKBP52 but not FKBP51, although the latter was part of unliganded PR heterocomplex associated with hsp90.	Tritium	16-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	287-292
9658403-12	1998	The nuclear 9S-[3H]Org2058-PR resulting from cells exposed to Rap, contained, in addition to the heat shock proteins of 90 kDa and 70 kDa (hsp90 and hsp70), the FK506-binding immunophilin FKBP52 but not FKBP51, although the latter was part of unliganded PR heterocomplex associated with hsp90.	Tacrolimus	161-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	287-292
9658403-15	1998	Immunoprecipitation experiments distinguished two PR- and glucocorticosteroid (GR)-associated molecular chaperone complexes, containing hsp90 and hsp70 and FKBP52 or FKBP51.	glucocorticosteroid	58-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
9691273-0	1998	ATP sensitive tryptophans of hsp90.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
9738900-0	1998	Interaction of vanadate oligomers and permolybdate with the 90-kDa heat-shock protein, Hsp90.	Vanadates	15-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
9738900-2	1998	Hsp90 x protein complexes can be stabilized by molybdate and by other transition metal oxyanions such as vanadate.	molybdate	47-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
9738900-2	1998	Hsp90 x protein complexes can be stabilized by molybdate and by other transition metal oxyanions such as vanadate.	Metals	81-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
9738900-2	1998	Hsp90 x protein complexes can be stabilized by molybdate and by other transition metal oxyanions such as vanadate.	Vanadates	105-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
9738900-6	1998	268, 1901-1907] showed that vanadate and molybdate can induce a large conformational change of Hsp90.	Vanadates	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
9738900-6	1998	268, 1901-1907] showed that vanadate and molybdate can induce a large conformational change of Hsp90.	molybdate	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
9691273-0	1998	ATP sensitive tryptophans of hsp90.	Tryptophan	14-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
9691273-1	1998	The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature.	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
9691273-1	1998	The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature.	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
9691273-1	1998	The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature.	Tryptophan	132-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
9691273-7	1998	The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.	Tryptophan	139-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9691273-1	1998	The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature.	Tryptophan	132-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
9691273-3	1998	Acrylamide quenching of tryptophan fluorescence in hsp90 is also principally collisional and identifies two classes of residues, one readily accessible to quenching the other less accessible.	Acrylamide	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9691273-3	1998	Acrylamide quenching of tryptophan fluorescence in hsp90 is also principally collisional and identifies two classes of residues, one readily accessible to quenching the other less accessible.	Tryptophan	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9691273-4	1998	ATP quenching of tryptophan fluorescence in hsp90 is more complex exhibiting no overall preferred mechanism.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
9691273-4	1998	ATP quenching of tryptophan fluorescence in hsp90 is more complex exhibiting no overall preferred mechanism.	Tryptophan	17-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
9691273-6	1998	The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
9691273-6	1998	The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
9691273-6	1998	The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific.	Tryptophan	13-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
9691273-6	1998	The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
9691273-6	1998	The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
9691273-7	1998	The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.	Tryptophan	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9626660-0	1998	Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm.	RU 58668	89-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
9672245-0	1998	Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin.	monorden	11-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
9672245-0	1998	Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin.	geldanamycin	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
9672245-2	1998	A 15 A deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/ADP-binding site and has also been shown to bind geldanamycin, the only specific inhibitor of Hsp90 function described to date.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
9672245-2	1998	A 15 A deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/ADP-binding site and has also been shown to bind geldanamycin, the only specific inhibitor of Hsp90 function described to date.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
9672245-2	1998	A 15 A deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/ADP-binding site and has also been shown to bind geldanamycin, the only specific inhibitor of Hsp90 function described to date.	Adenosine Diphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
9672245-2	1998	A 15 A deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/ADP-binding site and has also been shown to bind geldanamycin, the only specific inhibitor of Hsp90 function described to date.	Adenosine Diphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
9672245-2	1998	A 15 A deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/ADP-binding site and has also been shown to bind geldanamycin, the only specific inhibitor of Hsp90 function described to date.	geldanamycin	126-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
9672245-2	1998	A 15 A deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/ADP-binding site and has also been shown to bind geldanamycin, the only specific inhibitor of Hsp90 function described to date.	geldanamycin	126-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
9672245-3	1998	We now show that radicicol, a macrocyclic antifungal structurally unrelated to geldanamycin, also specifically binds to Hsp90.	monorden	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
9672245-5	1998	Radicicol, as does geldanamycin, also inhibits the binding of the accessory protein p23 to Hsp90, and interferes with assembly of the mature progesterone receptor complex.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
9672245-5	1998	Radicicol, as does geldanamycin, also inhibits the binding of the accessory protein p23 to Hsp90, and interferes with assembly of the mature progesterone receptor complex.	geldanamycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
9672245-6	1998	Radicicol does not deplete cells of Hsp90, but rather increases synthesis as well as the steady-state level of this protein, similar to a stress response.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
9672245-8	1998	Radicicol thus represents a structurally unique antibiotic, and the first non-benzoquinone ansamycin, capable of binding to Hsp90 and interfering with its function.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
9672245-8	1998	Radicicol thus represents a structurally unique antibiotic, and the first non-benzoquinone ansamycin, capable of binding to Hsp90 and interfering with its function.	benzoquinone ansamycin	78-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
9672247-8	1998	Binding of p23 mapped most strongly to the N-terminal ATP-binding domain of Hsp90 while binding of TPR proteins mapped to the C-terminal half of Hsp90.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
9602032-4	1998	However, Hsp89alpha DeltaN cDNA lacks the ATP/geldanamycin binding domain (codons 1-220), instead containing 544 nucleotides of unique DNA at its 5" end including 30 novel codons.	Adenosine Triphosphate	42-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-19
9602032-4	1998	However, Hsp89alpha DeltaN cDNA lacks the ATP/geldanamycin binding domain (codons 1-220), instead containing 544 nucleotides of unique DNA at its 5" end including 30 novel codons.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-19
11326954-7	1998	The more hsp 90 gene expression, the less T lymphocytes were inhibited by Dex.	Dexamethasone	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-15
9632140-6	1998	This was confirmed by demonstrating the ability of radicicol to specifically bind purified human HSP90.	monorden	51-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
9580552-2	1998	Here we show that Hsp90 associates with endothelial nitric oxide synthase (eNOS) and is rapidly recruited to the eNOS complex by agonists that stimulate production of nitric oxide, namely vascular endothelial growth factor, histamine and fluid shear stress.	Nitric Oxide	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
9580552-2	1998	Here we show that Hsp90 associates with endothelial nitric oxide synthase (eNOS) and is rapidly recruited to the eNOS complex by agonists that stimulate production of nitric oxide, namely vascular endothelial growth factor, histamine and fluid shear stress.	Histamine	224-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
9580552-4	1998	Inhibition of signalling through Hsp90 attenuates both agonist-stimulated production of nitric oxide and endothelium-dependent relaxation of isolated blood vessels.	Nitric Oxide	88-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
9480920-7	1998	Glycerol gradient centrifugation at the physiological salt concentration as well as native PAGE analysis of rat liver cytosol revealed oligomeric forms of HSP90alpha sedimenting at 8-10S as predominant ones.	Glycerol	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-165
9691273-7	1998	The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9744771-0	1998	The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
9563819-5	1998	Nucleotide binding to ATP-dependent chaperones (e.g. GroEL, Hsp70, Hsp90) leads to sometimes large conformational changes in the chaperone which allow to shift between high- and low-affinity states for substrate proteins.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
9488468-0	1998	The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent.	geldanamycin	96-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
9488468-8	1998	To examine the effect of directly disrupting chaperone interactions with mutant p53, we made use of geldanamycin (GA), a selective hsp90-binding agent which has been shown to alter the chaperone associations regulating the function of unliganded steroid receptors.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
9488468-8	1998	To examine the effect of directly disrupting chaperone interactions with mutant p53, we made use of geldanamycin (GA), a selective hsp90-binding agent which has been shown to alter the chaperone associations regulating the function of unliganded steroid receptors.	geldanamycin	114-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
9465043-0	1998	Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
9465043-9	1998	Furthermore, the antitumor drug geldanamycin both inhibits the weak ATPase of Hsp90 and stimulates peptide release.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
9447995-1	1998	Prior to ligand activation, the unactivated aryl hydrocarbon receptor (AhR) exists in a heterotetrameric 9S core complex consisting of the AhR ligand-binding subunit, a dimer of hsp90, and an unknown subunit.	CHEMBL3403964	105-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
9744771-0	1998	The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
9744771-4	1998	We therefore examined the biologic effects of 17-allylamino-17-demethoxygeldanamycin (17-AG), an ansamycin derivative with lower in vivo toxicity than GA. METHODS: Binding of 17-AG to HSP90 was studied in vitro using a GA-affinity beads competition assay.	tanespimycin	175-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
9744771-7	1998	RESULTS: We found that, in a similar manner to GA itself, 17-AG bound specifically to HSP90.	geldanamycin	47-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
9744771-7	1998	RESULTS: We found that, in a similar manner to GA itself, 17-AG bound specifically to HSP90.	tanespimycin	58-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
9428803-0	1998	Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
9428803-1	1998	Geldanamycin, a benzoquinone ansamycin, binds specifically to hsp90 and GRP94 in vitro and in vivo.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
9428803-1	1998	Geldanamycin, a benzoquinone ansamycin, binds specifically to hsp90 and GRP94 in vitro and in vivo.	benzoquinone ansamycin	16-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
9428803-2	1998	Treatment of cells with geldanamycin alters the molecular chaperone function of hsp90, and as a result, blocks certain cytosolic proteins from reaching their mature form, inhibits their activity, and/or affects their stability.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
9744771-0	1998	The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin.	tanespimycin	27-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
9747895-0	1998	The Hsp90-specific inhibitor, geldanamycin, blocks CD28-mediated activation of human T lymphocytes.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
9747895-2	1998	Hsp90-mediated folding can be disrupted by the Hsp90-specific drug, geldanamycin.	geldanamycin	68-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
9747895-2	1998	Hsp90-mediated folding can be disrupted by the Hsp90-specific drug, geldanamycin.	geldanamycin	68-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
9390191-1	1997	Geldanamycin (GA) binds directly to hsp90 and apparently disrupts certain hsp90 heterocomplexes.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
9390191-1	1997	Geldanamycin (GA) binds directly to hsp90 and apparently disrupts certain hsp90 heterocomplexes.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
9390191-1	1997	Geldanamycin (GA) binds directly to hsp90 and apparently disrupts certain hsp90 heterocomplexes.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
9390191-1	1997	Geldanamycin (GA) binds directly to hsp90 and apparently disrupts certain hsp90 heterocomplexes.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
9390191-3	1997	Incubation of 2-[125I]-iodo-3-azido-7,8-dibromo-p-dioxin-labeled Hepa 1c1c7 cytosol with GA-coupled beads revealed a stable association of Ah receptor (AhR)/hsp90 complex with GA.	2-[125i]-iodo-3-azido-7,8-dibromo-p-dioxin	14-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
9390191-3	1997	Incubation of 2-[125I]-iodo-3-azido-7,8-dibromo-p-dioxin-labeled Hepa 1c1c7 cytosol with GA-coupled beads revealed a stable association of Ah receptor (AhR)/hsp90 complex with GA.	geldanamycin	89-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
9367823-2	1997	The benzoquinone ansamycin Geldanamycin (GA) specifically binds to the heat shock protein HSP90 and alters its complex with Raf-1.	geldanamycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
9417863-8	1997	hsp90 does not bind p53 in a spatial-specific manner because it remains bound to p53 when induced to translocate to the nucleus by the protein synthesis inhibitor cycloheximide (CHX).	Cycloheximide	163-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
9417863-8	1997	hsp90 does not bind p53 in a spatial-specific manner because it remains bound to p53 when induced to translocate to the nucleus by the protein synthesis inhibitor cycloheximide (CHX).	Cycloheximide	178-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
9417863-9	1997	Treatment of transformed cells with geldanamycin (GA), a small molecule that binds hsp90, causes a rapid destabilization of p53 by 50%.	geldanamycin	36-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
9417863-9	1997	Treatment of transformed cells with geldanamycin (GA), a small molecule that binds hsp90, causes a rapid destabilization of p53 by 50%.	geldanamycin	50-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
9414113-4	1997	The chaperone activity of the N-domain is inhibited by geldanamycin, a specific inhibitor of hsp90-mediated protein refolding.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
9367823-2	1997	The benzoquinone ansamycin Geldanamycin (GA) specifically binds to the heat shock protein HSP90 and alters its complex with Raf-1.	geldanamycin	41-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	Adenosine Diphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
9367823-2	1997	The benzoquinone ansamycin Geldanamycin (GA) specifically binds to the heat shock protein HSP90 and alters its complex with Raf-1.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
9334248-6	1997	We also showed that hGRbeta bound to hsp90 by immunoprecipitation of in vitro translated hGRbeta in reticulocyte lysate with hsp90-specific antibodies, a coprecipitation occurring also in the presence of dexamethasone.	Dexamethasone	204-217	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	Adenosine Diphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
9295332-1	1997	Many functions of the chaperone, heat shock protein 90 (hsp90), are inhibited by the drug geldanamycin that specifically binds hsp90.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-54
9295332-1	1997	Many functions of the chaperone, heat shock protein 90 (hsp90), are inhibited by the drug geldanamycin that specifically binds hsp90.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
9295332-1	1997	Many functions of the chaperone, heat shock protein 90 (hsp90), are inhibited by the drug geldanamycin that specifically binds hsp90.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
9295332-2	1997	We have studied an amino-terminal domain of hsp90 whose crystal structure has recently been solved and determined to contain a geldanamycin-binding site.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
9295332-6	1997	Mutation of four glycine residues within two proposed ATP binding motifs diminishes both geldanamycin binding and the ATP-dependent conversion of hsp90 to a conformation capable of binding the co-chaperone p23.	Glycine	17-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
9295332-6	1997	Mutation of four glycine residues within two proposed ATP binding motifs diminishes both geldanamycin binding and the ATP-dependent conversion of hsp90 to a conformation capable of binding the co-chaperone p23.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
9295332-6	1997	Mutation of four glycine residues within two proposed ATP binding motifs diminishes both geldanamycin binding and the ATP-dependent conversion of hsp90 to a conformation capable of binding the co-chaperone p23.	Adenosine Triphosphate	118-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
9295332-7	1997	Since p23 binding requires regions outside the 1-221 domain of hsp90, these results indicate a common site for nucleotides and geldanamycin that regulates the conformation of other hsp90 domains.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
9295332-7	1997	Since p23 binding requires regions outside the 1-221 domain of hsp90, these results indicate a common site for nucleotides and geldanamycin that regulates the conformation of other hsp90 domains.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
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
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	geldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	geldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	geldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
9295332-0	1997	The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.	Adenosine Diphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
9269769-6	1997	Immunoprecipitations with antibodies against either the heat-shock cognate protein 70 (hsc70) or heat-shock protein 90 (hsp90) showed the presence of a phosphoprotein complex in 32P-labeled, resting human platelets.	Phosphorus-32	178-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-118
9269769-6	1997	Immunoprecipitations with antibodies against either the heat-shock cognate protein 70 (hsc70) or heat-shock protein 90 (hsp90) showed the presence of a phosphoprotein complex in 32P-labeled, resting human platelets.	Phosphorus-32	178-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
9296382-4	1997	The present study was designed to determine how the new hsp 90-binding agent geldanamycin, which was previously shown to disrupt the formation of steroid receptor/hsp complexes, interferes with MR- and GR-mediated transactivation in intact cells.	geldanamycin	77-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-62
9288847-7	1997	The rates of synthesis of oxygen-regulated proteins (GRP78, GRP94, HSP70 and HSP90) were transiently perturbed to a similar extent in all lines after hypoxia treatment.	Oxygen	26-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
9285055-5	1997	Immunochemical analysis by use of the mAbs revealed that both of the HSP90 isoforms were present in human cells even under unstressed conditions and that the expression of HSP90 alpha was more strongly induced when the cells were exposed to arsenate.	arsenic acid	241-249	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
9285055-5	1997	Immunochemical analysis by use of the mAbs revealed that both of the HSP90 isoforms were present in human cells even under unstressed conditions and that the expression of HSP90 alpha was more strongly induced when the cells were exposed to arsenate.	arsenic acid	241-249	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-183
9228040-1	1997	The ansamycin antibiotic geldanamycin, which specifically interacts with the heat shock protein hsp90, was used to study the function of hsp90 in steroid hormone receptors.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
9228028-0	1997	ATP-binding properties of human Hsp90.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
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
9228028-3	1997	It is well established that the level of Hsp90 increases severalfold under stress conditions, and it has been shown that the chaperone function of Hsp90 is ATP-independent.	Adenosine Triphosphate	156-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
9201920-8	1997	In this work, we show that treatment of L cells with geldanamycin, a benzoquinone ansamycin that binds to hsp90 and disrupts its function, impedes dexamethasone-dependent trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
9228028-5	1997	Here, we have reinvestigated ATP-binding properties and ATPase activity of human Hsp90 under various conditions.	Adenosine Triphosphate	29-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
9228040-0	1997	The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin.	geldanamycin	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
9228040-1	1997	The ansamycin antibiotic geldanamycin, which specifically interacts with the heat shock protein hsp90, was used to study the function of hsp90 in steroid hormone receptors.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
9228040-1	1997	The ansamycin antibiotic geldanamycin, which specifically interacts with the heat shock protein hsp90, was used to study the function of hsp90 in steroid hormone receptors.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
9228040-1	1997	The ansamycin antibiotic geldanamycin, which specifically interacts with the heat shock protein hsp90, was used to study the function of hsp90 in steroid hormone receptors.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
9195923-0	1997	Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.	Tacrolimus	108-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
9195923-2	1997	The immunophilin, which can be of the FK506- or cyclosporin A-binding class, binds to hsp90 via its tetratricopeptide repeat (TPR) domain, and different receptor heterocomplexes exist depending upon which immunophilin occupies the TPR-binding region of hsp90.	Tacrolimus	38-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
9195923-2	1997	The immunophilin, which can be of the FK506- or cyclosporin A-binding class, binds to hsp90 via its tetratricopeptide repeat (TPR) domain, and different receptor heterocomplexes exist depending upon which immunophilin occupies the TPR-binding region of hsp90.	Cyclosporine	48-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
9195923-7	1997	Approximately one-half of the GR.hsp90 heterocomplexes in L cell cytosol contains an immunophilin with high affinity FK506 binding activity, such as FKBP51 or FKBP52, and approximately 35% contains PP5.	Tacrolimus	117-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
9195923-8	1997	Only a small (but undetermined) fraction of the native GR.hsp90 heterocomplexes contain the cyclosporin A-binding immunophilin CyP-40.	Cyclosporine	92-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
9201920-8	1997	In this work, we show that treatment of L cells with geldanamycin, a benzoquinone ansamycin that binds to hsp90 and disrupts its function, impedes dexamethasone-dependent trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus.	benzoquinone ansamycin	69-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
9201920-11	1997	However, as reported previously for the progesterone receptor, geldanamycin blocks assembly of the glucocorticoid receptor-hsp90 heterocomplex at an intermediate state of assembly where the receptor is bound to hsp70 and p60, both of which are required components in the assembly mechanism.	geldanamycin	63-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
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
9148915-11	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.	Adenosine Triphosphate	280-283	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
9148915-12	1997	When the GR is incubated with hsp90, hsp70, and p60 in the presence of the hsp90-binding antibiotic geldanamycin, GR.hsp90.p60.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
9261129-12	1997	p23 stabilizes the GR.hsp90 heterocomplex in a dynamic and ATP-independent manner.	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
9261129-13	1997	In contrast to hsp90 that is bound to the GR, free hsp90 binds p23 in an ATP-dependent manner, and hsp90 in the hsp90.p60.hsp70 heterocomplex is in a conformation that does not bind p23 at all.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9148915-12	1997	When the GR is incubated with hsp90, hsp70, and p60 in the presence of the hsp90-binding antibiotic geldanamycin, GR.hsp90.p60.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
9261129-13	1997	In contrast to hsp90 that is bound to the GR, free hsp90 binds p23 in an ATP-dependent manner, and hsp90 in the hsp90.p60.hsp70 heterocomplex is in a conformation that does not bind p23 at all.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
9148915-12	1997	When the GR is incubated with hsp90, hsp70, and p60 in the presence of the hsp90-binding antibiotic geldanamycin, GR.hsp90.p60.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
9261129-13	1997	In contrast to hsp90 that is bound to the GR, free hsp90 binds p23 in an ATP-dependent manner, and hsp90 in the hsp90.p60.hsp70 heterocomplex is in a conformation that does not bind p23 at all.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
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
9261129-15	1997	Molybdate has the same ability as p23 to stabilize GR heterocomplexes with mammalian hsp90, but GR heterocomplexes with plant hsp90 are stabilized by p23 and not by molybdate.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
9261129-16	1997	We propose that incubation of the GR with hsp90.p60.hsp70 forms a GR.hsp90 heterocomplex in which hsp90 is in an ATP-dependent conformation.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
9164841-11	1997	After its associated proteins, especially the heat-shock protein hsp90, had been cross-linked with the hMR by dimethylpimelimidate, 18C7 was still able to react with the receptor.	dimethyl pimelimidate	110-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
9261129-16	1997	We propose that incubation of the GR with hsp90.p60.hsp70 forms a GR.hsp90 heterocomplex in which hsp90 is in an ATP-dependent conformation.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
9261129-16	1997	We propose that incubation of the GR with hsp90.p60.hsp70 forms a GR.hsp90 heterocomplex in which hsp90 is in an ATP-dependent conformation.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
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.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
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
9108479-0	1997	Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
9115298-8	1997	Hormone binding studies showed that the ligand-binding domain of VP16-GAL-ERV was destabilized by incubation in the presence of high concentrations of salt or in the absence of sodium molybdate, conditions that disrupt its interaction with hsp90.	Salts	151-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
9115298-8	1997	Hormone binding studies showed that the ligand-binding domain of VP16-GAL-ERV was destabilized by incubation in the presence of high concentrations of salt or in the absence of sodium molybdate, conditions that disrupt its interaction with hsp90.	sodium molybdate(VI)	177-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
9115298-9	1997	The ligand-binding domain of the Val-400 ER thus behaves similarly to that of the wild-type glucocorticoid receptor, which has previously been shown to interact with hsp90 in vitro.	Valine	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
9108479-2	1997	The geldanamycin antibiotic has antiproliferative and antitumor effects, as it binds to Hsp90, inhibits the Hsp90-mediated conformational maturation/refolding reaction, and results in the degradation of Hsp90 substrates.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
9108479-2	1997	The geldanamycin antibiotic has antiproliferative and antitumor effects, as it binds to Hsp90, inhibits the Hsp90-mediated conformational maturation/refolding reaction, and results in the degradation of Hsp90 substrates.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
9108479-2	1997	The geldanamycin antibiotic has antiproliferative and antitumor effects, as it binds to Hsp90, inhibits the Hsp90-mediated conformational maturation/refolding reaction, and results in the degradation of Hsp90 substrates.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
9108479-3	1997	The structure of the geldanamycin-binding domain of Hsp90 (residues 9-232) reveals a pronounced pocket, 15 A deep, that is highly conserved across species.	geldanamycin	21-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
9049266-8	1997	When 35S-labelled B. napus cytosolic extracts were immunoprecipitated with the R2 antiserum, hsp90 and two additional proteins with approximate molecular masses of 49 and 45 kDa were detected in the immunoprecipitates.	Sulfur-35	5-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
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
9148915-9	1997	In this minimal reconstituted system, the GR is incubated with the chaperones in the presence of [3H]triamcinolone acetonide ([3H]TA), which binds to the receptor as GR.hsp90 complexes are formed.	[3h]triamcinolone acetonide	97-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
9148915-9	1997	In this minimal reconstituted system, the GR is incubated with the chaperones in the presence of [3H]triamcinolone acetonide ([3H]TA), which binds to the receptor as GR.hsp90 complexes are formed.	[3h]ta	126-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
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
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.	Adenosine Triphosphate	280-283	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
8962087-2	1996	The recent discovery that a class of ansamycin antibiotics bind specifically to Hsp90 allowed us to address this problem from a new angle.	Rifabutin	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
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
8962087-3	1996	We find that mammalian Hsp90, in cooperation with Hsp70, p60, and other factors, mediates the ATP-dependent refolding of heat-denatured proteins, such as firefly luciferase.	Adenosine Triphosphate	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
8962087-5	1996	The ansamycins inhibit refolding, both in vivo and in a cell extract, by preventing normal dissociation of Hsp90 from luciferase, causing its enhanced degradation.	Lactams, Macrocyclic	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
8962087-6	1996	This mechanism also explains the ansamycin-induced proteolysis of several protooncogenic protein kinases, such as Raf-1, which interact with Hsp90.	Rifabutin	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
8962087-9	1996	The ansamycins shift the mode of Hsp90 from refolding to degradation, and this effect is probably amplified for specific Hsp90 substrates.	Lactams, Macrocyclic	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
8962087-9	1996	The ansamycins shift the mode of Hsp90 from refolding to degradation, and this effect is probably amplified for specific Hsp90 substrates.	Lactams, Macrocyclic	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
8892646-0	1996	Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: a possible role in immunopathology.	Cycloheximide	154-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-31
8892646-0	1996	Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: a possible role in immunopathology.	Cycloheximide	154-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
8892646-7	1996	This was complemented by the finding that reduced hsp90 levels correlate with protection against apoptosis in the TNF-alpha- and cx-treated cells.	Cycloheximide	129-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
9159187-5	1996	More recently, however, Hsp90 has been identified as an ATP independent molecular chaperone, which binds transiently to folding intermediates in vitro, prevents aggregation and supports the refolding of the intermediates to the native state.	Adenosine Triphosphate	56-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
8806428-7	1996	Decreased hsp90 levels slowed the rate of cell division and levels of hsp90 correlated both with the responses to phorbol esters and with phenotypic changes: antisense-transfected cells expressed less CD50.	Phorbol Esters	114-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
9065472-1	1997	Previous studies have demonstrated the ATP-dependent formation of a complex containing the heat shock protein hsp90, the unique hsp90 binding protein p23, and one of three high molecular weight immunophilins.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
9065472-1	1997	Previous studies have demonstrated the ATP-dependent formation of a complex containing the heat shock protein hsp90, the unique hsp90 binding protein p23, and one of three high molecular weight immunophilins.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
9065472-2	1997	In the present study, hsp90 and p23 are shown to form a complex that requires elevated temperature and ATP/Mg2+.	Adenosine Triphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
9065472-2	1997	In the present study, hsp90 and p23 are shown to form a complex that requires elevated temperature and ATP/Mg2+.	magnesium ion	107-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
9065472-5	1997	The ATP-dependent process alters the state of hsp90, not p23, and influences the ability of hsp90 to bind to phenyl-Sepharose.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
9065472-5	1997	The ATP-dependent process alters the state of hsp90, not p23, and influences the ability of hsp90 to bind to phenyl-Sepharose.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
9065472-5	1997	The ATP-dependent process alters the state of hsp90, not p23, and influences the ability of hsp90 to bind to phenyl-Sepharose.	phenyl-sepharose	109-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
9065472-5	1997	The ATP-dependent process alters the state of hsp90, not p23, and influences the ability of hsp90 to bind to phenyl-Sepharose.	phenyl-sepharose	109-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
9065472-6	1997	Conversion of hsp90 to the ATP-bound state lowers its affinity for phenyl-Sepharose.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
9065472-6	1997	Conversion of hsp90 to the ATP-bound state lowers its affinity for phenyl-Sepharose.	phenyl-sepharose	67-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
8806428-7	1996	Decreased hsp90 levels slowed the rate of cell division and levels of hsp90 correlated both with the responses to phorbol esters and with phenotypic changes: antisense-transfected cells expressed less CD50.	Phorbol Esters	114-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
8626558-0	1996	Assessment of the ATP binding properties of Hsp90.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
8776730-4	1996	At the molecular level, GA bound hsp90, but not GR, in a stable and specific manner in intact cells.	geldanamycin	24-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
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
8764065-6	1996	Since hemin treatment of K562 cells also induced the increased expression of several heat shock proteins (Hsp70, Hsc70, Hsp90, and cohort p60), we tested the hypothesis that their increased expression may play a role in altering poliovirus infection in hemin-treated K562 cells.	Hemin	6-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
8626558-5	1996	Hsp90 behaved very similarly to the non-ATP-binding proteins and very differently from the ATP-binding protein Hsc70.	Adenosine Triphosphate	40-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
8626558-1	1996	Hsp90, one of the most prominent proteins in eucaryotic cells under physiological and stress conditions, chaperones protein folding reactions in an ATP-independent way.	Adenosine Triphosphate	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
8626558-2	1996	Surprisingly, ATP binding and ATPase activity of Hsp90 has been reported by several groups.	Adenosine Triphosphate	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
8615809-9	1996	In addition, we showed that the unbound and the aldosterone-bound 30 kDa fragment were both associated with heat-shock protein (hsp) 90, indicating that the ligand-induced conformational change takes place within the hetero-oligomeric structure and that the 711-984 region is sufficient for hsp90-MR interaction.	Aldosterone	48-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-135
8621522-0	1996	Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain.	Sulfhydryl Compounds	11-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
8621522-0	1996	Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain.	N-iodoacetyl-3-iodotyrosine	45-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
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
8621522-5	1996	Here, we assess the effects of hsp90 binding on the accessibility of cysteine residues in both the HBD and DBD to derivatization by a thiol-specific reagent.	Cysteine	69-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
8621522-5	1996	Here, we assess the effects of hsp90 binding on the accessibility of cysteine residues in both the HBD and DBD to derivatization by a thiol-specific reagent.	Sulfhydryl Compounds	134-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
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.	n-iodoacetyltyrosine	15-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
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
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.	Cysteine	190-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
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.	Dithiothreitol	203-217	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
8621522-7	1996	The 125I-labeled IAT derivative N-iodoacetyl-3-[125I]iodotyrosine ([125I]IAIT) covalently labels the immunopurified, hsp90-bound receptor in a thiol-specific manner.	N-iodoacetyl-3-iodotyrosine	32-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
8621522-7	1996	The 125I-labeled IAT derivative N-iodoacetyl-3-[125I]iodotyrosine ([125I]IAIT) covalently labels the immunopurified, hsp90-bound receptor in a thiol-specific manner.	Sulfhydryl Compounds	143-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
8621522-9	1996	The increase in thiol labeling is related to the presence of hsp90 because it is blocked by molybdate, which prevents hsp90 dissociation.	Sulfhydryl Compounds	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
8621522-9	1996	The increase in thiol labeling is related to the presence of hsp90 because it is blocked by molybdate, which prevents hsp90 dissociation.	Sulfhydryl Compounds	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
8621522-9	1996	The increase in thiol labeling is related to the presence of hsp90 because it is blocked by molybdate, which prevents hsp90 dissociation.	molybdate	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
8621522-9	1996	The increase in thiol labeling is related to the presence of hsp90 because it is blocked by molybdate, which prevents hsp90 dissociation.	molybdate	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
8621522-12	1996	These data are consistent with the proposal that dissociation of hsp90 from the GR produces a conformational change in the HBD such that some of the thiols that are exposed in the GR*hsp90 complex become buried and are no longer accessible to the [125I]IAIT probe.	Sulfhydryl Compounds	149-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
8621522-12	1996	These data are consistent with the proposal that dissociation of hsp90 from the GR produces a conformational change in the HBD such that some of the thiols that are exposed in the GR*hsp90 complex become buried and are no longer accessible to the [125I]IAIT probe.	Sulfhydryl Compounds	149-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
8621522-13	1996	In contrast, binding of the GR to hsp90 restricts access of cysteines in the DBD to this small thiol-derivatizing agent, a restriction that is relieved as a result of unmasking or conformational change accompanying hsp90 dissociation.	Cysteine	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
8621522-13	1996	In contrast, binding of the GR to hsp90 restricts access of cysteines in the DBD to this small thiol-derivatizing agent, a restriction that is relieved as a result of unmasking or conformational change accompanying hsp90 dissociation.	Cysteine	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
8621522-13	1996	In contrast, binding of the GR to hsp90 restricts access of cysteines in the DBD to this small thiol-derivatizing agent, a restriction that is relieved as a result of unmasking or conformational change accompanying hsp90 dissociation.	Sulfhydryl Compounds	95-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
8621522-13	1996	In contrast, binding of the GR to hsp90 restricts access of cysteines in the DBD to this small thiol-derivatizing agent, a restriction that is relieved as a result of unmasking or conformational change accompanying hsp90 dissociation.	Sulfhydryl Compounds	95-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
8615809-9	1996	In addition, we showed that the unbound and the aldosterone-bound 30 kDa fragment were both associated with heat-shock protein (hsp) 90, indicating that the ligand-induced conformational change takes place within the hetero-oligomeric structure and that the 711-984 region is sufficient for hsp90-MR interaction.	Aldosterone	48-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	291-296
8576234-4	1996	DHFR was released from the complex with HSP90 by incubating with GroEL/ES complexes in an ATP-dependent manner and refolded into the native form.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
9052936-3	1996	Synthesis of 70 kDa hsp (hsp70) and 90 kDa hsp (hsp90) was determined by SDS-PAGE and Western blot analysis in porcine day 6 embryos subjected to heat stresses.	Sodium Dodecyl Sulfate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
8645616-9	1996	These analyses demonstrated that the [3H]aldosterone-MBP-HBD complex is at least associated with hsp90 in reticulocyte lysate and that the HBD of hMR is sufficient to bind hsp90.	Tritium	38-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
8619831-0	1996	Oxidative stress response in iron-induced acute nephrotoxicity: enhanced expression of heat shock protein 90.	Iron	29-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-108
8619831-6	1996	Steady accumulation of HSP90 was observed in the subacute toxicity experiments with multiple injections of Fe-NTA, suggesting that the enhanced production of HSP90 is important in increasing resistance to subsequent injury caused by the Fe-NTA-induced oxidative stress.	ferric nitrilotriacetate	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
8619831-6	1996	Steady accumulation of HSP90 was observed in the subacute toxicity experiments with multiple injections of Fe-NTA, suggesting that the enhanced production of HSP90 is important in increasing resistance to subsequent injury caused by the Fe-NTA-induced oxidative stress.	ferric nitrilotriacetate	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
8619831-6	1996	Steady accumulation of HSP90 was observed in the subacute toxicity experiments with multiple injections of Fe-NTA, suggesting that the enhanced production of HSP90 is important in increasing resistance to subsequent injury caused by the Fe-NTA-induced oxidative stress.	ferric nitrilotriacetate	237-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
8619831-6	1996	Steady accumulation of HSP90 was observed in the subacute toxicity experiments with multiple injections of Fe-NTA, suggesting that the enhanced production of HSP90 is important in increasing resistance to subsequent injury caused by the Fe-NTA-induced oxidative stress.	ferric nitrilotriacetate	237-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
8838140-6	1996	GR/hsp90 complexes were stabilized in vivo by the introduction of sodium molybdate to cultured cells using a liposome-mediated delivery system.	sodium molybdate(VI)	66-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
8745575-3	1995	It was found that even though quercetin could specifically inhibit the expression of hsp90 alpha and hsp70 mRNA, it could not prevent GR from the decrease in response to the heat shock treatment.	Quercetin	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-96
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
7499384-0	1995	Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase.	Serine	18-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
7499384-0	1995	Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase.	Threonine	25-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
8524246-0	1995	Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent.	geldanamycin	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
8524246-2	1995	Using the selective hsp90 binding agent geldanamycin (GA), we have found that PR assembly in vitro can be arrested at a previously observed intermediate assembly step.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
8524246-2	1995	Using the selective hsp90 binding agent geldanamycin (GA), we have found that PR assembly in vitro can be arrested at a previously observed intermediate assembly step.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
8524246-5	1995	An important functional consequence of GA-mediated assembly arrest in vitro is the inability of the resulting PR complexes to bind progesterone, despite the presence of hsp90 in the receptor complexes.	geldanamycin	39-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
7588731-11	1995	Taken together, these results indicate that the dimeric structure of HSP90 alpha is mediated by the C-terminal 191 amino acids and consists of duplicate interactions of the C-terminal region (Met628/Ala629-Asp732) of one subunit and the adjacent more N-terminal region (Val542-Try627/Met628) of the other subunit.	try627	277-283	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-80
7581991-7	1995	HSP 70a and HSP 90 alpha expression were stimulated by oestradiol.	Estradiol	55-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-24
7581991-8	1995	Progesterone generally depressed HSP 90 alpha expression and simultaneous addition of both oestradiol and progesterone to the culture medium was antagonistic to HSP 90 alpha expression.	Estradiol	91-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-173
7581991-8	1995	Progesterone generally depressed HSP 90 alpha expression and simultaneous addition of both oestradiol and progesterone to the culture medium was antagonistic to HSP 90 alpha expression.	Progesterone	106-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-173
7782303-4	1995	Both procaryotic and eucaryotic members of the Hsp90 family were found to have very similar physicochemical properties: (i) they are stable against thermal unfolding up to at least 50 degrees C, (ii) they show biphasic, reversible unfolding transitions in guanidinium chloride, and (iii) their oligomerization state is strongly and rapidly affected by millimolar concentrations of divalent cations.	Guanidine	256-276	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
7592678-2	1995	The benzoquinone ansamycin, geldanamycin, specifically binds to Hsp90 and disrupts certain multimolecular complexes containing this protein.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
7592678-2	1995	The benzoquinone ansamycin, geldanamycin, specifically binds to Hsp90 and disrupts certain multimolecular complexes containing this protein.	geldanamycin	28-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
8578578-4	1995	Induction of monocytoid and granulocytoid differentiation with phorbor ester and ATRA was accompanied by increased expression of HSP73 and HSP90 with distinct kinetics.	phorbor ester	63-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
8578578-4	1995	Induction of monocytoid and granulocytoid differentiation with phorbor ester and ATRA was accompanied by increased expression of HSP73 and HSP90 with distinct kinetics.	Tretinoin	81-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
7476027-3	1995	In the present study, we determined that CSH treatment resulted in an increase in HSP 27, HSP 90 and heme oxygenase (HO-1) at both the protein and mRNA level.	csh	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-96
7794926-9	1995	Heparin, which binds to CKII alpha, inhibited the binding of CKII to HSP90-Sepharose.	Heparin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
7794926-9	1995	Heparin, which binds to CKII alpha, inhibited the binding of CKII to HSP90-Sepharose.	Sepharose	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
7782303-5	1995	In the presence of MnCl2 and MgCl2 defined changes in the quaternary structure of Hsp90 could be observed which resulted in a decrease in thermostability and an increased tendency to form larger aggregates.	manganese chloride	19-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
7782303-5	1995	In the presence of MnCl2 and MgCl2 defined changes in the quaternary structure of Hsp90 could be observed which resulted in a decrease in thermostability and an increased tendency to form larger aggregates.	Magnesium Chloride	29-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
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
7775471-0	1995	Differential expression and regulation of hsp70 and hsp90 by phorbol esters and heat shock.	Phorbol Esters	61-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
7779083-0	1995	ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: interference with the binding of heavy meromyosin.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
7779083-0	1995	ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: interference with the binding of heavy meromyosin.	meromyosin	119-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
7779083-2	1995	hsp90 has also been shown to bind ATP, which causes a conformational change of the protein.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
7779083-3	1995	The physiological role and significance of ATP binding by hsp90, however, has remained unclear.	Adenosine Triphosphate	43-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
7779083-4	1995	Here we show through direct, microscopic observations, that ATP induces the dissociation of actin filaments from immobilized molecules of hsp90 as well as the dissociation of F-actin from heavy meromyosin in the presence of hsp90.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
7779083-4	1995	Here we show through direct, microscopic observations, that ATP induces the dissociation of actin filaments from immobilized molecules of hsp90 as well as the dissociation of F-actin from heavy meromyosin in the presence of hsp90.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
7890776-2	1995	We have found earlier that the 50% homologous 90-kDa heat shock protein, hsp90, has ATP-binding site(s) and autophosphorylating activity (Csermely, P., and Kahn, C. R. (1991) J. Biol.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
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
7717993-2	1995	When the fusion protein was coupled to a GSH affinity matrix, heat-shock protein 90 (hsp90) was found to be the predominant associated protein in all tissue extracts examined.	Glutathione	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
7717993-2	1995	When the fusion protein was coupled to a GSH affinity matrix, heat-shock protein 90 (hsp90) was found to be the predominant associated protein in all tissue extracts examined.	Glutathione	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
8043004-4	1994	Upon removal of TG, normal protein synthesis is restored by 48 h. Immunoblots showed increased concentrations of the stress proteins HSP90, HSP72/73 and HSP60 in chondrocytes treated with TG, but induction of newly synthesized heat-shock proteins by TG was not apparent on [35S]methionine-labelled gels.	Thapsigargin	16-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
8089152-10	1994	Importantly, co-immunoprecipitation experiments showed that genistein inhibited ligand-induced release of hsp90 from the glucocorticoid receptor.	Genistein	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
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
8078881-0	1994	Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.	benzoquinone ansamycins	84-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
8078881-5	1994	In a range of cell lines, immobilized geldanamycin bound elements of a major class of heat shock protein (HSP90) in a stable and pharmacologically specific manner.	geldanamycin	38-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
8078881-6	1994	Consistent with these binding data, we found that soluble geldanamycin and herbimycin A inhibited specifically the formation of a previously described src-HSP90 heteroprotein complex.	geldanamycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
8078881-6	1994	Consistent with these binding data, we found that soluble geldanamycin and herbimycin A inhibited specifically the formation of a previously described src-HSP90 heteroprotein complex.	herbimycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
7882155-2	1994	In this study, we propose that domain III, common to the hsp60s and hsp70s is also found in the hsp90s and adopts a beta-alpha-beta Rossmann-folded structure which is encountered in the NAD-binding domain of dehydrogenases.	NAD	186-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
8043004-4	1994	Upon removal of TG, normal protein synthesis is restored by 48 h. Immunoblots showed increased concentrations of the stress proteins HSP90, HSP72/73 and HSP60 in chondrocytes treated with TG, but induction of newly synthesized heat-shock proteins by TG was not apparent on [35S]methionine-labelled gels.	Thapsigargin	188-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
8117717-0	1994	Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with Hsc70 and Hsp90.	gusperimus	57-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
7914036-3	1994	Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
8146188-4	1994	As a CKII substrate, recombinant hHSP90 beta displayed a Km of 9.8 microM and a kcat of 4.1 min-1 and was phosphorylated to 1.5 mol/mol, whereas ryHSP90, lacking the known serine CKII sites of hHSP90, was phosphorylated at a 19-fold lower kcat/Km ratio to levels of 0.8 mol/mol.	Serine	172-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-39
8139547-5	1994	Addition of a specific fraction from wild-type hepatoma cells, however, to the in vitro-expressed receptor promoted dioxin-dependent release of hsp90.	Dioxins	116-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
8139547-9	1994	In support of this model, addition of in vitro-expressed wild-type Arnt, but not a mutated form of Arnt lacking the bHLH motif, promoted release of hsp90 from the dioxin receptor in the presence of dioxin.	Dioxins	163-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
8208912-4	1994	We now present evidence that overexpression of hsp90 in lupus patients is associated with the presence of the anti-phospholipid syndrome, and with the absence of the HLA allo-/haplotypes most commonly found in this particular cohort of patients.	Phospholipids	115-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
8117717-6	1994	Glyoxylylspermidine and des(aminopropyl)DSG, two inactive metabolites, have much reduced affinity for Hsc70 and Hsp90.	glyoxylylspermidine	0-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
8117717-6	1994	Glyoxylylspermidine and des(aminopropyl)DSG, two inactive metabolites, have much reduced affinity for Hsc70 and Hsp90.	des(aminopropyl)dsg	24-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
8056761-0	1994	Association of the beta gamma subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90.	Guanosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
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
8056761-6	1994	The brain hsp90 inhibited beta gamma-supported pertussis toxin-catalyzed ADP-ribosylation of alpha subunits.	Adenosine Diphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
8056761-7	1994	The hsp90 was also capable of binding to beta gamma subunits which had been reconstituted into phospholipid vesicles.	Phospholipids	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
8056761-8	1994	The binding of hsp90 to beta gamma subunits was inhibited by the addition of GDP-bound alpha subunits, but not by GTP gamma S-bound ones.	Guanosine Diphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
8056761-8	1994	The binding of hsp90 to beta gamma subunits was inhibited by the addition of GDP-bound alpha subunits, but not by GTP gamma S-bound ones.	Guanosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
7907089-3	1994	The formation of the inactive form of HCI by hemin is prevented by treatment with sulfhydryl reagents such as N-ethylmaleimide or when hsp90 is previously phosphorylated (Mendez, R., Moreno, A., and de Haro, C. (1992) J. Biol.	Hemin	45-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
7907089-10	1994	The data strongly suggest that hemin promotes formation of an inactive HCI.hsp90 dimer preventing phosphorylation by CK II.	Hemin	31-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
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.	Tritium	36-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
8120027-4	1994	The Raf-hsp90-p50 complex was observed in starved cells and in cells activated with serum or phorbol ester.	Phorbol Esters	93-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
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
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.	tungstate	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
7906860-2	1993	Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes.	Progesterone	401-413	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
7906860-2	1993	Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes.	Progesterone	401-413	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
7906860-2	1993	Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes.	Progesterone	401-413	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
7906860-2	1993	Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes.	Progesterone	432-444	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
7906860-2	1993	Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes.	Progesterone	432-444	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
7906860-2	1993	Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes.	Progesterone	432-444	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
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.	dithiol	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
8348742-1	1993	During the phorbol myristate acetate (PMA)-induced differentiation of U937 cells to a macrophage-like phenotype, the levels of the heat shock proteins hsp90, hsp72 and hsp65 increased dramatically to a peak level following 24 h of treatment, and then declined.	Tetradecanoylphorbol Acetate	11-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
8348742-1	1993	During the phorbol myristate acetate (PMA)-induced differentiation of U937 cells to a macrophage-like phenotype, the levels of the heat shock proteins hsp90, hsp72 and hsp65 increased dramatically to a peak level following 24 h of treatment, and then declined.	Tetradecanoylphorbol Acetate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
7510997-9	1994	Purification of cytosol PR on immobilized FK506 yields a 9S form still containing hsp90, hsp70 and p59/HBI associated to PR units.	Tacrolimus	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
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
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.	Adenosine Monophosphate	266-269	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
7680324-4	1993	For heparin-binding sites, HSP90 was digested completely with trypsin, and the digests were applied to a heparin-Sepharose column and eluted with 1.0 M NaCl, followed by 8.0 M urea.	Heparin	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
8417966-0	1993	A metal-linked gapped zipper model is proposed for the hsp90-glucocorticoid receptor interaction.	Metals	2-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
8417966-3	1993	The heptads could interact hydrophobically with similar regions on the hsp90 homodimer, bringing putative metal binding residues on each protein close enough to establish a shared metal bridge.	Metals	106-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
8417966-3	1993	The heptads could interact hydrophobically with similar regions on the hsp90 homodimer, bringing putative metal binding residues on each protein close enough to establish a shared metal bridge.	Metals	180-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
7680324-4	1993	For heparin-binding sites, HSP90 was digested completely with trypsin, and the digests were applied to a heparin-Sepharose column and eluted with 1.0 M NaCl, followed by 8.0 M urea.	Sodium Chloride	152-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
7680324-4	1993	For heparin-binding sites, HSP90 was digested completely with trypsin, and the digests were applied to a heparin-Sepharose column and eluted with 1.0 M NaCl, followed by 8.0 M urea.	Urea	176-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
7680324-16	1993	For antibody-binding sites, HSP90 was mildly digested with trypsin, electrophoresed on SDS-polyacrylamide gels and transferred to PVDF membranes.	Sodium Dodecyl Sulfate	87-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
7680324-16	1993	For antibody-binding sites, HSP90 was mildly digested with trypsin, electrophoresed on SDS-polyacrylamide gels and transferred to PVDF membranes.	polyacrylamide	91-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
7680324-16	1993	For antibody-binding sites, HSP90 was mildly digested with trypsin, electrophoresed on SDS-polyacrylamide gels and transferred to PVDF membranes.	polyvinylidene fluoride	130-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
7680324-23	1993	Therefore, the epitopes of HSP90 are present between Pro-2 and Leu-282.	Leucine	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
7680324-25	1993	The heparin-binding sites are present from the middle region of the HSP90 molecule, and the antigen sites are at the N-terminal domain.	Heparin	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
1447308-1	1992	Submicromolar concentrations of tributyltin (TBT), a commercially used organotin compound, were found to induce the expression of several stress proteins, most notably HSP89 and HSP70, in IMR-90 human diploid fibroblasts in a time- and dose-dependent manner.	tributyltin	32-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
1447308-1	1992	Submicromolar concentrations of tributyltin (TBT), a commercially used organotin compound, were found to induce the expression of several stress proteins, most notably HSP89 and HSP70, in IMR-90 human diploid fibroblasts in a time- and dose-dependent manner.	tributyltin	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
1482554-4	1992	However, Ishikawa cells treated with 10(-5) M of the antimicrotubule agents colchicine or triethyl lead showed residual filamentous structures stained with anti-HSP90 antibodies, while no microtubules were visualized with anti-tubulin antibodies.	Colchicine	76-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
1491008-8	1992	From these results it was suggested that the conformation of purified vero ER tends to change quickly in a time dependent manner, and so a chemical perturbant, NaSCN, is generally necessary for the reconstitution of 9 S ER from purified vero ER and purified hsp 90.	sodium thiocyanate	160-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	258-264
1482554-4	1992	However, Ishikawa cells treated with 10(-5) M of the antimicrotubule agents colchicine or triethyl lead showed residual filamentous structures stained with anti-HSP90 antibodies, while no microtubules were visualized with anti-tubulin antibodies.	triethyllead	90-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
1482554-5	1992	In the presence of 10(-5) M cytochalasin B, the microfilament staining of the cells disappeared, while residual filamentous structures were labeled with anti-HSP90 antibodies.	Cytochalasin B	28-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
1482554-7	1992	Conversely, similar reorganized morphology of filamentous structures stained with both anti-HSP90 and anti-cytokeratins antibodies were observed when Ishikawa cells were treated with 2 x 10(-5) M cytochalasin B and 2 x 10(-5) M colchicine.	Cytochalasin B	196-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
1482554-8	1992	HSP90 was also present in Ishikawa cell preparations of the Triton X-100 insoluble cytoskeleton.	Octoxynol	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
1508207-1	1992	Hemin induces nonterminal differentiation of human K562 erythroleukemia cells, which is accompanied by the expression of certain erythroid cell-specific genes, such as the embryonic and fetal globins, and elevated expression of the stress genes hsp70, hsp90, and grp78/BiP.	Hemin	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	252-257
1376003-3	1992	A 59-kilodalton member of the FK506- and rapamycin-binding class was found to associate in the absence of these drugs with two heat shock proteins (hsp90 and hsp70) and the glucocorticoid receptor (GR).	Tacrolimus	30-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
1525047-3	1992	This antibody was able to complex both free and rabbit uterine progesterone receptor-associated hsp90 as demonstrated by sedimentation analysis on sucrose gradients.	Sucrose	147-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
1425772-6	1992	A major part of hsp90 immunoreactivity was diffusely distributed throughout the interphase cytoplasm, but a weak nuclear staining with non-stained nucleoli was also present, however, only detectable after methanol and not after formaldehyde/Triton X-100 fixation.	Formaldehyde	228-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
1425772-6	1992	A major part of hsp90 immunoreactivity was diffusely distributed throughout the interphase cytoplasm, but a weak nuclear staining with non-stained nucleoli was also present, however, only detectable after methanol and not after formaldehyde/Triton X-100 fixation.	Octoxynol	241-253	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
1504008-9	1992	The PR-hsp90 association was stabilized in the presence of 10 mM iodoacetamide when the ligand binding site was occupied by Org 31806 and 31710.	Iodoacetamide	65-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-12
1304385-2	1992	Because no ATPase activity has previously been reported for the hsp90 class, ATP utilization by C. fasciculata hsp83 was characterized: this hsp83 has an ATPase kcat of 150 min-1 and a Km of 60 microM, whereas the homologous mammalian hsp90 binds ATP but has no ATPase activity.	Adenosine Triphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
1304385-2	1992	Because no ATPase activity has previously been reported for the hsp90 class, ATP utilization by C. fasciculata hsp83 was characterized: this hsp83 has an ATPase kcat of 150 min-1 and a Km of 60 microM, whereas the homologous mammalian hsp90 binds ATP but has no ATPase activity.	Adenosine Triphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	235-240
1497645-4	1992	Furthermore, a combination of low pH and quercetin treatment distinctively altered the expression of HSP70 gene compared with that of HSP28 or HSP90 gene.	Quercetin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
1629193-0	1992	The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal.	molybdate	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
1629193-0	1992	The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal.	Vanadates	84-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
1629193-0	1992	The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal.	tungstate	94-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
1629193-0	1992	The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal.	Metals	133-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
1629193-6	1992	The pp60v-src-hsp90 complex is stabilized by sodium molybdate with the same concentration dependence as the glucocorticoid receptor-hsp90 complex.	sodium molybdate(VI)	45-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
1629193-7	1992	As with the steroid receptor heterocomplexes, vanadate and tungstate also stabilize the pp60v-src-hsp90 interaction.	Vanadates	46-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
1629193-7	1992	As with the steroid receptor heterocomplexes, vanadate and tungstate also stabilize the pp60v-src-hsp90 interaction.	tungstate	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
1629193-8	1992	Passage of cytosol through a Chelex-100 metal-chelating resin destabilizes the native pp60v-src-hsp90 complex, suggesting that the complex is normally stabilized by an endogenous metal factor.	Chelex 100	29-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
1629193-8	1992	Passage of cytosol through a Chelex-100 metal-chelating resin destabilizes the native pp60v-src-hsp90 complex, suggesting that the complex is normally stabilized by an endogenous metal factor.	Metals	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
1629193-8	1992	Passage of cytosol through a Chelex-100 metal-chelating resin destabilizes the native pp60v-src-hsp90 complex, suggesting that the complex is normally stabilized by an endogenous metal factor.	Metals	179-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
1629193-10	1992	Molybdate also stabilizes the presence of p50, a known hsp90-associated protein, in the pp60v-src heterocomplex.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
1631114-1	1992	Treatment of human K562 erythroleukemia cells with the antiproliferative prostaglandin A1 results in the elevated transcription of two heat shock genes, HSP70 and HSP90.	Prostaglandins	73-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
1614549-6	1992	The action of Hsp90 does not depend on the presence of nucleoside triphosphates, so it may be that Hsp90 uses a novel molecular mechanism to assist protein folding in vivo.	nucleoside triphosphates	55-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
1551911-3	1992	The protein kinase was separable from HSP90 by adsorption to heparin-Sepharose or phosphocellulose.	Heparin	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
1551911-3	1992	The protein kinase was separable from HSP90 by adsorption to heparin-Sepharose or phosphocellulose.	Sepharose	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
1551911-5	1992	Sucrose density gradient centrifugation analysis revealed that an addition of anti-HSP90 antibodies to cell extracts induces a shift of the sedimentation peak of CKII toward the bottom of a centrifuge tube.	Sucrose	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
1551911-6	1992	These results suggest that CKII is associated with HSP90 in cell lysates at low salt conditions.	Salts	80-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
1312348-2	1992	Receptors activated by hormone binding in vivo and extracted from nuclei with 0.5 M NaCl no longer associate with hsp 90 but retain association with hsp 70.	Sodium Chloride	84-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-120
1312348-12	1992	Interestingly, sodium arsenite produced both a greater induction of hsp 90 and hsp 70 synthesis and a greater fold enhancement of PR-mediated gene transcription than did heat shock.	sodium arsenite	15-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-74
1376003-3	1992	A 59-kilodalton member of the FK506- and rapamycin-binding class was found to associate in the absence of these drugs with two heat shock proteins (hsp90 and hsp70) and the glucocorticoid receptor (GR).	Sirolimus	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
1314085-0	1992	Differences between aldosterone and its antagonists in binding kinetics and ligand-induced hsp90 release from mineralocorticosteroid receptor.	Aldosterone	20-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
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
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
1890971-2	1991	Secondary structure analyses of the hsp 90 molecule reveal the presence of a cysteine-containing, leucine-rich, heptad repeat, which we refer to as region C. Similar analyses on the hER, at its hormone binding domain (HBD), have indicated the presence of a central subdomain bordered by 2 alpha-helical flanking segments which also display the heptad substructure.	Cysteine	77-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-42
1310678-5	1992	The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate.	molybdate	151-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
1915656-2	1991	The study was prompted by earlier data showing that one of the heat shock proteins (HSP90) is an essential component of the GR complex and that treatment of mammalian cells with hydrocortisone induces resistance to heat damage.	Hydrocortisone	178-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
1936287-4	1991	This increased turnover of hsp90 phosphate groups might reflect a greater protein binding activity of hsp90 in stressed cells.	Phosphates	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
1936287-4	1991	This increased turnover of hsp90 phosphate groups might reflect a greater protein binding activity of hsp90 in stressed cells.	Phosphates	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
1909966-5	1991	SDH (10 min, 45 degrees C + 1 to 6 h, 41.5 degrees C) completely inhibited labeling of HSP110, partially inhibited HSP90 labeling, and had virtually no effect on HSP72/70 synthesis, when compared with chronic hyperthermia alone.	sdh	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
1754738-2	1991	We observed an increase in mRNA levels of heat-shock protein (hsp) 70, hsp 90, hsp 32 and metallothionein after treatment of GOTO cells with cadmium, although the time courses of the changes of individual mRNA of the heat-shock proteins and metallothionein were somewhat different from each other.	Cadmium	141-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-77
1890971-2	1991	Secondary structure analyses of the hsp 90 molecule reveal the presence of a cysteine-containing, leucine-rich, heptad repeat, which we refer to as region C. Similar analyses on the hER, at its hormone binding domain (HBD), have indicated the presence of a central subdomain bordered by 2 alpha-helical flanking segments which also display the heptad substructure.	Leucine	98-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-42
2052560-1	1991	Treatment of cultured human tumor cells with the chloroethylnitrosourea antitumor drug 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) selectively induces transcription and protein synthesis of a subset of the human heat shock or stress-induced genes (HSP90 and HSP70) with little effect on other stress genes or on expression of the c-fos, c-myc, or beta-actin genes.	1-(2-chloroethyl)-1-nitrosourea	49-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	248-253
2052560-1	1991	Treatment of cultured human tumor cells with the chloroethylnitrosourea antitumor drug 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) selectively induces transcription and protein synthesis of a subset of the human heat shock or stress-induced genes (HSP90 and HSP70) with little effect on other stress genes or on expression of the c-fos, c-myc, or beta-actin genes.	Carmustine	87-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	248-253
2052560-1	1991	Treatment of cultured human tumor cells with the chloroethylnitrosourea antitumor drug 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) selectively induces transcription and protein synthesis of a subset of the human heat shock or stress-induced genes (HSP90 and HSP70) with little effect on other stress genes or on expression of the c-fos, c-myc, or beta-actin genes.	Carmustine	125-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	248-253
2052560-5	1991	This suggests that BCNU-induced, isocyanate-mediated damage to newly synthesized protein(s) may be responsible for activation of the heat shock transcription factor and increased transcription of the HSP90 and HSP70 genes.	Carmustine	19-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
2052560-5	1991	This suggests that BCNU-induced, isocyanate-mediated damage to newly synthesized protein(s) may be responsible for activation of the heat shock transcription factor and increased transcription of the HSP90 and HSP70 genes.	Isocyanates	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
2002041-0	1991	The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-37
2002041-2	1991	Incubation of highly purified hsp-90 with [gamma-32P]ATP results in its autophosphorylation on serine residues.	[gamma-32p]atp	42-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-36
2002041-2	1991	Incubation of highly purified hsp-90 with [gamma-32P]ATP results in its autophosphorylation on serine residues.	Serine	95-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-36
2002041-8	1991	6) Finally, and most importantly, purified hsp-90 can be labeled with azido-ATP and it is able to bind to ATP-agarose.	azido-atp	70-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-49
2002041-8	1991	6) Finally, and most importantly, purified hsp-90 can be labeled with azido-ATP and it is able to bind to ATP-agarose.	ATP-sepharose	106-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-49
2002259-5	1991	Exposure of these cells to weak inducing agents such as heat or cadmium sulphate resulted in the synthesis of HSP72 and HSP90, whereas HSP28 and HSP116 synthesis was detected in keratinocytes and fibroblasts following exposure to the strong inducing agent sodium arsenite.	cadmium sulfate	64-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
2241151-9	1990	The brain HSP90 was separable from glucocorticoid receptor by heparin-agarose and DNA-cellulose columns.	Heparin	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
2051300-8	1991	Dexamethasone 17 beta-carboxamide derivates share with all other antiglucocorticoids tested the same ability to stabilize a high molecular form of the receptor associated to HSP90, a heat shock protein, in intact cells.	Dexamethasone	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
2051300-8	1991	Dexamethasone 17 beta-carboxamide derivates share with all other antiglucocorticoids tested the same ability to stabilize a high molecular form of the receptor associated to HSP90, a heat shock protein, in intact cells.	beta-carboxamide	17-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
2282978-2	1990	The heat shock protein (hsp-90) bound to receptor was precipitated with monoclonal antibodies H222 or JS 34/32, coupled to protein A-Sepharose and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions.	Sepharose	133-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-30
2282978-2	1990	The heat shock protein (hsp-90) bound to receptor was precipitated with monoclonal antibodies H222 or JS 34/32, coupled to protein A-Sepharose and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions.	Sodium Dodecyl Sulfate	159-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-30
2282978-2	1990	The heat shock protein (hsp-90) bound to receptor was precipitated with monoclonal antibodies H222 or JS 34/32, coupled to protein A-Sepharose and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions.	polyacrylamide gels	182-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-30
2282978-2	1990	The heat shock protein (hsp-90) bound to receptor was precipitated with monoclonal antibodies H222 or JS 34/32, coupled to protein A-Sepharose and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions.	Sodium Dodecyl Sulfate	218-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-30
2282978-4	1990	It was found that estradiol treatment of the cells markedly increased phosphate incorporation in the free hsp-90, without affecting heat shock protein bound to receptor.	Estradiol	18-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-112
2282978-4	1990	It was found that estradiol treatment of the cells markedly increased phosphate incorporation in the free hsp-90, without affecting heat shock protein bound to receptor.	Phosphates	70-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-112
2282978-8	1990	A 50% reduction of the phosphate content in the free hsp-90 was observed after 15 min treatment.	Phosphates	23-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-59
2282978-9	1990	The observation that estradiol, TPA and forskolin had effect only on hsp-90 not bound to receptor is an indication that the receptor-hsp-90 complex exists in vivo.	Estradiol	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-75
2282978-9	1990	The observation that estradiol, TPA and forskolin had effect only on hsp-90 not bound to receptor is an indication that the receptor-hsp-90 complex exists in vivo.	Estradiol	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-139
2282978-9	1990	The observation that estradiol, TPA and forskolin had effect only on hsp-90 not bound to receptor is an indication that the receptor-hsp-90 complex exists in vivo.	Tetradecanoylphorbol Acetate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-75
2282978-9	1990	The observation that estradiol, TPA and forskolin had effect only on hsp-90 not bound to receptor is an indication that the receptor-hsp-90 complex exists in vivo.	Tetradecanoylphorbol Acetate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-139
2282978-9	1990	The observation that estradiol, TPA and forskolin had effect only on hsp-90 not bound to receptor is an indication that the receptor-hsp-90 complex exists in vivo.	Colforsin	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-75
2282978-9	1990	The observation that estradiol, TPA and forskolin had effect only on hsp-90 not bound to receptor is an indication that the receptor-hsp-90 complex exists in vivo.	Colforsin	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-139
2282978-12	1990	Either estradiol induces an increase in the degree of phosphorylation of hsp-90, or hsp-90 is translocated to the cytosol from a different cellular compartment.	Estradiol	7-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-79
15374479-8	1990	At these concentrations, idebenone induced a slight, but detectable, enhancement of the intracellular stress proteins, HSP70 and HSP90.	idebenone	25-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
2247067-6	1990	Previously we showed that the dsDNA-activated kinase phosphorylates two threonines at the N terminus of hsp90 alpha (S. P. Lees-Miller and C. W. Anderson, J. Biol.	Threonine	72-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-115
2241151-9	1990	The brain HSP90 was separable from glucocorticoid receptor by heparin-agarose and DNA-cellulose columns.	Sepharose	70-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
2365690-1	1990	Hydrogen peroxide produces all of the effects on glucocorticoid receptors that are produced by molybdate, including stabilization of the receptor 90-kDa heat shock protein (hsp90) complex (Tienrungroj, W., Meshinchi, S., Sanchez, E. R., Pratt, S. E., Grippo, J. F., Holmgren, A., and Pratt, W. B.	Hydrogen Peroxide	0-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
2365690-1	1990	Hydrogen peroxide produces all of the effects on glucocorticoid receptors that are produced by molybdate, including stabilization of the receptor 90-kDa heat shock protein (hsp90) complex (Tienrungroj, W., Meshinchi, S., Sanchez, E. R., Pratt, S. E., Grippo, J. F., Holmgren, A., and Pratt, W. B.	molybdate	95-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
2365690-13	1990	These modifications occur in a region of the receptor that is known to contain its sites of interaction with both hsp90 and molybdate, with the latter having a well-established avidity for sulfur.	Sulfur	189-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
2318869-5	1990	In this work, we demonstrate that removal of this factor by passage of L cell cytosol through the metal-chelating resin Chelex-100 makes the glucocorticoid receptor unstable, thus markedly facilitating both its dissociation from hsp90 and its transformation to the DNA-binding state.	Metals	98-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	229-234
2191718-7	1990	The effects of aluminum fluoride are due to stabilization of the complex between the glucocorticoid receptor and the 90-kDa mammalian heat-shock protein hsp90, which suggests that aluminum fluoride interacts directly with the receptor.	aluminum fluoride	15-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
2191718-7	1990	The effects of aluminum fluoride are due to stabilization of the complex between the glucocorticoid receptor and the 90-kDa mammalian heat-shock protein hsp90, which suggests that aluminum fluoride interacts directly with the receptor.	aluminum fluoride	180-197	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
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
2355020-5	1990	In 0.4 M KCl, tungstate-stabilized (but not molybdate-stabilized) PR, AR, ER, and GR retained hsp90, but lost p59.	tungstate	14-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
2355020-6	1990	Dimethylpimelimidate cross-linking prevented p59 dissociation from hsp90-receptor complexes.	dimethyl pimelimidate	0-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
2318869-5	1990	In this work, we demonstrate that removal of this factor by passage of L cell cytosol through the metal-chelating resin Chelex-100 makes the glucocorticoid receptor unstable, thus markedly facilitating both its dissociation from hsp90 and its transformation to the DNA-binding state.	Chelex 100	120-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	229-234
2318869-7	1990	In the Chelex-treated, metal-depleted cytosol, however, temperature-mediated dissociation of hsp90 and receptor transformation occur very rapidly in a manner that is no longer hormone-dependent.	chelex	7-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
2318869-7	1990	In the Chelex-treated, metal-depleted cytosol, however, temperature-mediated dissociation of hsp90 and receptor transformation occur very rapidly in a manner that is no longer hormone-dependent.	Metals	23-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
2318869-8	1990	When boiled L cell cytosol is added to the metal-depleted receptor system, the hormone dependence of both temperature-mediated dissociation of receptor from hsp90 and receptor transformation to the DNA-binding state is reconstituted.	Metals	43-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
33794753-9	2021	STA-9090 inhibited ATP hydrolysis and protein folding process of HSP90.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
2405907-1	1990	We have used three methods to measure the stoichiometry of the glucocorticoid receptor and the 90-kDa heat shock protein (hsp90) in L-cell glucocorticoid receptor complexes that were purified by immunoadsorption to protein A-Sepharose with an anti-receptor monoclonal antibody, followed by a minimal washing procedure that permits retention of receptor-associated protein.	Sepharose	225-234	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
2405907-4	1990	In a third method, which detects total receptor protein rather than just steroid-bound receptor, the ratio of hsp90 to receptor was determined by immunopurifying receptor complexes from [35S]methionine-labeled L cells, and the amount of 35S incorporated into receptor and hsp90 was corrected for the established methionine content of the respective proteins.	Sulfur-35	187-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
2405907-4	1990	In a third method, which detects total receptor protein rather than just steroid-bound receptor, the ratio of hsp90 to receptor was determined by immunopurifying receptor complexes from [35S]methionine-labeled L cells, and the amount of 35S incorporated into receptor and hsp90 was corrected for the established methionine content of the respective proteins.	Methionine	191-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
2405907-4	1990	In a third method, which detects total receptor protein rather than just steroid-bound receptor, the ratio of hsp90 to receptor was determined by immunopurifying receptor complexes from [35S]methionine-labeled L cells, and the amount of 35S incorporated into receptor and hsp90 was corrected for the established methionine content of the respective proteins.	Sulfur-35	237-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
2405907-4	1990	In a third method, which detects total receptor protein rather than just steroid-bound receptor, the ratio of hsp90 to receptor was determined by immunopurifying receptor complexes from [35S]methionine-labeled L cells, and the amount of 35S incorporated into receptor and hsp90 was corrected for the established methionine content of the respective proteins.	Methionine	312-322	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
2405907-6	1990	When immunoadsorbed receptor complexes are washed extensively with 0.5 M NaCl and 0.4% Triton X-100 in the presence of molybdate, the ratio of hsp90 to GR is 2:1.	Sodium Chloride	73-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
2405907-6	1990	When immunoadsorbed receptor complexes are washed extensively with 0.5 M NaCl and 0.4% Triton X-100 in the presence of molybdate, the ratio of hsp90 to GR is 2:1.	molybdate	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
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
2340977-7	1990	Sodium arsenite induced the highest levels of synthesis of these two proteins, approximately 10-fold and 3-fold increases in hsp-70 and hsp-90, respectively.	sodium arsenite	0-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-142
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
33031796-0	2020	Sulfoxythiocarbamate S-4 inhibits HSP90 in human cutaneous squamous cell carcinoma cells.	sulfoxythiocarbamate	0-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
33921173-10	2021	The findings indicate that the pharmacological action of PG against GC might be associated with the regulation of three core targets: HSP90AA1, CDK2, and MMP1.	pg	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-142
33768253-0	2021	A cyclic lipopeptide surfactin is a species-selective Hsp90 inhibitor that suppresses cyanobacterial growth.	surfactin peptide	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
33768253-3	2021	We found that a cyclic lipopeptide surfactin inhibits the ATPase activity of Hsp90 from the cyanobacterium Synechococcus elongatus (S. elongatus) PCC 7942 but does not inhibit Escherichia coli (E. coli), yeast and human Hsp90s.	surfactin peptide	35-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
33768253-4	2021	Molecular docking simulations indicated that surfactin could bind to the N-terminal dimerization interface of the cyanobacterial Hsp90 in the ATP- and ADP-bound states, which provided molecular insights into the species-selective inhibition.	surfactin peptide	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
33768253-4	2021	Molecular docking simulations indicated that surfactin could bind to the N-terminal dimerization interface of the cyanobacterial Hsp90 in the ATP- and ADP-bound states, which provided molecular insights into the species-selective inhibition.	Adenosine Triphosphate	142-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
33768253-4	2021	Molecular docking simulations indicated that surfactin could bind to the N-terminal dimerization interface of the cyanobacterial Hsp90 in the ATP- and ADP-bound states, which provided molecular insights into the species-selective inhibition.	Adenosine Diphosphate	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
33768253-5	2021	The data suggest that surfactin inhibits a rate-limiting conformational change of S. elongatus Hsp90 in the ATP hydrolysis.	surfactin peptide	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
33768253-5	2021	The data suggest that surfactin inhibits a rate-limiting conformational change of S. elongatus Hsp90 in the ATP hydrolysis.	Adenosine Triphosphate	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
33768253-6	2021	Surfactin also inhibited the interaction of the cyanobacterial Hsp90 with a model substrate, and suppressed S. elongatus growth under heat stress, but not that of E. coli.	surfactin peptide	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
33768253-8	2021	These results indicate that surfactin inhibits the cellular function of Hsp90 specifically in the cyanobacterium.	surfactin peptide	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
33031796-4	2020	We previously identified sulfoxythiocarbamate S-4 as an HSP90 inhibitor.	sulfoxythiocarbamate	25-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
32796651-5	2020	It is one of the most studied Hsp90 inhibitors for a variety of cancers in Phase I and II clinical trials and is similar to its predecessors such as the ansamycin class of molecules.	Rifabutin	153-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
27666928-0	2016	The purine scaffold Hsp90 inhibitor PU-H71 sensitizes cancer cells to heavy ion radiation by inhibiting DNA repair by homologous recombination and non-homologous end joining.	purine	4-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32795627-1	2020	Compount 7t, 4-(4-bromophenyl)-6-(1-(4-chlorophenyl)-3-(4-nitrophenyl)-1H-pyrazol-4-yl) pyrimidin-2-amine, is a proven potent anticancer agent exhibiting Hsp90 inhibition in our previous studies.	t, 4-(4-bromophenyl)-6-(1-(4-chlorophenyl)-3-(4-nitrophenyl)-1h-pyrazol-4-yl) pyrimidin-2-amine	10-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
28143869-9	2017	Administration of 17-AAG or PU-H71, two distinct Hsp90 inhibitors, depletes ICN1, inhibits T-ALL cell proliferation, and triggers dramatic apoptotic cell death.	tanespimycin	18-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
32795627-0	2020	Novel anticancer Hsp90 inhibitor disubstituted pyrazolyl 2-aminopyrimidine compound 7t induces cell cycle arrest and apoptosis via mitochondrial pathway in MCF-7 cells.	pyrazolyl 2-aminopyrimidine	47-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
27666928-1	2016	BACKGROUND AND PURPOSE: PU-H71 is a purine-scaffold Hsp90 inhibitor developed to overcome limitations of conventional Hsp90 inhibitors.	purine	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
11701613-0	2001	Hsp90 and caveolin are key targets for the proangiogenic nitric oxide-mediated effects of statins.	Nitric Oxide	57-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24750035-9	2015	Furthermore, we demonstrated that CSE, the main vascular H2S-synthesizing enzyme, is physically associated with the NR3C4/hsp90 complex and the generation of such a ternary system represents a key event leading to CSE activation.	Hydrogen Sulfide	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
11701613-9	2001	Finally, we showed that statin promoted the tyrosine phosphorylation of hsp90 and the direct interaction of hsp90 with Akt, which further potentiated the NO-dependent angiogenic processes.	Tyrosine	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24750035-7	2015	The NR3C4-multicomplex-derived heat shock protein 90 (hsp90) was also involved in this effect; its specific inhibitor geldanamycin strongly reduced testosterone-induced H2S production.	geldanamycin	118-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-52
24750035-7	2015	The NR3C4-multicomplex-derived heat shock protein 90 (hsp90) was also involved in this effect; its specific inhibitor geldanamycin strongly reduced testosterone-induced H2S production.	geldanamycin	118-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
24750035-7	2015	The NR3C4-multicomplex-derived heat shock protein 90 (hsp90) was also involved in this effect; its specific inhibitor geldanamycin strongly reduced testosterone-induced H2S production.	Testosterone	148-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-52
24750035-7	2015	The NR3C4-multicomplex-derived heat shock protein 90 (hsp90) was also involved in this effect; its specific inhibitor geldanamycin strongly reduced testosterone-induced H2S production.	Testosterone	148-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
24750035-7	2015	The NR3C4-multicomplex-derived heat shock protein 90 (hsp90) was also involved in this effect; its specific inhibitor geldanamycin strongly reduced testosterone-induced H2S production.	Hydrogen Sulfide	169-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-52
24750035-7	2015	The NR3C4-multicomplex-derived heat shock protein 90 (hsp90) was also involved in this effect; its specific inhibitor geldanamycin strongly reduced testosterone-induced H2S production.	Hydrogen Sulfide	169-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
34954542-0	2022	HSP90 inhibitors 17-AAG and VER-82576 inhibit porcine deltacoronavirus replication in vitro.	NVP-BEP800	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
34802714-7	2022	Our analysis showed that the anti-angiogenic activity of CDDO-Im is mediated by its inhibition of the expression of PLAT, ETS1, A2M, SPAG9, RASGRP3, FBXO32, GCNT1 and HDGFRP3 and its direct interactions with EGFR, mTOR, NOS2, HSP90AA1, MDM2, SYK, IRF3, ATR and KIF14.	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-234
34958756-0	2022	Theaflavin-3-gallate, a natural antagonist for Hsp90: In-silico and in-vitro approach.	Theaflavin 3-gallate	0-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
34958756-4	2022	In the present study, screening and stimulation of potential natural compounds result in the identification of theaflavin-3-gallate as a promising inhibitory compound of Hsp90.	Theaflavin 3-gallate	111-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
34958756-8	2022	Furthermore, theaflavin-3-gallate significantly downregulated the mRNA expression patterns of the HSP90, MMP9, VEGFA, and SPP1 genes.	Theaflavin 3-gallate	13-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
34958756-9	2022	Collectively, our results demonstrated theaflavin-3-gallate as a potential natural Hsp90 inhibitor that can be used to enhance the therapeutic efficacy of existing breast cancer therapies and improve overall survival of breast cancer patients.	Theaflavin 3-gallate	39-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
34954542-8	2022	From our data we can conclude that the HSP90 inhibitors 17-AAG and VER-82576 are promising candidates for the treatment of PDCoV infection.	NVP-BEP800	67-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
34791698-4	2022	We found that HSP90 inhibitor geldanamycin and aldosterone antagonist spironolactone reduced DPR levels by promoting protein degradation via the proteasome and autophagy pathways respectively.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
34844036-0	2022	Novel O-acylated (E)-3-aryl-6,7-dihydrobenzisoxazol-4(5H)-one oximes targeting HSP90-HER2 axis in breast cancer cells.	o-acylated (e)-3-aryl-6,7-dihydrobenzisoxazol-4(5h)-one	6-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
34844036-0	2022	Novel O-acylated (E)-3-aryl-6,7-dihydrobenzisoxazol-4(5H)-one oximes targeting HSP90-HER2 axis in breast cancer cells.	Oximes	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
34844036-1	2022	Novel O-acylated (E)-3-aryl-6,7-dihydrobenzisoxazol-4(5H)-one oximes were designed as potential HSP90 inhibitors.	o-acylated (e)-3-aryl-6,7-dihydrobenzisoxazol-4(5h)-one	6-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
34844036-1	2022	Novel O-acylated (E)-3-aryl-6,7-dihydrobenzisoxazol-4(5H)-one oximes were designed as potential HSP90 inhibitors.	Oximes	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
34763035-5	2021	Flow cytometric studies tracking HER2 surface expression revealed ~ 10 nM geldanamycin (GA) as the threshold for inhibiting HSP90 mediated HER2 recycling.	geldanamycin	74-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
34637110-5	2022	In our label-free, high-throughput, quantitative LC-MS/MS-based proteomic studies of MDA-MB-231, human, triple-negative breast cancer cells, treated with electrical pulses (EP) and cisplatin (CsP), we identified a number of HSPs, such as HSP90AA1, and others to be significantly downregulated in EP + CsP, compared to CsP alone.	Cisplatin	181-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	238-246
34937942-8	2022	Hop interacts with all components of the complex, including GR, and poises Hsp90 for subsequent ATP hydrolysis.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
34231170-9	2022	The ten hub targets for quercetin in preventing preterm birth were AKT serine/threonine kinase 1, mitogen-activated protein kinase 3, epidermal growth factor receptor, prostaglandin-endoperoxide synthase 2, mitogen-activated protein kinase 1, estrogen receptor 1, heat shock protein 90 alpha family class A member 1, mitogen-activated protein kinase 8, androgen receptor, and matrix metallopeptidase 9.	Quercetin	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	264-315
34945845-3	2021	Many of the clients of Hsp90 are found in pathways known to be pathogenic in the heart, ranging from transforming growth factor beta (TGF-beta) and mitogen activated kinase (MAPK) signaling to tumor necrosis factor alpha (TNFalpha), Gs and Gq g-protein coupled receptor (GPCR) and calcium (Ca2+) signaling.	Calcium	281-288	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
34962586-4	2021	The aim of the study has been on the eugenol compounds, which has potent actions on Eralpha, PR, EGFR, CDK2, mTOR, ERBB2, c-Src, HSP90, and chemokines receptors inhibition.	Eugenol	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
34786537-0	2021	Oral Hsp90 inhibitor SNX-5422 attenuates SARS-CoV-2 replication and dampens inflammation in airway cells.	SNX-5422	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
34786537-4	2021	We demonstrate that an orally bioavailable Hsp90 inhibitor, SNX-5422, currently in clinical trials as an anti-cancer therapeutic, inhibits SARS-CoV-2 replication in vitro at a high selectivity index.	SNX-5422	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
34593531-1	2021	PURPOSE: This is a phase 1b trial of TAS-116, an oral HSP90 inhibitor, plus nivolumab for colorectal cancer (CRC) and other solid tumors.	TAS-116	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
34976842-4	2021	In clinical specimens, the expression level of A20 did not relate with the outcome in patients receiving sorafenib; however, high levels of HSP90 were associated with poor outcomes in these patients.	Sorafenib	105-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
34763035-5	2021	Flow cytometric studies tracking HER2 surface expression revealed ~ 10 nM geldanamycin (GA) as the threshold for inhibiting HSP90 mediated HER2 recycling.	geldanamycin	88-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
34887522-3	2022	We performed in vivo preclinical studies of the HSP90 inhibitor onalespib with olaparib and conducted a Phase 1 combination study.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	64-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
34887522-3	2022	We performed in vivo preclinical studies of the HSP90 inhibitor onalespib with olaparib and conducted a Phase 1 combination study.	olaparib	79-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
34884975-3	2021	Excitingly, we screened out heat shock protein 90 alpha (HSP90A), a key regulatory protein associated with liver cancer, as a potential target of (20S) G-Rh2 by phage display analysis and mass spectrometry.	ginsenoside Rh2	152-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-63
34957217-1	2021	The Hsp90 molecular chaperone, along with a set of approximately 50 cochaperones, mediates the folding and activation of hundreds of cellular proteins in an ATP-dependent cycle.	Adenosine Triphosphate	157-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
34944784-4	2021	In the case of resistant PDAC cells, we identified a synergism of cisplatin with HSP90 inhibitors.	Cisplatin	66-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
34944784-7	2021	On top of this, HSP90 inhibition also enhanced the accumulation of DNA-bound platinum.	Platinum	77-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
34944784-9	2021	Here again, when treating established tumors, the combination of cisplatin with the HSP90 inhibitor onalespib was highly effective and almost completely prevented further tumor growth.	Cisplatin	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
34944784-9	2021	Here again, when treating established tumors, the combination of cisplatin with the HSP90 inhibitor onalespib was highly effective and almost completely prevented further tumor growth.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
34884975-8	2021	Taken together, this study for the first time reveals that (20S) G-Rh2 exerts its anti-tumor effect by targeting HSP90A and consequently disturbing the HSP90A-Cdc37 chaperone system.	ginsenoside Rh2	65-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-119
34884975-8	2021	Taken together, this study for the first time reveals that (20S) G-Rh2 exerts its anti-tumor effect by targeting HSP90A and consequently disturbing the HSP90A-Cdc37 chaperone system.	ginsenoside Rh2	65-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-158
34956178-9	2021	Inhibition of HSP90 with 17-DMAG impaired the upregulation of type I IFNs and ISGs induced by NLRP12.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	25-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
34265086-7	2021	S-nitrosylation site-mutated plasmids or adeno-associated virus, gene deletion and pharmacological antagonists were used to identify the contribution of SNO-HSP90 in myocardial fibrosis.	sno	153-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
34494397-5	2021	Gambogic acid (GA) which surmounts tumor cell thermotolerance by inhibiting heat shock protein 90 (HSP90) expression is coloaded into the nanoparticles, RGD peptide is further introduced to the nanoparticle surface to improve tumor accumulation.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-97
34494397-5	2021	Gambogic acid (GA) which surmounts tumor cell thermotolerance by inhibiting heat shock protein 90 (HSP90) expression is coloaded into the nanoparticles, RGD peptide is further introduced to the nanoparticle surface to improve tumor accumulation.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
34871064-0	2022	Heterogeneous Responses and Isoform Compensation Dim Therapeutic Window of Hsp90 ATP-Binding Inhibitors in Cancer.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
34871064-5	2022	Among randomly selected cancer cell lines, the same client proteins for regulation of cell growth exhibited unexpectedly heterogenous reactions in response to Hsp90 ATP-binding inhibitor, inconsistent with the current understanding.	Adenosine Triphosphate	165-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
34265086-8	2021	KEY RESULTS: SNO-HSP90 level was positively correlated with fibrosis marker expression in hearts from patients and significantly higher in fibrotic hearts from spontaneously hypertensive rats and mice subjected to transverse aortic constriction, as well as in angiotensin II- or isoproterenol-treated neonatal rat cardiac fibroblasts.	sno	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
34265086-8	2021	KEY RESULTS: SNO-HSP90 level was positively correlated with fibrosis marker expression in hearts from patients and significantly higher in fibrotic hearts from spontaneously hypertensive rats and mice subjected to transverse aortic constriction, as well as in angiotensin II- or isoproterenol-treated neonatal rat cardiac fibroblasts.	Isoproterenol	279-292	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
34758612-2	2021	In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) was identified as a potent inhibitor of mitochondrial Hsp90, known as a tumor necrosis factor receptor-associated protein 1 (TRAP1).	mitoquinone	53-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
34633754-3	2021	Moreover, it has been reported that PDHK1, which presents an ATP-binding pocket similar to that of Hsp90, plays an important role in tumor initiation, maintenance and progression, participating also to the senescence process induced by B-Raf oncogenic proteins.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
34758612-2	2021	In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) was identified as a potent inhibitor of mitochondrial Hsp90, known as a tumor necrosis factor receptor-associated protein 1 (TRAP1).	mitoquinone	66-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
34344239-7	2021	Docking studies showed that complexes between quinuclidine-bearing 8-13 and Hsp90 are stabilised by extra hydrophobic interactions between the C(17)-arms and K58 or Y61 of Hsp90.	Quinuclidines	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
34655925-0	2021	Phase 1 multicenter study of the HSP90 inhibitor SNX-5422 plus carboplatin and paclitaxel in patients with lung cancers.	SNX-5422	49-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
34655925-2	2021	SNX-5422 is an oral HSP90 inhibitor with increased activity in vitro with the addition of carboplatin and paclitaxel.	SNX-5422	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
34655925-2	2021	SNX-5422 is an oral HSP90 inhibitor with increased activity in vitro with the addition of carboplatin and paclitaxel.	Carboplatin	90-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
34655925-2	2021	SNX-5422 is an oral HSP90 inhibitor with increased activity in vitro with the addition of carboplatin and paclitaxel.	Paclitaxel	106-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
34344239-7	2021	Docking studies showed that complexes between quinuclidine-bearing 8-13 and Hsp90 are stabilised by extra hydrophobic interactions between the C(17)-arms and K58 or Y61 of Hsp90.	Quinuclidines	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
34834129-0	2021	The Antileukemic Effect of Xestoquinone, A Marine-Derived Polycyclic Quinone-Type Metabolite, Is Mediated through ROS-Induced Inhibition of HSP-90.	xestoquinone	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-146
34944441-9	2021	These findings provide evidence that selective activation of mitochondrial PKCepsilon-ALDH2 axis is important to mitigate aldehyde-mediated pain in rodents, suggesting that PsiepsilonHSP90 and small molecules that mimic it may be a potential treatment for patients with pain.	Aldehydes	122-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-188
34834129-0	2021	The Antileukemic Effect of Xestoquinone, A Marine-Derived Polycyclic Quinone-Type Metabolite, Is Mediated through ROS-Induced Inhibition of HSP-90.	ros	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-146
34834129-9	2021	Molecular docking, Western blotting, and thermal shift assay verified the catalytic inhibitory activity of xestoquinone by high binding affinity to HSP-90 and Topo I/II.	xestoquinone	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-154
34723462-8	2021	Molecular modeling studies suggest that the new conglobatins bind to human Hsp90 and disrupt Hsp90/Cdc37 chaperone/co-chaperone interactions in the same manner as conglobatin.	conglobatin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
34723462-8	2021	Molecular modeling studies suggest that the new conglobatins bind to human Hsp90 and disrupt Hsp90/Cdc37 chaperone/co-chaperone interactions in the same manner as conglobatin.	conglobatin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
34794206-0	2022	TAS-116 (pimitespib), an HSP90 inhibitor, exhibits efficacy in preclinical models of adult T-cell leukemia.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
34794206-0	2022	TAS-116 (pimitespib), an HSP90 inhibitor, exhibits efficacy in preclinical models of adult T-cell leukemia.	TAS-116	9-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
34794206-3	2022	Accordingly, we investigated the anti-ATL effects of a novel oral HSP90 inhibitor TAS-116 (pimitespib) and the mechanisms involved in ex vivo and in vivo preclinical models.	TAS-116	82-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
34772945-6	2021	Additionally, we show that cromolyn and F-cromolyn reduce pro-inflammatory proteins PLP1, PELP1, HSP90, IL-2, GRO-alpha, Eotaxin, and VEGF-Alpha, while promoting secretion of anti-inflammatory IL-4 in HMC3 microglia.	Cromolyn Sodium	27-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
34772945-6	2021	Additionally, we show that cromolyn and F-cromolyn reduce pro-inflammatory proteins PLP1, PELP1, HSP90, IL-2, GRO-alpha, Eotaxin, and VEGF-Alpha, while promoting secretion of anti-inflammatory IL-4 in HMC3 microglia.	f-cromolyn	40-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
34778741-5	2021	Meanwhile, GA could inhibit heat shock protein 90 (HSP90) to reduce the heat resistance of tumor cells, and forcefully consume glutathione (GSH) to weaken the antioxidant capacity of cells.	gambogic acid	11-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
34831356-7	2021	The colocalization ratios for Hsp60/3-nitrotyrosine and Hsp60/acetylate-lisine were significantly increased in the COVID-19 group compared to the control group, similar to the colocalization ratio for Hsp90/acetylate-lisine.	acetylate	62-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
34831356-7	2021	The colocalization ratios for Hsp60/3-nitrotyrosine and Hsp60/acetylate-lisine were significantly increased in the COVID-19 group compared to the control group, similar to the colocalization ratio for Hsp90/acetylate-lisine.	lisine	72-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
34831356-7	2021	The colocalization ratios for Hsp60/3-nitrotyrosine and Hsp60/acetylate-lisine were significantly increased in the COVID-19 group compared to the control group, similar to the colocalization ratio for Hsp90/acetylate-lisine.	acetylate	207-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
34831356-7	2021	The colocalization ratios for Hsp60/3-nitrotyrosine and Hsp60/acetylate-lisine were significantly increased in the COVID-19 group compared to the control group, similar to the colocalization ratio for Hsp90/acetylate-lisine.	lisine	217-223	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
34748646-0	2022	HSP90 inhibitor RGRN-305 for oral treatment of plaque type psoriasis: efficacy, safety and biomarker results in an open-label proof-of-concept study.	rgrn-305	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
34748646-2	2022	OBJECTIVE: This phase 1b proof-of-concept study was undertaken to evaluate the safety and efficacy of a novel HSP90 inhibitor (RGRN-305) in the treatment of plaque psoriasis.	rgrn-305	127-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
34748646-13	2022	CONCLUSION: Treatment with RGRN-305 showed an acceptable safety, especially in the low-dose group, and was associated with clinically meaningful improvement in a subset of patients with plaque psoriasis, indicating that HSP90 may serve as a novel future target in psoriasis treatment.	rgrn-305	27-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
34657428-1	2021	The total synthesis of geldanamycin, a well-known polyketide that exhibited potent anticancer activity by inhibiting Hsp90, was finished in 26 long linear steps with 2.65% overall yield.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
34657428-1	2021	The total synthesis of geldanamycin, a well-known polyketide that exhibited potent anticancer activity by inhibiting Hsp90, was finished in 26 long linear steps with 2.65% overall yield.	Polyketides	50-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
34778741-5	2021	Meanwhile, GA could inhibit heat shock protein 90 (HSP90) to reduce the heat resistance of tumor cells, and forcefully consume glutathione (GSH) to weaken the antioxidant capacity of cells.	gambogic acid	11-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
34228232-7	2021	The binding level of HSP90 and Raf-1 in FK1706 group was the highest.	FK1706	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
34291863-6	2021	DMC decreases HER2 level through inhibiting the interaction of HER2 and Hsp90.	demethoxycurcumin	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
34406420-5	2021	In this study, miltefosine and octenidine were identified as new HSP90 inhibitors.	miltefosine	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
34406420-5	2021	In this study, miltefosine and octenidine were identified as new HSP90 inhibitors.	octenidine	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
34406420-7	2021	Western blotting analysis revealed that miltefosine and octenidine significantly down-regulated the expression levels of HSP90 client proteins including p-AKT, CDK6, and ERK, and did not induce overexpression of heat shock proteins including HSP70 and HSP90 in MCF-7 cells.	miltefosine	40-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
34406420-7	2021	Western blotting analysis revealed that miltefosine and octenidine significantly down-regulated the expression levels of HSP90 client proteins including p-AKT, CDK6, and ERK, and did not induce overexpression of heat shock proteins including HSP70 and HSP90 in MCF-7 cells.	octenidine	56-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
34406420-9	2021	In conclusion, miltefosine and octenidine could disrupt the molecular chaperone function of HSP90, and thus, their strong and broad-spectrum anticancer activity is at least in part attributed to the inhibition activity against HSP90.	miltefosine	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
34406420-9	2021	In conclusion, miltefosine and octenidine could disrupt the molecular chaperone function of HSP90, and thus, their strong and broad-spectrum anticancer activity is at least in part attributed to the inhibition activity against HSP90.	miltefosine	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	227-232
34228232-9	2021	The putative mechanism of action stated that FK1706 could promote the binding of HSP90 and Raf-1, make Raf-1 continue to be activated, thereby affecting key proteins in the Ras/Raf/MAPK/ERK signaling pathway related to the neurotrophic effects of NGF to promote the proliferation and neurite regrowth of nerve cells.	FK1706	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
34406420-9	2021	In conclusion, miltefosine and octenidine could disrupt the molecular chaperone function of HSP90, and thus, their strong and broad-spectrum anticancer activity is at least in part attributed to the inhibition activity against HSP90.	octenidine	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
34406420-9	2021	In conclusion, miltefosine and octenidine could disrupt the molecular chaperone function of HSP90, and thus, their strong and broad-spectrum anticancer activity is at least in part attributed to the inhibition activity against HSP90.	octenidine	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	227-232
34077750-3	2021	We demonstrate that the resorcinol clinical candidates ganetespib and, to a lesser extent, luminespib, display unique off-target kinase pharmacology as compared with other HSP90 inhibitors.	resorcinol	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
34425163-4	2021	On the contrary, down-regulation of HSP90beta by RNAi or geldanamycin inhibits EMCV replication.	geldanamycin	57-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-45
34694437-6	2022	Hsp60, Hsp70, and Hsp90 levels decreased significantly in the BCP-group but increased markedly in the CCP-group.	bcp	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
34694437-6	2022	Hsp60, Hsp70, and Hsp90 levels decreased significantly in the BCP-group but increased markedly in the CCP-group.	ccp	102-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
34694437-11	2022	Our findings show that dNCP provides the most effective myocardial preservation in pediatric open-heart surgery and indicate that an increase in Hsp70 expression may be associated with a cardioprotective effect, while an increase in Hsp60 and Hsp90 levels may be an indicator of myocardial damage during CPB.	1,3-Dinitroimidazolidine	23-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
34746036-0	2021	Proline Isomerization as a Key Determinant for Hsp90-Toxin Interactions.	Proline	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
34746036-2	2021	Here, we hypothesize that cis proline residues play a key role in toxin recognition by Hsp90.	cis proline	26-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
34770993-0	2021	Anti-Cancer Properties of Ginkgolic Acids in Human Nasopharyngeal Carcinoma CNE-2Z Cells via Inhibition of Heat Shock Protein 90.	ginkgolic acid	26-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-128
34770993-6	2021	Together, GAS are new Hsp90 inhibitors by binding to Hsp90 (hydrogen bond and hydrophobic interaction).	Hydrogen	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
34770993-6	2021	Together, GAS are new Hsp90 inhibitors by binding to Hsp90 (hydrogen bond and hydrophobic interaction).	Hydrogen	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
34827586-0	2021	Heat Shock Proteins HSPA1 and HSP90AA1 Are Upregulated in Colorectal Polyps and Can Be Targeted in Cancer Cells by Anti-Inflammatory Oxicams with Arylpiperazine Pharmacophore and Benzoyl Moiety Substitutions at Thiazine Ring.	Thiazines	211-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-38
34827586-9	2021	HSPA1 in cancer cells and, to lesser degree, HSP90AA1 can be reduced by oxicam analogues with thiazine ring substituted via propylene linker by arylpiperazine pharmacophore with fluorine substituents and by benzoyl moiety.	oxicam	72-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-53
34827586-9	2021	HSPA1 in cancer cells and, to lesser degree, HSP90AA1 can be reduced by oxicam analogues with thiazine ring substituted via propylene linker by arylpiperazine pharmacophore with fluorine substituents and by benzoyl moiety.	Thiazines	94-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-53
34827586-9	2021	HSPA1 in cancer cells and, to lesser degree, HSP90AA1 can be reduced by oxicam analogues with thiazine ring substituted via propylene linker by arylpiperazine pharmacophore with fluorine substituents and by benzoyl moiety.	propylene	124-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-53
34827586-9	2021	HSPA1 in cancer cells and, to lesser degree, HSP90AA1 can be reduced by oxicam analogues with thiazine ring substituted via propylene linker by arylpiperazine pharmacophore with fluorine substituents and by benzoyl moiety.	arylpiperazine	144-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-53
34827586-9	2021	HSPA1 in cancer cells and, to lesser degree, HSP90AA1 can be reduced by oxicam analogues with thiazine ring substituted via propylene linker by arylpiperazine pharmacophore with fluorine substituents and by benzoyl moiety.	Fluorine	178-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-53
34827586-9	2021	HSPA1 in cancer cells and, to lesser degree, HSP90AA1 can be reduced by oxicam analogues with thiazine ring substituted via propylene linker by arylpiperazine pharmacophore with fluorine substituents and by benzoyl moiety.	Benzoyl Peroxide	207-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-53
34586789-4	2021	Our results demonstrate that the cellular uptake and the tumor-specific accumulation of ZIPP-Apt:DOX/siHSPs were significantly increased due to the AS1411-nucleolin affinity and further confirmed that the simultaneous depletion of HSP70 and HSP90 sensitized magnetic hyperthermia and chemotherapy-induced cell death both in vitro and in vivo.	zipp-apt	88-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
34586789-4	2021	Our results demonstrate that the cellular uptake and the tumor-specific accumulation of ZIPP-Apt:DOX/siHSPs were significantly increased due to the AS1411-nucleolin affinity and further confirmed that the simultaneous depletion of HSP70 and HSP90 sensitized magnetic hyperthermia and chemotherapy-induced cell death both in vitro and in vivo.	Doxorubicin	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
34586789-4	2021	Our results demonstrate that the cellular uptake and the tumor-specific accumulation of ZIPP-Apt:DOX/siHSPs were significantly increased due to the AS1411-nucleolin affinity and further confirmed that the simultaneous depletion of HSP70 and HSP90 sensitized magnetic hyperthermia and chemotherapy-induced cell death both in vitro and in vivo.	AGRO 100	148-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
34693877-0	2021	Computational investigation of ginkgetin and theaflavin as potential inhibitors of heat shock protein 90 (Hsp90).	ginkgetin	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
34693877-0	2021	Computational investigation of ginkgetin and theaflavin as potential inhibitors of heat shock protein 90 (Hsp90).	ginkgetin	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
34693877-0	2021	Computational investigation of ginkgetin and theaflavin as potential inhibitors of heat shock protein 90 (Hsp90).	theaflavin	45-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
34693877-0	2021	Computational investigation of ginkgetin and theaflavin as potential inhibitors of heat shock protein 90 (Hsp90).	theaflavin	45-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
34693877-4	2021	This process helped in the identification of the top two scoring ligands, ginkgetin and theaflavin with favorable as well as crucial interactions with the Hsp90 ligand-binding pocket.	ginkgetin	74-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
34693877-4	2021	This process helped in the identification of the top two scoring ligands, ginkgetin and theaflavin with favorable as well as crucial interactions with the Hsp90 ligand-binding pocket.	theaflavin	88-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
34693877-5	2021	Molecular dynamics simulations of these two natural molecules exhibited minimal fluctuations in the binding pattern of ginkgetin and theaflavin to Hsp90 which retained crucial contacts throughout the simulation time.	ginkgetin	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
34693877-5	2021	Molecular dynamics simulations of these two natural molecules exhibited minimal fluctuations in the binding pattern of ginkgetin and theaflavin to Hsp90 which retained crucial contacts throughout the simulation time.	theaflavin	133-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
34693877-6	2021	We anticipate that ginkgetin and theaflavin could act as potent Hsp90 inhibitors which are under current investigation in our laboratory.Communicated by Ramaswamy H. Sarma.	ginkgetin	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
34693877-6	2021	We anticipate that ginkgetin and theaflavin could act as potent Hsp90 inhibitors which are under current investigation in our laboratory.Communicated by Ramaswamy H. Sarma.	theaflavin	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
34376581-8	2021	Inhibition of Hsp90 N-terminal by STA9090 decreased the location of Hsp90alpha in nucleus, Hsp90alpha-SP1 interaction, SP1 level and the binding of Hsp90alpha/SP1 at the proximal promoter region of PRKDC.	STA 9090	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
34645797-7	2021	The TSSK4 kinase activity is found to be closely related to the function of HSP90-AKT pathway that TSSK4 can phosphorylate its substrate HSP90beta on serine 255, to inhibit the ATPase activity of HSP90beta and reduce its molecular chaperone function on AKT.	Serine	150-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
34645797-7	2021	The TSSK4 kinase activity is found to be closely related to the function of HSP90-AKT pathway that TSSK4 can phosphorylate its substrate HSP90beta on serine 255, to inhibit the ATPase activity of HSP90beta and reduce its molecular chaperone function on AKT.	Serine	150-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-146
34645797-7	2021	The TSSK4 kinase activity is found to be closely related to the function of HSP90-AKT pathway that TSSK4 can phosphorylate its substrate HSP90beta on serine 255, to inhibit the ATPase activity of HSP90beta and reduce its molecular chaperone function on AKT.	Serine	150-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-205
34392176-2	2021	In this framework, we have developed in recent years a family of benzofuran compounds that act as Hsp90 allosteric modulators.	benzofuran	65-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
34392176-5	2021	Western blotting, DARTS (i.e., Drug Affinity Responsive Target Stability) and enzymatic assays data confirmed a dose-dependent interaction of MDH2 with several members of the benzofuran Hsp90 modulators family and a computational model allowed to interpret the observed interactions.	benzofuran	175-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
34376581-10	2021	Consistently, inhibition of Hsp90 increased the number of heat shock-induced gamma-H2AX foci and delayed the repair of DSBs.	dsbs	119-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
34746702-4	2021	In addition, the optical trapping force of the plasmonic nanopores allows 20-nm polystyrene beads and proteins, such as beta-amylase and Heat Shock Protein (HSP90), to be trapped for very long times (approximately minutes).	Polystyrenes	80-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
34314918-0	2021	Selective targeting of cancer cells using a hydrogen peroxide-activated Hsp90 inhibitor.	Hydrogen Peroxide	44-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
34314918-3	2021	To avoid undesirable toxicity, we herein report a hydrogen peroxide-activated Hsp90 inhibitor, Boro-BZide (3), which is capable of selectively targeting cancer cells over normal cells.	Hydrogen Peroxide	50-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
34314918-3	2021	To avoid undesirable toxicity, we herein report a hydrogen peroxide-activated Hsp90 inhibitor, Boro-BZide (3), which is capable of selectively targeting cancer cells over normal cells.	boro-bzide	95-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
34314918-4	2021	Boro-BZide (3) can be activated by high levels of hydrogen peroxide, releasing its parent active Hsp90 inhibitor.	boro-bzide	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
34314918-4	2021	Boro-BZide (3) can be activated by high levels of hydrogen peroxide, releasing its parent active Hsp90 inhibitor.	Hydrogen Peroxide	50-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
34314918-6	2021	These efforts ultimately led to the identification of a novel hydrogen peroxide-activated Hsp90 prodrug with improved therapeutic index, which was less prone to furnish unwanted adverse effects.	Hydrogen Peroxide	62-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
34314918-7	2021	This hydrogen peroxide-responsive prodrug strategy will be beneficial for overcoming the toxicity hurdles of Hsp90 inhibitors for clinical application.	Hydrogen Peroxide	5-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
34186047-12	2021	SIGNIFICANCE: We implied that XL888 promoted apoptosis of HCC cells induced by heat via disrupting the binding of HSP90 and STAT3, providing theoretical basis for a novel combination strategy for HCC.	XL 888	30-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
34376581-11	2021	Altogether, our results suggest that Hsp90 inhibitor STA9090 decreases DNA-PKcs protein stability and PRKDC mRNA level, which provide a theoretical basis for the promising combination therapy of hyperthermia and Hsp90 inhibitor in HCC.	STA 9090	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
34376581-11	2021	Altogether, our results suggest that Hsp90 inhibitor STA9090 decreases DNA-PKcs protein stability and PRKDC mRNA level, which provide a theoretical basis for the promising combination therapy of hyperthermia and Hsp90 inhibitor in HCC.	STA 9090	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
34376581-8	2021	Inhibition of Hsp90 N-terminal by STA9090 decreased the location of Hsp90alpha in nucleus, Hsp90alpha-SP1 interaction, SP1 level and the binding of Hsp90alpha/SP1 at the proximal promoter region of PRKDC.	STA 9090	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-78
34376581-8	2021	Inhibition of Hsp90 N-terminal by STA9090 decreased the location of Hsp90alpha in nucleus, Hsp90alpha-SP1 interaction, SP1 level and the binding of Hsp90alpha/SP1 at the proximal promoter region of PRKDC.	STA 9090	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-101
34376581-8	2021	Inhibition of Hsp90 N-terminal by STA9090 decreased the location of Hsp90alpha in nucleus, Hsp90alpha-SP1 interaction, SP1 level and the binding of Hsp90alpha/SP1 at the proximal promoter region of PRKDC.	STA 9090	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-158
34585447-0	2021	Zeylenone synergizes with cisplatin in osteosarcoma by enhancing DNA damage, apoptosis, and necrosis via the Hsp90/AKT/GSK3beta and Fanconi anaemia pathway.	zeylenone	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
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
34585447-0	2021	Zeylenone synergizes with cisplatin in osteosarcoma by enhancing DNA damage, apoptosis, and necrosis via the Hsp90/AKT/GSK3beta and Fanconi anaemia pathway.	Cisplatin	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
34607394-2	2021	Although many HSP90 inhibitors have been tested in the treatment of KRAS-mutant non-small cell lung cancer (NSCLC), most, including AUY922, have failed due to toxic effects and resistance generation, even though a modest efficacy has been observed for these drugs in clinical trials.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	132-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
34585447-7	2021	Thus, the Hsp90/AKT/GSK3beta and FA pathway are the key to the synergism between zey and cisplatin.	zeylenone	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
34585447-7	2021	Thus, the Hsp90/AKT/GSK3beta and FA pathway are the key to the synergism between zey and cisplatin.	Cisplatin	89-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
34685574-3	2021	Heat shock protein 70 kDa (Hsp70) and 90 kDa (Hsp90) are two of the most important chaperones whose functions are dependent on ATP hydrolysis and collaboration with their co-chaperones.	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
34685577-0	2021	Co-Expression of CD34, CD90, OV-6 and Cell-Surface Vimentin Defines Cancer Stem Cells of Hepatoblastoma, Which Are Affected by Hsp90 Inhibitor 17-AAG.	tanespimycin	143-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
34685577-6	2021	When we treated the cells with the Hsp90 inhibitor 17-AAG, we observed a significant reduction in the CSC subset.	tanespimycin	51-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
34297462-6	2021	Owing to the knockout of Hsp90alpha for reducing thermal-resistance of cancer cells, highly effective tumor ablation both in vitro and in vivo was achieved with APACPs under mild PTT.	apacps	161-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-35
34495872-5	2021	Using H2O2-induced senescent ARPE-19 cells and replicative senescent primary RPE cells from rhesus monkey, we found that HSP90 upregulates the expression of IKKalpha, and HIF1alpha in senescent ARPE-19 cells and subsequently controls the induction of distinct senescence-associated inflammatory factors.	Hydrogen Peroxide	6-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
34495872-6	2021	Senescent ARPE-19 cells are more resistant to the cytotoxic HSP90 inhibitor IPI504 (IC50 = 36.78 muM) when compared to normal ARPE-19 cells (IC50 = 6.16 muM).	tanespimycin	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
34495872-8	2021	In addition, we found that inhibition of HSP90 by IPI504 reduces SA-beta-Gal"s protein expression and enzyme activity in a dose-dependent manner.	tanespimycin	50-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
34495872-8	2021	In addition, we found that inhibition of HSP90 by IPI504 reduces SA-beta-Gal"s protein expression and enzyme activity in a dose-dependent manner.	2-(2-quinolinyl)-1H-indene--1,3(2H)-dione-6'-sulfonic acid	65-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
34495872-9	2021	HSP90 interacts with and regulates SA-beta-Gal protein stabilization in senescent ARPE-19 cells.	2-chloro-10-(4'(N-beta-hydroxyethyl)piperazinyl-1')acetylphenothiazine	35-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
34495872-11	2021	HSP90 inhibitors (e.g. IPI504) could be a promising senomorphic drug candidate for AMD intervention.	tanespimycin	23-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
34496826-4	2021	A previous study reported that leflunomide (LEF) with a corticosteroid was effective for adult patients with HSPN and nephrotic proteinuria.	Leflunomide	31-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-113
34496826-4	2021	A previous study reported that leflunomide (LEF) with a corticosteroid was effective for adult patients with HSPN and nephrotic proteinuria.	Leflunomide	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-113
34147560-8	2021	Treatment of cells with specific Hsp90 inhibitors, geldanamycin and 17-AAG, abolished the association of Hsp90 and Cdc37 with DYRK1B and DYRK4, but not of Hsp70.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
34380015-1	2021	The Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators.	Adenosine Triphosphate	106-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
34380015-4	2021	A helix extension in the TPR functions as a key recognition element, interacting across the Hsp90 C-terminal dimer interface presented in the closed, ATP conformation.	Adenosine Triphosphate	150-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
34401540-14	2021	However, Zn supplementation increased (P < 0.05) copper zinc superoxide dismutase (CuZnSOD) activity and metallothionein mRNA expression, and effectively decreased (P < 0.05) the expressions of HSP70 mRNA and protein, as well as HSP90 mRNA.	Zinc	9-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	229-234
34147560-8	2021	Treatment of cells with specific Hsp90 inhibitors, geldanamycin and 17-AAG, abolished the association of Hsp90 and Cdc37 with DYRK1B and DYRK4, but not of Hsp70.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
34147560-8	2021	Treatment of cells with specific Hsp90 inhibitors, geldanamycin and 17-AAG, abolished the association of Hsp90 and Cdc37 with DYRK1B and DYRK4, but not of Hsp70.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
34147560-8	2021	Treatment of cells with specific Hsp90 inhibitors, geldanamycin and 17-AAG, abolished the association of Hsp90 and Cdc37 with DYRK1B and DYRK4, but not of Hsp70.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
34147560-10	2021	DYRK1B and DYRK4 underwent rapid formation of cytoplasmic punctate dots after the geldanamycin treatment, suggesting that the chaperone function of Hsp90 is required for prevention of protein aggregation of the target kinases.	geldanamycin	82-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
34147560-11	2021	Prolonged inhibition of Hsp90 by geldanamycin, 17-AAG, or ganetespib, decreased cellular levels of DYRK1B and DYRK4.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
34147560-11	2021	Prolonged inhibition of Hsp90 by geldanamycin, 17-AAG, or ganetespib, decreased cellular levels of DYRK1B and DYRK4.	tanespimycin	47-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
34147560-11	2021	Prolonged inhibition of Hsp90 by geldanamycin, 17-AAG, or ganetespib, decreased cellular levels of DYRK1B and DYRK4.	STA 9090	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
34147560-12	2021	Finally, DYRK1B and DYRK4 were ubiquitinated in cells, and ubiquitinated DYRK1B and DYRK4 further increased by Hsp90 inhibition with geldanamycin.	geldanamycin	133-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
34331200-0	2021	Gambogic acid and gambogenic acid induce a thiol-dependent heat shock response and disrupt the interaction between HSP90 and HSF1 or HSF2.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
34343460-0	2021	Retraction: Hsp90beta is involved in the development of high salt-diet-induced nephropathy via interaction with various signalling proteins.	Salts	61-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-21
34331200-0	2021	Gambogic acid and gambogenic acid induce a thiol-dependent heat shock response and disrupt the interaction between HSP90 and HSF1 or HSF2.	neo-gambogic acid	18-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
34331200-0	2021	Gambogic acid and gambogenic acid induce a thiol-dependent heat shock response and disrupt the interaction between HSP90 and HSF1 or HSF2.	Sulfhydryl Compounds	43-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
34331200-3	2021	The bioactive natural compound gambogic acid (GB) is a prenylated xanthone with antitumor activity, and it has been proposed to function as an HSP90 inhibitor.	gambogic acid	31-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
34331200-3	2021	The bioactive natural compound gambogic acid (GB) is a prenylated xanthone with antitumor activity, and it has been proposed to function as an HSP90 inhibitor.	gambogic acid	46-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
34331200-7	2021	Intriguingly, using closed form ATP-bound HSP90 mutants that can be co-precipitated with HSF1, a known facilitator of cancer, we show that also endogenous HSF2 co-precipitates with HSP90.	Adenosine Triphosphate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
34331200-7	2021	Intriguingly, using closed form ATP-bound HSP90 mutants that can be co-precipitated with HSF1, a known facilitator of cancer, we show that also endogenous HSF2 co-precipitates with HSP90.	Adenosine Triphosphate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
34331200-8	2021	GB and GBA treatment disrupt the interaction between HSP90 and HSF1 and HSP90 and HSF2.	gambogic acid	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
34331200-8	2021	GB and GBA treatment disrupt the interaction between HSP90 and HSF1 and HSP90 and HSF2.	gambogic acid	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
34331200-9	2021	Our study implies that these compounds should be used cautiously if developed for cancer therapies, since GB and its derivative GBA are strong inducers of the HSR, in multiple cell types, by involving the dissociation of a HSP90-HSF1/HSF2 complex.	gambogic acid	106-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
34497513-3	2021	Thus, treatment with 1G6-D7 (a selective HSP90alpha monoclonal antibody) to antagonize eHSP90alpha could effectively ameliorate fibrosis.	1g6-d7	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-51
34659125-5	2021	We aimed to evaluate the Hsp90alpha as a biomarker in predicting metabolic-associated fatty liver disease (MAFLD) and define the therapeutic effects of geranylgeranylacetone for the disease.	geranylgeranylacetone	152-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-35
34403222-9	2021	The Hsp90 inhibitor, 17-AAG, rather than HDN-1, disrupted the interaction between Hsp90 and PGK1, and reduced GSK3beta expression, resulting in significantly reduced inhibition of beta-catenin expression, to maintain the stemness of breast cancer stem cells.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
34403222-9	2021	The Hsp90 inhibitor, 17-AAG, rather than HDN-1, disrupted the interaction between Hsp90 and PGK1, and reduced GSK3beta expression, resulting in significantly reduced inhibition of beta-catenin expression, to maintain the stemness of breast cancer stem cells.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
34452244-0	2021	Structure-Activity Relationships of Benzothiazole-Based Hsp90 C-Terminal-Domain Inhibitors.	benzothiazole	36-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
34452244-4	2021	Several structural features have been shown to be useful in the design of Hsp90 CTD inhibitors, including an aromatic ring, a cationic center and the benzothiazole moiety.	benzothiazole	150-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
34452244-6	2021	Using ligand-based design methodologies and structure-based pharmacophore models, a library of 29 benzothiazole-based Hsp90 CTD inhibitors was prepared, and their antiproliferative activities were evaluated in MCF-7 breast cancer cells.	benzothiazole	98-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
34149899-6	2021	Compared with the PBS control group, the A549, A549/DDP and A549/Taxol cells treated with NaI131, GA or a combination of the drugs exhibited G2/M arrest and increased percentages of total apoptotic cells, as well as significantly decreased protein levels of CDK1, cyclin B, mtp53, HSP90, Bcl-2 and P-gp, increased protein levels of Bax and decreased mRNA levels of p53 and HSP90.	pbs	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	373-378
34149899-6	2021	Compared with the PBS control group, the A549, A549/DDP and A549/Taxol cells treated with NaI131, GA or a combination of the drugs exhibited G2/M arrest and increased percentages of total apoptotic cells, as well as significantly decreased protein levels of CDK1, cyclin B, mtp53, HSP90, Bcl-2 and P-gp, increased protein levels of Bax and decreased mRNA levels of p53 and HSP90.	nai131	90-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	281-286
34149899-6	2021	Compared with the PBS control group, the A549, A549/DDP and A549/Taxol cells treated with NaI131, GA or a combination of the drugs exhibited G2/M arrest and increased percentages of total apoptotic cells, as well as significantly decreased protein levels of CDK1, cyclin B, mtp53, HSP90, Bcl-2 and P-gp, increased protein levels of Bax and decreased mRNA levels of p53 and HSP90.	nai131	90-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	373-378
34149899-6	2021	Compared with the PBS control group, the A549, A549/DDP and A549/Taxol cells treated with NaI131, GA or a combination of the drugs exhibited G2/M arrest and increased percentages of total apoptotic cells, as well as significantly decreased protein levels of CDK1, cyclin B, mtp53, HSP90, Bcl-2 and P-gp, increased protein levels of Bax and decreased mRNA levels of p53 and HSP90.	gambogic acid	98-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	281-286
34149899-6	2021	Compared with the PBS control group, the A549, A549/DDP and A549/Taxol cells treated with NaI131, GA or a combination of the drugs exhibited G2/M arrest and increased percentages of total apoptotic cells, as well as significantly decreased protein levels of CDK1, cyclin B, mtp53, HSP90, Bcl-2 and P-gp, increased protein levels of Bax and decreased mRNA levels of p53 and HSP90.	gambogic acid	98-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	373-378
34170694-2	2021	Celastrol, a natural friedelane triterpenoid, can disrupt the Hsp90-Cdc37 interaction to provide antitumor effects.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
34269521-6	2021	Hsp90alpha, one subunit of heat shock protein 90 (Hsp90), is targeted by Cas9 RNP to reduce tumor heat tolerance for enhanced mild-PTT effects ( 43  C).	Bialaphos	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
34269521-6	2021	Hsp90alpha, one subunit of heat shock protein 90 (Hsp90), is targeted by Cas9 RNP to reduce tumor heat tolerance for enhanced mild-PTT effects ( 43  C).	Bialaphos	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-48
34269521-6	2021	Hsp90alpha, one subunit of heat shock protein 90 (Hsp90), is targeted by Cas9 RNP to reduce tumor heat tolerance for enhanced mild-PTT effects ( 43  C).	Bialaphos	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
34170694-3	2021	In this study, 31 new celastrol derivatives, 2a-2d, 3a-3g, and 4a-4t, were designed and synthesized, and their Hsp90-Cdc37 disruption activities and antiproliferative activities against cancer cells were evaluated.	celastrol	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
34301262-1	2021	BACKGROUND: Ocular adverse events are common dose-limiting toxicities in cancer patients treated with HSP90 inhibitors, such as AUY922; however, the pathology and molecular mechanisms that mediate AUY922-induced retinal toxicity remain undescribed.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	128-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
34301262-1	2021	BACKGROUND: Ocular adverse events are common dose-limiting toxicities in cancer patients treated with HSP90 inhibitors, such as AUY922; however, the pathology and molecular mechanisms that mediate AUY922-induced retinal toxicity remain undescribed.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	197-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
34820556-3	2022	Herein, we propose a multi-hit strategy that is based on the biodegradable hollow mesoporous Prussian blue (HMPB)-based nanosystem for tumor-specific therapy that encapsulated the critical heat shock protein 90 (HSP90) inhibitor 17-dimethylamino-ethylamino-17-demethoxydeldanamycin (17-DMAG).	mesoporous prussian blue	82-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-210
34820556-3	2022	Herein, we propose a multi-hit strategy that is based on the biodegradable hollow mesoporous Prussian blue (HMPB)-based nanosystem for tumor-specific therapy that encapsulated the critical heat shock protein 90 (HSP90) inhibitor 17-dimethylamino-ethylamino-17-demethoxydeldanamycin (17-DMAG).	mesoporous prussian blue	82-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
34820556-3	2022	Herein, we propose a multi-hit strategy that is based on the biodegradable hollow mesoporous Prussian blue (HMPB)-based nanosystem for tumor-specific therapy that encapsulated the critical heat shock protein 90 (HSP90) inhibitor 17-dimethylamino-ethylamino-17-demethoxydeldanamycin (17-DMAG).	17-dimethylamino-ethylamino-17-demethoxydeldanamycin	229-281	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-210
34820556-3	2022	Herein, we propose a multi-hit strategy that is based on the biodegradable hollow mesoporous Prussian blue (HMPB)-based nanosystem for tumor-specific therapy that encapsulated the critical heat shock protein 90 (HSP90) inhibitor 17-dimethylamino-ethylamino-17-demethoxydeldanamycin (17-DMAG).	17-dimethylamino-ethylamino-17-demethoxydeldanamycin	229-281	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
34820556-3	2022	Herein, we propose a multi-hit strategy that is based on the biodegradable hollow mesoporous Prussian blue (HMPB)-based nanosystem for tumor-specific therapy that encapsulated the critical heat shock protein 90 (HSP90) inhibitor 17-dimethylamino-ethylamino-17-demethoxydeldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	283-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-210
34820556-3	2022	Herein, we propose a multi-hit strategy that is based on the biodegradable hollow mesoporous Prussian blue (HMPB)-based nanosystem for tumor-specific therapy that encapsulated the critical heat shock protein 90 (HSP90) inhibitor 17-dimethylamino-ethylamino-17-demethoxydeldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	283-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
34820556-5	2022	Upon cell internalization of 17-DMAG-HMPB@sPP@HA and under 808 nm laser irradiation, photothermal-conversion effect of HMPB directly kills cells using hyperthermia, which further causes phase transition of sPP to trigger release of 17-DMAG, inhibits HSP90 activity and blocks multiple signaling pathways, including cell cycle, Akt and HIF pathways.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	29-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	250-255
34820556-7	2022	Importantly, the antitumor effect of 17-DMAG and ferroptosis damage were amplified using photothermal effect of HMPB by accelerating release of ferric and ferrous ions, and reducing HSP90 expression in cells, which induced powerful antitumor effect in vitro and in vivo.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
34286666-11	2021	HighlightsHsp90 inhibitors that entered different phases of clinical trials were subjected to Zinc15 based structure query to afford potential enzyme inhibitors 19 and 20.Quantum chemical calculations confirmed docking results and verified pivotal role of a conserved residues (Asn51, Leu103, Phe138 and Tyr139) in making effective hydrogen bonds.MD simulations of top-ranked docked derivatives revealed the achievement of stable binding modes with less conformational variation of 20 than 19 in the active site of Hsp90-alpha NTD.H-bond, hydrophobic contacts and salt bridge interactions were determinant forces in binding interactions of in silico hits.Resorcinol and isoxazole were important structural motifs of in silico hits in binding to the active site of Hsp90-alpha NTD.Communicated by Ramaswamy H. Sarma.	ZINC15	94-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	515-526
34286666-11	2021	HighlightsHsp90 inhibitors that entered different phases of clinical trials were subjected to Zinc15 based structure query to afford potential enzyme inhibitors 19 and 20.Quantum chemical calculations confirmed docking results and verified pivotal role of a conserved residues (Asn51, Leu103, Phe138 and Tyr139) in making effective hydrogen bonds.MD simulations of top-ranked docked derivatives revealed the achievement of stable binding modes with less conformational variation of 20 than 19 in the active site of Hsp90-alpha NTD.H-bond, hydrophobic contacts and salt bridge interactions were determinant forces in binding interactions of in silico hits.Resorcinol and isoxazole were important structural motifs of in silico hits in binding to the active site of Hsp90-alpha NTD.Communicated by Ramaswamy H. Sarma.	Hydrogen	332-340	heat shock protein 90 alpha family class A member 1	Homo sapiens	515-526
34286666-11	2021	HighlightsHsp90 inhibitors that entered different phases of clinical trials were subjected to Zinc15 based structure query to afford potential enzyme inhibitors 19 and 20.Quantum chemical calculations confirmed docking results and verified pivotal role of a conserved residues (Asn51, Leu103, Phe138 and Tyr139) in making effective hydrogen bonds.MD simulations of top-ranked docked derivatives revealed the achievement of stable binding modes with less conformational variation of 20 than 19 in the active site of Hsp90-alpha NTD.H-bond, hydrophobic contacts and salt bridge interactions were determinant forces in binding interactions of in silico hits.Resorcinol and isoxazole were important structural motifs of in silico hits in binding to the active site of Hsp90-alpha NTD.Communicated by Ramaswamy H. Sarma.	resorcinol	655-665	heat shock protein 90 alpha family class A member 1	Homo sapiens	515-526
34286666-11	2021	HighlightsHsp90 inhibitors that entered different phases of clinical trials were subjected to Zinc15 based structure query to afford potential enzyme inhibitors 19 and 20.Quantum chemical calculations confirmed docking results and verified pivotal role of a conserved residues (Asn51, Leu103, Phe138 and Tyr139) in making effective hydrogen bonds.MD simulations of top-ranked docked derivatives revealed the achievement of stable binding modes with less conformational variation of 20 than 19 in the active site of Hsp90-alpha NTD.H-bond, hydrophobic contacts and salt bridge interactions were determinant forces in binding interactions of in silico hits.Resorcinol and isoxazole were important structural motifs of in silico hits in binding to the active site of Hsp90-alpha NTD.Communicated by Ramaswamy H. Sarma.	Isoxazoles	670-679	heat shock protein 90 alpha family class A member 1	Homo sapiens	515-526
34298835-6	2021	Unexpectedly, mutp53 protein, which is stabilized by interaction with the chaperone HSP90 and mediates cell oncogenic addiction, becomes destabilized after D-Prop treatment.	d-prop	156-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
34298835-7	2021	HSP90 phosphorylation by PKA and its interaction with mutp53 are decreased by D-Prop, releasing mutp53 towards proteasomal degradation.	d-prop	78-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
34359868-7	2021	Mutating the two serines to alanines increased the amount of proteins interacting with Hsp90beta globally and increased the sensitivity to tryptic cleavage in the C-terminal domain.	Serine	17-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-96
34359663-3	2021	The inhibition of LDH activity by oxamate or GNE-140, glucose deprivation and LDHA/B double knockout (LDH-/-) in B16F10 and LS174T cells significantly diminish tumor growth; ROS production and the cytosolic expression of different HSPs, including Hsp90, Hsp70 and Hsp27 concomitant with a reduction of heat shock factor 1 (HSF1)/pHSF1.	Oxamic Acid	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	247-252
34359663-3	2021	The inhibition of LDH activity by oxamate or GNE-140, glucose deprivation and LDHA/B double knockout (LDH-/-) in B16F10 and LS174T cells significantly diminish tumor growth; ROS production and the cytosolic expression of different HSPs, including Hsp90, Hsp70 and Hsp27 concomitant with a reduction of heat shock factor 1 (HSF1)/pHSF1.	GNE-140	45-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	247-252
34359868-7	2021	Mutating the two serines to alanines increased the amount of proteins interacting with Hsp90beta globally and increased the sensitivity to tryptic cleavage in the C-terminal domain.	Alanine	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-96
34290605-0	2021	Synergistic Activity of the HSP90 Inhibitor Ganetespib With Lapatinib Reverses Acquired Lapatinib Resistance in HER2-Positive Breast Cancer Cells.	STA 9090	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
34290605-0	2021	Synergistic Activity of the HSP90 Inhibitor Ganetespib With Lapatinib Reverses Acquired Lapatinib Resistance in HER2-Positive Breast Cancer Cells.	Lapatinib	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
34290605-0	2021	Synergistic Activity of the HSP90 Inhibitor Ganetespib With Lapatinib Reverses Acquired Lapatinib Resistance in HER2-Positive Breast Cancer Cells.	Lapatinib	88-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
34290605-3	2021	In the present study, we established breast cancers cells with acquired lapatinib resistance and investigated the antitumor activity of the second-generation HSP90 inhibitor ganetespib in association with lapatinib in lapatinib-sensitive and -resistant cells.	STA 9090	174-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
34262899-8	2021	The inhibition of Hsp90 ATPase activity by either geldanamycin or radicicol decreases the protein stability of filamin A.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
34252884-4	2021	The antiviral chaperone ATPase inhibitor AR12 reduced the ATPase activities and total expression of GRP78, HSP90, and HSP70, and of Tau, Tau 301L, APP, APP692, APP715, SOD1 G93A and TDP-43.	ar12	41-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
34210023-5	2021	HSP70 shows the damage of the membrane, while HSP90 increases the insulation properties of tBLM.	tblm	91-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
34262899-8	2021	The inhibition of Hsp90 ATPase activity by either geldanamycin or radicicol decreases the protein stability of filamin A.	monorden	66-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
34199261-0	2021	The HSP90 Inhibitor, AUY-922, Protects and Repairs Human Lung Microvascular Endothelial Cells from Hydrochloric Acid-Induced Endothelial Barrier Dysfunction.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
34267888-3	2021	A series of purine-8-one and pyrrolo(2,3-d)pyrimidine derivatives was developed based on TRAP1 structure and identified to be highly selective in vitro for TRAP1 over the paralogous enzymes, Hsp90alpha and Grp94.	purine-8-one	12-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-201
34267888-3	2021	A series of purine-8-one and pyrrolo(2,3-d)pyrimidine derivatives was developed based on TRAP1 structure and identified to be highly selective in vitro for TRAP1 over the paralogous enzymes, Hsp90alpha and Grp94.	Pyrrolo(2,3-d)pyrimidine	29-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-201
34199261-0	2021	The HSP90 Inhibitor, AUY-922, Protects and Repairs Human Lung Microvascular Endothelial Cells from Hydrochloric Acid-Induced Endothelial Barrier Dysfunction.	Hydrochloric Acid	99-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
34199261-4	2021	Pre-treatment or post-treatment of HLMVEC with AUY-922, a third-generation HSP90 inhibitor, prevented and restored HCl-induced endothelial barrier dysfunction.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	47-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
34199261-7	2021	We conclude that, by increasing the expression of cytoprotective proteins, interfering with actomyosin contractility, and enhancing the expression of junction proteins, inhibition of HSP90 may represent a useful approach for the management of HCl-induced endothelial dysfunction and acute lung injury.	Hydrochloric Acid	243-246	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
34117308-2	2021	As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
34178628-8	2021	Highly stabilized mutp53 is degradable by the Hsp90 inhibitors Onalespib and Ganetespib, and correlates with growth suppression, possibly suggesting therapeutic vulnerabilities to target GOF mutp53 proteins in PDAC.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	63-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
34178628-8	2021	Highly stabilized mutp53 is degradable by the Hsp90 inhibitors Onalespib and Ganetespib, and correlates with growth suppression, possibly suggesting therapeutic vulnerabilities to target GOF mutp53 proteins in PDAC.	STA 9090	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
34117308-2	2021	As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
34069389-2	2021	The leishmanicidal effect of an Hsp90 inhibitor, 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), was previously demonstrated in both in vitro and in vivo models of cutaneous leishmaniasis.	tanespimycin	49-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
34112202-8	2021	Moreover, Western blot and flow cytometry assays showed that CRT and HSP90 (biomarkers of early ICD) significantly accumulated on the cell membrane surface after approximately 6 h of treatment with bullatacin.	bullatacin	198-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
34200311-0	2021	Inhibition of Hsp90 Counteracts the Established Experimental Dermal Fibrosis Induced by Bleomycin.	Bleomycin	88-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
34200311-3	2021	In the next step of the preclinical analysis, herein, we aimed to evaluate the efficacy of an Hsp90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), in the treatment of established experimental dermal fibrosis induced by bleomycin.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	111-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
34200311-3	2021	In the next step of the preclinical analysis, herein, we aimed to evaluate the efficacy of an Hsp90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), in the treatment of established experimental dermal fibrosis induced by bleomycin.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	164-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
34200311-3	2021	In the next step of the preclinical analysis, herein, we aimed to evaluate the efficacy of an Hsp90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), in the treatment of established experimental dermal fibrosis induced by bleomycin.	Bleomycin	246-255	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
34199986-0	2021	Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity.	elaiophylin	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
34199986-4	2021	Here, we elaborated that elaiophylin likewise disrupts the Hsp90/ Cdc37 interaction, without affecting the ATP-pocket of Hsp90.	elaiophylin	25-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
34199986-5	2021	Similarly to conglobatin A, elaiophylin decreased expression levels of the Hsp90 client HIF1alpha, a transcription factor with various downstream targets, including galectin-3.	elaiophylin	28-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
34199986-7	2021	In agreement with this K-Ras targeting and the potent effect on other Hsp90 clients, we observed with elaiophylin treatment a submicromolar IC50 for MDA-MB-231 and MIA-PaCa-2 3D spheroid formation.	elaiophylin	102-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
34199986-9	2021	These results suggest that several other macrodiolides may have the Hsp90/ Cdc37 interface as a target site.	macrodiolides	41-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
34079010-5	2021	Ipom-F treatment results in two cellular stress responses: firstly, an upregulation of stress-inducible cytosolic chaperones, Hsp70 and Hsp90; secondly, an atypical unfolded protein response (UPR) linked to the Ipom-F-mediated perturbation of ER function.	ipomoeassin F	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
34221862-3	2021	The first discovered Hsp90 inhibitors, geldanamycin and radicicol, function by competitively binding to Hsp90"s N-terminal binding site and inhibiting its ATPase activity.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
34221862-3	2021	The first discovered Hsp90 inhibitors, geldanamycin and radicicol, function by competitively binding to Hsp90"s N-terminal binding site and inhibiting its ATPase activity.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
34221862-3	2021	The first discovered Hsp90 inhibitors, geldanamycin and radicicol, function by competitively binding to Hsp90"s N-terminal binding site and inhibiting its ATPase activity.	monorden	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
34221862-3	2021	The first discovered Hsp90 inhibitors, geldanamycin and radicicol, function by competitively binding to Hsp90"s N-terminal binding site and inhibiting its ATPase activity.	monorden	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
33904516-0	2021	A novel C-terminal Hsp90 inhibitor KU758 synergizes efficacy in combination with BRAF or MEK inhibitors and targets drug-resistant pathways in BRAF-mutant melanomas.	ku758	35-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
33904516-6	2021	Taken together, we hypothesize that our novel C-terminal Hsp90 inhibitor, KU758, in combination with the current standard of care targeted therapies (e.g. vemurafenib and cobimetinib) can both synergize melanoma treatment efficacy in BRAF-mutant tumors, as well as target and overcome several major resistance pathways in this disease.	ku758	74-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
34069389-8	2021	In addition, Hsp90 inhibition resulted in greater accumulation of ubiquitylated proteins in both WT- and Deltaatg5-treated parasites compared to controls, in the absence of proteasome overload.	deltaatg5	105-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
34062977-0	2021	TAS-116, a Well-Tolerated Hsp90 Inhibitor, Prevents the Activation of the NLRP3 Inflammasome in Human Retinal Pigment Epithelial Cells.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
34326484-0	2022	Okicamelliaside targets the N-terminal chaperone pocket of HSP90 disrupts the chaperone protein interaction of HSP90-CDC37 and exerts antitumor activity.	okicamelliaside	0-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
34326484-0	2022	Okicamelliaside targets the N-terminal chaperone pocket of HSP90 disrupts the chaperone protein interaction of HSP90-CDC37 and exerts antitumor activity.	okicamelliaside	0-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
34326484-2	2022	However, various toxic reactions targeting the ATP binding site of HSP90 may not be the best choice for HSP90 inhibitors.	Adenosine Triphosphate	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
34326484-6	2022	Mutation analysis of the target protein and molecular dynamics simulation revealed that OCS could competitively act on the key Glu-47 site at the N-terminal chaperone pocket of HSP90, where the co-chaperone CDC37 binds to HSP90, affect its stability and reduce the  Gbind of HSP90-CDC37.	Glutamic Acid	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
34326484-6	2022	Mutation analysis of the target protein and molecular dynamics simulation revealed that OCS could competitively act on the key Glu-47 site at the N-terminal chaperone pocket of HSP90, where the co-chaperone CDC37 binds to HSP90, affect its stability and reduce the  Gbind of HSP90-CDC37.	Glutamic Acid	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	222-227
34326484-6	2022	Mutation analysis of the target protein and molecular dynamics simulation revealed that OCS could competitively act on the key Glu-47 site at the N-terminal chaperone pocket of HSP90, where the co-chaperone CDC37 binds to HSP90, affect its stability and reduce the  Gbind of HSP90-CDC37.	Glutamic Acid	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	275-280
34062977-4	2021	In that study, we used a well-known Hsp90 inhibitor geldanamycin, but it cannot be used as a therapy due to its adverse effects, including ocular toxicity.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
34062977-5	2021	Here, we have tested the effects of a novel Hsp90 inhibitor, TAS-116, on NLRP3 activation using geldanamycin as a reference compound.	TAS-116	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
35569376-5	2022	Either inhibitor of SLC6A14 (alpha-methyltryptophan) or of HSP90 (radicicol) had the cytotoxic effect, when added alone, while treatment with both compounds had a synergistic effect.	monorden	66-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
33802597-3	2021	Given the need to maximize treatment efficacy, the objective of this study was to use isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomic techniques to identify proteins in human lung adenocarcinoma cell lines whose basal abundances were correlated with response to HSP90 inhibitors (geldanamycin and radicicol derivatives).	geldanamycin	309-321	heat shock protein 90 alpha family class A member 1	Homo sapiens	291-296
33802597-3	2021	Given the need to maximize treatment efficacy, the objective of this study was to use isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomic techniques to identify proteins in human lung adenocarcinoma cell lines whose basal abundances were correlated with response to HSP90 inhibitors (geldanamycin and radicicol derivatives).	monorden	326-335	heat shock protein 90 alpha family class A member 1	Homo sapiens	291-296
33802597-7	2021	In contrast, arginine biosynthesis was correlated with sensitivity to HSP90 inhibitors.	Arginine	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
34164105-2	2021	This allows us to delineate how ATP hydrolysis in a protein causes allosteric changes at a distant protein binding site, using the chaperone Hsp90 as test system.	Adenosine Triphosphate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
34481829-0	2021	HSP90 inhibitors reduce cholesterol storage in Niemann-Pick type C1 mutant fibroblasts.	Cholesterol	24-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
34612127-10	2021	In addition, treatment with 120CEM43 increased intracellular HSP70 and the percentage of HCT116/HT29 cells in the G2/M cell cycle phase, ATP release and Calreticulin/HSP70/HSP90 exposure in the plasma membrane, while downregulating CD47 compared to sham-exposed cells.	120cem43	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
34612127-13	2021	CONCLUSION: Sub-ablative heating can act synergistically with the clinically relevant HSP90 inhibitor NVP-AUY922 to induce a pro-immunogenic form of cell death in colon cancer cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	102-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
34481829-6	2021	We found that HSP90 inhibition resulted in clearance of cholesterol from LE/Ly, and this was associated with enhanced delivery of the mutant NPC1I1061T protein to LE/Ly.	Cholesterol	56-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
35417848-0	2022	Panaxytriol upregulates CYP3A4 expression based on the interaction of PXR, CAR, HSP90alpha, and RXRalpha.	panaxytriol	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-90
35427968-4	2022	First, a proteomic analysis was used to screen for critical proteins (including RPL3, HSP90AA1, SOD, PGK1, GOT1, and PNP), indicating that abnormal protein synthesis, protein misfolding, oxidative stress, and metabolic dysfunction may contribute to SiNP-induced hepatotoxicity.	sinp	249-253	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-94
35405252-17	2022	Furthermore, Cortex Lycii made no change in the total AKT and mTOR protein levels, but caused the down-regulation of p-AKT and p-mTOR in human lung cancer cells, which was reversed by Terazosin, an agonist of HSP90.	Terazosin	184-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
35417848-5	2022	PURPOSE: This study investigated how the cofactors heat shock protein 90 alpha (HSP90alpha) and retinoid X receptor alpha (RXRalpha) interact with PXR and CAR to participate in the regulation of CYP3A4 by panaxytriol from the perspective of the PXR and CAR interaction.	panaxytriol	205-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-90
35417848-9	2022	RESULTS: In HepG2 cells and Huh-7 cells, panaxytriol (10-80 muM) upregulated CYP3A4 expression in a concentration-dependent manner by decreasing PXR binding to HSP90alpha and increasing PXR binding to RXRalpha.	panaxytriol	41-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-170
35417848-11	2022	Additionally, at the high concentration of 80 muM panaxytriol, CAR binding to HSP90alpha was weakened while binding to RXRalpha was enhanced.	panaxytriol	50-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-88
35417848-12	2022	CONCLUSION: Panaxytriol can upregulate CYP3A4 expression by promoting PXR dissociation from HSP90alpha and enhancing PXR binding to RXRalpha in HepG2 cells and Huh-7 cells.	panaxytriol	12-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-102
35501463-0	2022	A novel HSP90 inhibitor SL-145 suppresses metastatic triple-negative breast cancer without triggering the heat shock response.	sl-145	24-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
35501463-3	2022	SL-145 is a novel, rationally-designed C-terminal HSP90 inhibitor that induces apoptosis in TNBC cells via the suppression of oncogenic AKT, MEK/ERK, and JAK2/STAT3 signaling and does not trigger the HSR, in contrast to other inhibitors.	sl-145	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
35624462-0	2022	The HSP90 inhibitor KW-2478 depletes the malignancy of BCR/ABL and overcomes the imatinib-resistance caused by BCR/ABL amplification.	KW-2478	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
35624462-11	2022	KW-2478 inhibited the chaperone function of HSP90alpha and then weakened the BCR/ABL and MAPK signalling pathways.	KW-2478	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-54
35628494-8	2022	SK119 exhibited IC50 values in a nano-molar range, induced apoptosis and led to a dose-dependent increase in the expression and protein phosphorylation of HSP27 and HSP90 in WM9 and MUG-Mel 2 cells.	sk119	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
35588657-4	2022	Mass spectrometry results showed that C-316-1 bound to heat shock protein 90 (Hsp90), which was further confirmed by molecular docking and surface plasmon resonance.	Carbon	38-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-76
35588657-4	2022	Mass spectrometry results showed that C-316-1 bound to heat shock protein 90 (Hsp90), which was further confirmed by molecular docking and surface plasmon resonance.	Carbon	38-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
35588657-9	2022	Thereby, C-316-1 inhibited the Hsp90-Cdc37 complex formation and led to a significant decrease in RIPK1, which in turn reduced necroptosis.	Carbon	9-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
35588657-10	2022	Moreover, C-316-1 treatment did not protect against kidney injury in vivo and in vitro when Hsp90 was knocked down and R46, E47, and S50 in Cdc37 binding site of Hsp90 might form an important active pocket with C-316-1.	Carbon	211-212	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
35503206-0	2022	Crystal structure of the middle and C-terminal domains of Hsp90alpha labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target.	coumarin	84-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-68
35481368-4	2022	Using in vitro and in vivo results, it was confirmed that ADB enhanced the synergetic PDT and PTT upon irradiation using 685 nm near-infrared light (NIR) under a hypoxic tumor microenvironment where ATO can reduce O2 consumption and 17-DMAG can down-regulate HSP90.	adb	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	259-264
35481368-4	2022	Using in vitro and in vivo results, it was confirmed that ADB enhanced the synergetic PDT and PTT upon irradiation using 685 nm near-infrared light (NIR) under a hypoxic tumor microenvironment where ATO can reduce O2 consumption and 17-DMAG can down-regulate HSP90.	Atovaquone	199-202	heat shock protein 90 alpha family class A member 1	Homo sapiens	259-264
35586682-11	2022	This regulatory effect was related to the expression regulation of HSP90AA1, CDK2, STAT3, and phosphor-STAT3 (p-STAT3) by YQYJ, kaempferol, and quercetin.	kaempferol	128-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-75
35586682-11	2022	This regulatory effect was related to the expression regulation of HSP90AA1, CDK2, STAT3, and phosphor-STAT3 (p-STAT3) by YQYJ, kaempferol, and quercetin.	Quercetin	144-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-75
35247901-1	2022	PURPOSE: To investigate the anti-tumor activity of a mitochondrial-localized HSP90 inhibitor, Gamitrinib, in multiple glioma models, and to elucidate the anti-tumor mechanisms of Gamitrinib in gliomas.	Gamitrinib	94-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
35503206-2	2022	As drug targets for the treatment of cancer and neurodegenerative diseases, Hsp90 inhibitors that bind to the N-terminal ATP-binding site of Hsp90 have shown disappointing efficacy in clinical trials.	Adenosine Triphosphate	121-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
35522895-6	2022	Consequently, HSP90 inhibitor 17-AAG effectively blocks the growth and metastatic potential of MORC2-expressing breast cancer cells both in vitro and in vivo, and these noted effects are not due to HSP90 inhibition.	tanespimycin	30-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
35503206-2	2022	As drug targets for the treatment of cancer and neurodegenerative diseases, Hsp90 inhibitors that bind to the N-terminal ATP-binding site of Hsp90 have shown disappointing efficacy in clinical trials.	Adenosine Triphosphate	121-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
35503206-4	2022	Here, the crystal structure of the Hsp90alphaMC protein covalently linked to a coumarin derivative, MDCC {7-diethylamino-3-(N-(2-maleimidoethyl)carbamoyl)coumarin}, which is located in a hydrophobic pocket that is formed at the Hsp90alphaMC hexamer interface, is reported.	coumarin	79-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	228-233
35503206-4	2022	Here, the crystal structure of the Hsp90alphaMC protein covalently linked to a coumarin derivative, MDCC {7-diethylamino-3-(N-(2-maleimidoethyl)carbamoyl)coumarin}, which is located in a hydrophobic pocket that is formed at the Hsp90alphaMC hexamer interface, is reported.	mdcc {7-diethylamino-3-(n-(2-maleimidoethyl)carbamoyl)coumarin	100-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	228-233
35503206-6	2022	A fluorescence competition assay demonstrated that other characterized coumarin and isoflavone-containing Hsp90 inhibitors compete with MDCC binding, suggesting that they could bind at a common site or that they might allosterically alter the structure of the MDCC binding site.	Isoflavones	84-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
35503206-7	2022	This study provides insights into the mechanism by which the coumarin class of allosteric inhibitors potentially disrupt the function of Hsp90 by regulating its oligomerization and the burial of interaction sites involved in the ATP-dependent folding of Hsp90 clients.	coumarin	61-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
35503206-7	2022	This study provides insights into the mechanism by which the coumarin class of allosteric inhibitors potentially disrupt the function of Hsp90 by regulating its oligomerization and the burial of interaction sites involved in the ATP-dependent folding of Hsp90 clients.	coumarin	61-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	254-259
35503206-7	2022	This study provides insights into the mechanism by which the coumarin class of allosteric inhibitors potentially disrupt the function of Hsp90 by regulating its oligomerization and the burial of interaction sites involved in the ATP-dependent folding of Hsp90 clients.	Adenosine Triphosphate	229-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
35503206-7	2022	This study provides insights into the mechanism by which the coumarin class of allosteric inhibitors potentially disrupt the function of Hsp90 by regulating its oligomerization and the burial of interaction sites involved in the ATP-dependent folding of Hsp90 clients.	Adenosine Triphosphate	229-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	254-259
35307352-0	2022	Purine biosynthetic enzymes assemble into liquid-like condensates dependent on the activity of chaperone protein HSP90.	purine	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
35563784-0	2022	HSP90 Modulates T2R Bitter Taste Receptor Nitric Oxide Production and Innate Immune Responses in Human Airway Epithelial Cells and Macrophages.	Nitric Oxide	42-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35398094-4	2022	The ATP-dependent foldase function of both Hsp70 and Hsp90 actively transitions the toxic misfolded proteins back to their native conformation.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
35398094-5	2022	By contrast, the ATP-independent holdase function of Hsp70 and Hsp90 prevents the toxic accumulation of misfolded proteins.	Adenosine Triphosphate	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
35398094-11	2022	The holdase functions of Hsp70 and Hsp90 may thus allow neuronal cells to modulate misfolded proteins more energy efficient by reducing the long-term ATP running costs of the chaperone budget.	Adenosine Triphosphate	150-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
35563784-6	2022	Immunofluorescence showed that H441 cells express eNOS and T2Rs and that the bitter agonist denatonium benzoate activates NO production in a Ca2+- and HSP90-dependent manner in cells grown either as submerged cultures or at the air-liquid interface.	denatonium	92-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
35429283-0	2022	Design, synthesis, and biological evaluation of 4-(1H-1,2,3-triazol-1-yl)benzamides as HSP90 inhibitors.	4-(1h-1,2,3-triazol-1-yl)benzamides	48-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
35625528-1	2022	Hsp90 (Heat Shock Protein 90) is an ATP (Adenosine triphosphate) molecular chaperone responsible for the activation and maturation of client proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35625528-1	2022	Hsp90 (Heat Shock Protein 90) is an ATP (Adenosine triphosphate) molecular chaperone responsible for the activation and maturation of client proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-28
35625528-1	2022	Hsp90 (Heat Shock Protein 90) is an ATP (Adenosine triphosphate) molecular chaperone responsible for the activation and maturation of client proteins.	Adenosine	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35625528-1	2022	Hsp90 (Heat Shock Protein 90) is an ATP (Adenosine triphosphate) molecular chaperone responsible for the activation and maturation of client proteins.	Adenosine	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-28
35625528-4	2022	Hsp90 hydrolysis of ATP by each protomer may not be simultaneous and may be dependent on the specific client protein and co-chaperone complex involved.	Adenosine Triphosphate	20-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35429283-2	2022	Herein, a series of 4-(1H-1,2,3-triazol-1-yl)benzamides were rationally designed, synthesized as HSP90 inhibitors, and their structures were characterized by 1H NMR, 13C NMR, and HR-MS.	4-(1h-1,2,3-triazol-1-yl)benzamides	20-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
35429283-2	2022	Herein, a series of 4-(1H-1,2,3-triazol-1-yl)benzamides were rationally designed, synthesized as HSP90 inhibitors, and their structures were characterized by 1H NMR, 13C NMR, and HR-MS.	Carbon-13	166-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
35429283-5	2022	Molecular modeling studies also confirmed possible mode of interaction between 6u and the binding sites of HSP90 by hydrogen bond and hydrophobic interactions.	6u	79-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
35429283-5	2022	Molecular modeling studies also confirmed possible mode of interaction between 6u and the binding sites of HSP90 by hydrogen bond and hydrophobic interactions.	Hydrogen	116-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
35429283-6	2022	Above all, these encouraging data indicated that 6u could be used as a HSP90 inhibitor for further study and helped the recognition of the 4-(1H-1,2,3-triazol-1-yl)benzamide motif as a new scaffold for HSP90 inhibitors.	SCHEMBL6827358	139-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	202-207
35298171-0	2022	Species-Selective Targeting of Fungal Hsp90: Design, Synthesis, and Evaluation of Novel 4,5-Diarylisoxazole Derivatives for the Combination Treatment of Azole-Resistant Candidiasis.	4,5-diarylisoxazole	88-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
35586436-1	2022	KU-177 was recently shown to disrupt interactions between Hsp90 and Aha1 in vitro.	ku-177	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
35586436-2	2022	Subsequent studies in recombinant thioflavin T (ThT) assays demonstrated that KU-177 ablates Aha1-driven enhancement of Hsp90-dependent tau aggregation, which was confirmed by TEM.	thioflavin T	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
35586436-2	2022	Subsequent studies in recombinant thioflavin T (ThT) assays demonstrated that KU-177 ablates Aha1-driven enhancement of Hsp90-dependent tau aggregation, which was confirmed by TEM.	thioflavin T	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
35586436-3	2022	Using KU-177 as a lead compound, derivatives of KU-177 were synthesized and evaluated for their ability to disrupt Aha1/Hsp90 interactions and inhibit P301L tau aggregation.	ku-177	48-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
35298171-4	2022	Thus, a series of 4,5-diarylisoxazole analogues as fungal Hsp90 inhibitors were designed and synthesized that had potent synergistic effects with fluconazole in vitro and in vivo.	4,5-diarylisoxazole	18-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
35298171-4	2022	Thus, a series of 4,5-diarylisoxazole analogues as fungal Hsp90 inhibitors were designed and synthesized that had potent synergistic effects with fluconazole in vitro and in vivo.	Fluconazole	146-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
35463341-5	2022	Our results demonstrate that the membrane Hsp70 density, but not cytosolic HSP levels determines the radiosensitizing effect of the Hsp90 inhibitor NVP-AUY922 in LDH-/- cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	148-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
35400341-1	2022	Heat shock protein (Hsp) 90 is an ATP-dependent chaperone and plays a vital role in the folding, maturation, and stability of protein.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-27
35400341-3	2022	Inhibition of Hsp90 production and activity prevent ATP hydrolysis, resulting in the ubiquitination and proteasome degradation of client proteins.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
35464051-7	2022	We identified 24 related targets of mogroside V in patients with ovarian cancer and COVID-19 and characterised another 10 core targets of mogroside V against COVID-19 ovarian cancer, including Jun, IL2, HSP90AA1, AR, PRKCB, VEGFA, TLR9, TLR7, STAT3, and PRKCA.	mogroside V	138-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-211
35100463-7	2022	JAK degradation was caused by proteasome-dependent proteolysis, and we identified the direct binding of PAC to HSP90.	proanthocyanidin	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
35100463-8	2022	In addition, the binding of cochaperone ATPase homolog 1 (AHA1) to HSP90, which is required for activation of the cofactor HSP90, was inhibited by BB-PAC treatment.	bb-pac	147-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
35190872-0	2022	Hsp90 inhibition sensitizes DLBCL cells to cisplatin.	Cisplatin	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35190872-3	2022	Cisplatin resistance has been linked to impairments of the DNA damage response, and several DNA repair proteins have been identified as clients of the molecular chaperone Hsp90.	Cisplatin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
35190872-11	2022	Thus, cisplatin resistance could plausibly be overcome by combining the treatment with an Hsp90 inhibiting drug.	Cisplatin	6-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
35100463-8	2022	In addition, the binding of cochaperone ATPase homolog 1 (AHA1) to HSP90, which is required for activation of the cofactor HSP90, was inhibited by BB-PAC treatment.	bb-pac	147-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
35100463-9	2022	Therefore, BB-PAC inhibited the formation of the HSP90/AHA1 complex and promoted the degradation of JAK protein due to HSP90 dysfunction.	bb-pac	11-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
35100463-9	2022	Therefore, BB-PAC inhibited the formation of the HSP90/AHA1 complex and promoted the degradation of JAK protein due to HSP90 dysfunction.	bb-pac	11-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
35396004-4	2022	Cell morphology was observe; Cell viability and apoptosis rate of HSPC-1 were detected by MTT and flow cytometry, respectively.	monooxyethylene trimethylolpropane tristearate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-72
35396004-8	2022	The MTT analysis showed that cell viability of HSPC-1 in group B were lower than that of group A at 24 h, 48 h and 72 h (P<0.05); after transfected with DNMT3a, the cell viability of HSPC-1 in group D were higher than that of group B at 24 h, 48 h and 72 h (P<0.05).	monooxyethylene trimethylolpropane tristearate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-53
35107368-3	2022	Iinhibition of the Hsp90/Cdc37 complex by inhibitors (17-AAG and celastrol) or shRNAs significantly reduced expression levels of viral proteins and virus yield, suggesting that the Hsp90/Cdc37 chaperone complex functions in virus replication.	tanespimycin	54-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
35302136-3	2022	Here we present atomistic molecular dynamics (MD) simulations investigating the case study of dopamine-functionalized TiO2 nanoparticles and two proteins that are overexpressed in cancer cells, i.e. PARP1 and HSP90, since experiments proved them to be the main components of the corona in cell cultures.	Dopamine	94-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
35302136-3	2022	Here we present atomistic molecular dynamics (MD) simulations investigating the case study of dopamine-functionalized TiO2 nanoparticles and two proteins that are overexpressed in cancer cells, i.e. PARP1 and HSP90, since experiments proved them to be the main components of the corona in cell cultures.	titanium dioxide	118-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
35238566-1	2022	To discover celastrol (CEL) derivatives with enhanced Hsp90-Cdc37 inhibition, C-20-COOH was introduced with various substituted imidazoles, which might affect the Michael addition of CEL by nucleophilic attack.	celastrol	12-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
35238566-1	2022	To discover celastrol (CEL) derivatives with enhanced Hsp90-Cdc37 inhibition, C-20-COOH was introduced with various substituted imidazoles, which might affect the Michael addition of CEL by nucleophilic attack.	celastrol	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
35238566-1	2022	To discover celastrol (CEL) derivatives with enhanced Hsp90-Cdc37 inhibition, C-20-COOH was introduced with various substituted imidazoles, which might affect the Michael addition of CEL by nucleophilic attack.	c-20-cooh	78-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
35238566-1	2022	To discover celastrol (CEL) derivatives with enhanced Hsp90-Cdc37 inhibition, C-20-COOH was introduced with various substituted imidazoles, which might affect the Michael addition of CEL by nucleophilic attack.	Imidazoles	128-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
35238566-1	2022	To discover celastrol (CEL) derivatives with enhanced Hsp90-Cdc37 inhibition, C-20-COOH was introduced with various substituted imidazoles, which might affect the Michael addition of CEL by nucleophilic attack.	celastrol	183-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
35435890-8	2022	Hsp90 is an ATP-dependent molecular chaperone that plays an essential role in the folding, stability, maturation, and quality control of many proteins, thereby regulating multiple vital cellular functions.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35408505-5	2022	The experiments herein describe an anticancer mechanism in which heat shock protein 90 (HSP90) stabilizes HIF-1alpha, a master transcription factor of oxygen homeostasis that has been implicated in the survival, proliferation and malignant progression of cancers.	Oxygen	151-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-86
35408505-5	2022	The experiments herein describe an anticancer mechanism in which heat shock protein 90 (HSP90) stabilizes HIF-1alpha, a master transcription factor of oxygen homeostasis that has been implicated in the survival, proliferation and malignant progression of cancers.	Oxygen	151-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
35408505-9	2022	Interestingly, we found that 6-gingerol treatment suppressed activation of the transcription factor HIF-1alpha by downregulating HSP90 under both normoxic and hypoxic conditions.	gingerol	29-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
35107368-3	2022	Iinhibition of the Hsp90/Cdc37 complex by inhibitors (17-AAG and celastrol) or shRNAs significantly reduced expression levels of viral proteins and virus yield, suggesting that the Hsp90/Cdc37 chaperone complex functions in virus replication.	celastrol	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
35388292-7	2022	HSP90 inhibitors (AT13387 and AUY-922) prevented endothelial barrier dysfunction and hyperpermeability and reduced IKBalpha and AKT activation.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35388292-7	2022	HSP90 inhibitors (AT13387 and AUY-922) prevented endothelial barrier dysfunction and hyperpermeability and reduced IKBalpha and AKT activation.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	30-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35093502-0	2022	Elucidation of structure-activity relationship of humulanolides and identification of humulanolide analog as a novel HSP90 inhibitor.	humulanolide	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
35237814-7	2022	Biotin-tag cross-linking experiments indicated that the LH domain and PA28alpha interact with Luc bound by Hsp90 during refolding.	Biotin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
35093502-5	2022	Treatment with humulanolide analog E against human fibrosarcoma HT1080 cells increased the expression level of HSP70 protein and decreased the levels of AKT and CDK4, which are HSP90 client proteins.	humulanolide	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
35093502-6	2022	Moreover, humulanolide analog E inhibited refolding of denatured luciferase protein via suppression of HSP90 activity in vitro.	humulanolide	10-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
35093502-7	2022	These results suggest that humulanolide analog E possesses the anti-proliferative activity against human cancer cells by inhibiting HSP90 functions.	humulanolide	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
35266593-2	2022	Heat shock protein 90 (Hsp90) inhibitors are anti-inflammatory agents and P53 inducers, which reduce the production of reactive oxygen species (ROS) in a diverse variety of human tissues.	Reactive Oxygen Species	119-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
35370663-10	2022	Astragalus polysaccharides has the characteristics of multi-targets and multi-pathways, and its mechanism of action may be through regulating the expression of VCAM1, RELA, CDK2, JUN, CDK1, HSP90AA1, NOS2, SOD1, CASP3, AHSA1, PTGER3 and other genes during the development of pulmonary fibrosis.	astragalus polysaccharides	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-198
35327426-4	2022	Here, we evaluated the effects of the HSP90 inhibitors 17-DMAG, AUY922 and STA-9090 on MLS cell lines and in an MLS patient-derived xenograft (PDX) model.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	55-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
35327426-8	2022	Furthermore, all three tested HSP90 inhibitors displayed a synergistic combination effect with trabectidin, but not with doxorubicin.	trabectidin	95-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
35326427-2	2022	Studies on chaperon Hsp90 has revealed that it drives functional heme maturation of inducible nitric oxide synthase (iNOS), soluble guanylate cyclase (sGC) hemoglobin (Hb) and myoglobin (Mb) along with other proteins including GAPDH, while globin heme maturations also need an active sGC.	Heme	65-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
35326427-3	2022	In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes.	Heme	45-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
35326427-3	2022	In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes.	Heme	90-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
35326427-3	2022	In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes.	Adenosine Triphosphate	112-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
35326427-3	2022	In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes.	Heme	163-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
35326427-3	2022	In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes.	Heme	229-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
35266593-2	2022	Heat shock protein 90 (Hsp90) inhibitors are anti-inflammatory agents and P53 inducers, which reduce the production of reactive oxygen species (ROS) in a diverse variety of human tissues.	Reactive Oxygen Species	119-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
35266593-2	2022	Heat shock protein 90 (Hsp90) inhibitors are anti-inflammatory agents and P53 inducers, which reduce the production of reactive oxygen species (ROS) in a diverse variety of human tissues.	Reactive Oxygen Species	144-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
35266593-2	2022	Heat shock protein 90 (Hsp90) inhibitors are anti-inflammatory agents and P53 inducers, which reduce the production of reactive oxygen species (ROS) in a diverse variety of human tissues.	Reactive Oxygen Species	144-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
35238496-6	2022	Mechanistically, ITGB8 regulated lenvatinib resistance through an HSP90-mediated stabilization of AKT and enhanced AKT signaling.	lenvatinib	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
35264575-5	2022	Finally, we developed a universally applicable R-software package for predicting novel secondary therapies in chemotherapy-resistant cancers that outputs a list of the top drug combination candidates with rank and confidence scores.Thus, using 17AAG (HSP90 inhibitor) + FK866 (NAMPT inhibitor) as proof of principle secDrugs, we established a novel pipeline to introduce several new therapeutic options for the management of PI and IMiD-resistant myeloma.	tanespimycin	244-249	heat shock protein 90 alpha family class A member 1	Homo sapiens	251-256
35238496-7	2022	In support of this model, either an AKT inhibitor MK-2206 or an HSP90 inhibitor 17-AAG resensitized LR HCC cells to lenvatinib treatment.	tanespimycin	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
35238496-7	2022	In support of this model, either an AKT inhibitor MK-2206 or an HSP90 inhibitor 17-AAG resensitized LR HCC cells to lenvatinib treatment.	lenvatinib	116-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
35238496-8	2022	Conclusion: Collectively, our results establish a crucial role of ITGB8 in lenvatinib resistance, and suggest that targeting the ITGB8/HSP90/AKT axis is a promising therapeutic strategy in patients with HCC exhibiting lenvatinib resistance.	lenvatinib	75-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
35238496-8	2022	Conclusion: Collectively, our results establish a crucial role of ITGB8 in lenvatinib resistance, and suggest that targeting the ITGB8/HSP90/AKT axis is a promising therapeutic strategy in patients with HCC exhibiting lenvatinib resistance.	lenvatinib	218-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
35209223-6	2022	Bioinformatics analysis revealed these proteins are mainly ATP-binding and/or ATPase activity proteins, such as CKB, HSP86, HSP70-1, HSP90, ATPSF1beta and ACTG1, and highly associated with the regulation of the role of PKR in interferon induction and the antiviral response signaling pathway (P = 10-6), PI3K/AKT signaling pathway (P = 10-5) and eNOS signaling pathway (P = 10-4).	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
35263200-9	2022	Consistent with studies, Paclitaxel exhibited a significant inhibitory effect on Adriamycin-resistant DLBCL, which may have played a role in the five hub genes (UBC, TSR1, WDR46, HSP90AA1 and NOP56) and ribosome biosynthesis in eukaryotes pathway, but the specific regulation needs further experimental verification.	Paclitaxel	25-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-187
35110681-0	2022	HSP90 inhibitors induce GPNMB cell-surface expression by modulating lysosomal positioning and sensitize breast cancer cells to glembatumumab vedotin.	vedotin	141-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35110681-7	2022	Finally, treatment with HSP90 inhibitors sensitizes breast cancers to Glembatumumab Vedotin in vivo, suggesting that combination of HSP90 inhibitors and Glembatumumab Vedotin may be a viable treatment strategy for patients with metastatic TNBC.	vedotin	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
35110681-7	2022	Finally, treatment with HSP90 inhibitors sensitizes breast cancers to Glembatumumab Vedotin in vivo, suggesting that combination of HSP90 inhibitors and Glembatumumab Vedotin may be a viable treatment strategy for patients with metastatic TNBC.	vedotin	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
35110681-7	2022	Finally, treatment with HSP90 inhibitors sensitizes breast cancers to Glembatumumab Vedotin in vivo, suggesting that combination of HSP90 inhibitors and Glembatumumab Vedotin may be a viable treatment strategy for patients with metastatic TNBC.	vedotin	167-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
35045245-6	2022	Research findings indicated that flavonoids significantly exhibit various redox-based therapeutic responses against several diseases such as inflammatory, neurodegenerative, cardiovascular, and hepatic diseases and various types of cancer by activating the Nrf2/Keap1 transcription system, suppressing the nuclear factor kappaB (NF-kappaB)/IkappaB kinase inflammatory pathway, abrogating the function of the Hsp90/Hsf1 complex, inhibiting the PTEN/PI3K/Akt pathway, and preventing mitochondrial dysfunction.	Flavonoids	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	408-413
35022636-5	2022	This study proposed a novel multifunctional nanosystem for the targeted delivery of indocyanine green (ICG), 2,2"-azobis(2-(2-imidazolinI-2-yl) propane) dihydrochloride (AIBI), and heat shock protein 90 (Hsp90) inhibitor geldanamycin (17-AAG).	Indocyanine Green	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-202
35022636-5	2022	This study proposed a novel multifunctional nanosystem for the targeted delivery of indocyanine green (ICG), 2,2"-azobis(2-(2-imidazolinI-2-yl) propane) dihydrochloride (AIBI), and heat shock protein 90 (Hsp90) inhibitor geldanamycin (17-AAG).	Indocyanine Green	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
35022636-7	2022	Moreover, 17-AAG reduces heat resistance by inhibiting Hsp90, thereby achieving mild hyperthermia.	tanespimycin	10-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
35263200-6	2022	Five hub genes (UBC, TSR1, WDR46, HSP90AA1, and NOP56) were obtained via network analysis from 971 differentially expressed genes (DEGs) based on the RNA-seq of Paclitaxel-intervened Pfeiffer/ADM.	Paclitaxel	161-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-42
35227068-10	2022	Molecular docking verification showed that quercetin had the best binding with the core target protein HSP90AA1, and HSP90AA1 was the target protein with the best binding activity for the key chemical components in Xiexin capsules.	Quercetin	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-111
35227068-10	2022	Molecular docking verification showed that quercetin had the best binding with the core target protein HSP90AA1, and HSP90AA1 was the target protein with the best binding activity for the key chemical components in Xiexin capsules.	Quercetin	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-125
35227068-10	2022	Molecular docking verification showed that quercetin had the best binding with the core target protein HSP90AA1, and HSP90AA1 was the target protein with the best binding activity for the key chemical components in Xiexin capsules.	xiexin	215-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-125
35227068-11	2022	CONCLUSION: the main chemical components in the Xiexin capsules may participate in the regulation of PPAR and other signaling pathways by regulating key genes such as ESR1 (estrogen receptor 1), MAPK14 (mitogen-activated protein kinase 14), and HSP90AA1, to exert the pharmacological effect of the intervention on dyslipidemia.	xiexin	48-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	245-253
35280745-7	2022	Results by the complex crystal structure, TSA and ITC verified that NVP-AUY922 well accommodated in the ATP-binding pocket of Hsp90N to disable the molecular chaperone activity of Hsp90.	Adenosine Triphosphate	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-132
35280745-7	2022	Results by the complex crystal structure, TSA and ITC verified that NVP-AUY922 well accommodated in the ATP-binding pocket of Hsp90N to disable the molecular chaperone activity of Hsp90.	Adenosine Triphosphate	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
35051612-0	2022	Indoleamine dioxygenase and tryptophan dioxygenase activities are regulated through GAPDH- and Hsp90-dependent control of their heme levels.	Heme	128-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
35209223-6	2022	Bioinformatics analysis revealed these proteins are mainly ATP-binding and/or ATPase activity proteins, such as CKB, HSP86, HSP70-1, HSP90, ATPSF1beta and ACTG1, and highly associated with the regulation of the role of PKR in interferon induction and the antiviral response signaling pathway (P = 10-6), PI3K/AKT signaling pathway (P = 10-5) and eNOS signaling pathway (P = 10-4).	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
35163593-17	2022	Dissociation of HDAC6/Hsp90 with vimentin leading to increased vimentin acetylation and degradation was perceived in the cells with the addition of propolin G.	propolin G	148-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
35243415-0	2022	SU086, an inhibitor of HSP90, impairs glycolysis and represents a treatment strategy for advanced prostate cancer.	su086	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
35243415-5	2022	Cellular thermal shift assay reveals that SU086 binds to heat shock protein 90 (HSP90) and leads to a decrease in HSP90 levels.	su086	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
35243415-5	2022	Cellular thermal shift assay reveals that SU086 binds to heat shock protein 90 (HSP90) and leads to a decrease in HSP90 levels.	su086	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
35243415-5	2022	Cellular thermal shift assay reveals that SU086 binds to heat shock protein 90 (HSP90) and leads to a decrease in HSP90 levels.	su086	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
35243415-6	2022	Proteomic profiling demonstrates that SU086 binds to and decreases HSP90.	su086	38-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
35078937-2	2022	Hsp90 activity is often enhanced by cochaperones that drive conformational changes needed for ATP-dependent closure and capture of client proteins.	Adenosine Triphosphate	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
35051612-7	2022	In contrast, we found Hsp90 interacted with apo-IDO1 but not with apo-TDO, and was only needed to drive heme insertion into apo-IDO1.	Heme	104-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
35209964-8	2022	In the supernatant of FLC-4 cells with sunitinib, the heat shock protein (HSP) 90 was significantly increased.	Sunitinib	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-81
35046034-6	2022	The NO-triggered heme deployment involved cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-heme complexes and required the chaperone hsp90, and the newly formed sGC heterodimers remained functional long after NO generation had ceased.	Heme	17-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
35140796-14	2022	Molecular docking simulation indicated that potential glioma-related targets-MAPK1 and HSP90AA1 were bounded more firmly with epigallocatechin-3-gallate (EGCG) than with quercetin.	epigallocatechin gallate	126-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-95
35140796-14	2022	Molecular docking simulation indicated that potential glioma-related targets-MAPK1 and HSP90AA1 were bounded more firmly with epigallocatechin-3-gallate (EGCG) than with quercetin.	epigallocatechin gallate	154-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-95
35140796-14	2022	Molecular docking simulation indicated that potential glioma-related targets-MAPK1 and HSP90AA1 were bounded more firmly with epigallocatechin-3-gallate (EGCG) than with quercetin.	Quercetin	170-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-95
35140796-16	2022	Moreover, EGCG had the potential antiglioma activity by targeting MAPK1 and HSP90AA1.	epigallocatechin gallate	10-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-84
35046034-6	2022	The NO-triggered heme deployment involved cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-heme complexes and required the chaperone hsp90, and the newly formed sGC heterodimers remained functional long after NO generation had ceased.	Heme	100-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
34878465-5	2022	The released GA could enhance the NIR-II PTT efficacy by inhibiting the activity of HSP90, reducing the thermoresistance of tumors, exhibiting significant chemotherapeutic effects, and achieving synergistic anti-tumor efficiency.	gambogic acid	13-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
35022522-5	2022	High throughput screening identified the HDAC inhibitor, vorinostat and the HSP90 inhibitor, tanespimycin plus the JAK inhibitor, cerdulatinib as the most effective agents against cells expressing the MYB-TYK2 alteration.	tanespimycin	93-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
35090330-16	2022	We verified from molecular docking and protein level that gigantol can exert regulatory effects through three targets, ESR1, XIAP and HSP90AA1.	gigantol	58-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-142
35090330-17	2022	Furthermore, Western blot results tentatively revealed that gigantol may inhibit HCC progression through the HSP90/Akt/CDK1 pathway.	gigantol	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
35022522-5	2022	High throughput screening identified the HDAC inhibitor, vorinostat and the HSP90 inhibitor, tanespimycin plus the JAK inhibitor, cerdulatinib as the most effective agents against cells expressing the MYB-TYK2 alteration.	4-(cyclopropylamino)-2-((4-(4-(ethylsulfonyl)piperazin-1-yl)phenyl)amino)pyrimidine-5-carboxamide	130-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
35056725-0	2022	Synthesis and Biological Activity of 3-(Heteroaryl)quinolin-2(1H)-ones Bis-Heterocycles as Potential Inhibitors of the Protein Folding Machinery Hsp90.	3-(heteroaryl)quinolin-2(1h)-ones	37-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
34991674-5	2022	The potential mechanisms of Bufalin and KU-177 in AHSA1/HSP90 were verified by co-immunoprecipitation, mass spectrometry, site mutation and microscale thermophoresis assay.	bufalin	28-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
34991674-9	2022	Additionally, we identified AHSA1-K137 as the specific binding site of Bufalin on AHSA1, mutation of which decreased the interaction of AHSA1 with HSP90A and suppressed the function of AHSA1 on mediating CDK6 and PSMD2.	bufalin	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-153
35056769-7	2022	In conclusion, RF increased HSP90/BRAF/MEK/ERK expression, which decreased tyrosinase activity and increased lymphangiogenesis to eventually promote the clearance of dermal melanin-containing macrophages, thereby decreasing skin pigmentation.	Melanins	173-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
35056725-1	2022	In the context of our SAR study concerning 6BrCaQ analogues as C-terminal Hsp90 inhibitors, we designed and synthesized a novel series of 3-(heteroaryl)quinolin-2(1H), of types 3, 4, and 5, as a novel class of analogues.	6brcaq	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
35056725-1	2022	In the context of our SAR study concerning 6BrCaQ analogues as C-terminal Hsp90 inhibitors, we designed and synthesized a novel series of 3-(heteroaryl)quinolin-2(1H), of types 3, 4, and 5, as a novel class of analogues.	3-(heteroaryl)quinolin-2	138-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
35056725-1	2022	In the context of our SAR study concerning 6BrCaQ analogues as C-terminal Hsp90 inhibitors, we designed and synthesized a novel series of 3-(heteroaryl)quinolin-2(1H), of types 3, 4, and 5, as a novel class of analogues.	Hydrogen	163-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
35181624-7	2022	MiR-485-5p is a target for circ HIPK2 in non-small cell lung cancer; it reduced cell proliferation and accelerated HSP90 Ubiquitination in non-small cell lung cancer.	mir-485-5p	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
35059401-2	2021	Our previous study suggested the protective role of inhibiting heat shock protein 90 (HSP90) in IVDD, while the underlying mechanisms need advanced research.	ivdd	96-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-84
35059401-2	2021	Our previous study suggested the protective role of inhibiting heat shock protein 90 (HSP90) in IVDD, while the underlying mechanisms need advanced research.	ivdd	96-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
35091448-10	2022	Hsp90alpha was correlated with malondialdehyde to some extent and was an independent risk factor in the progression of diabetic vascular disease, with predictive ability.	Malondialdehyde	31-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
2507541-0	1989	The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues.	Threonine	133-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-112
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
34987637-5	2022	Regulation of Hsp90 by the selected compound NCT-80 (5-methoxy-N-(3-methoxy-4-(2-(pyridin-3-yl)ethoxy)phenyl)-2,2-dimethyl-2H-chromene-6-carboxamide) was investigated by immunoprecipitation, drug affinity responsive target stability assay, binding experiments using ATP-agarose beads and biotinylated drug, and docking analysis.	5-methoxy-n-(3-methoxy-4-(2-(pyridin-3-yl)ethoxy)phenyl)-2,2-dimethyl-2h-chromene-6-carboxamide	53-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
34987637-7	2022	Results: We demonstrated a distinct mechanism in which Hsp90 inhibitors that block N-terminal ATP-binding pocket causes transcriptional upregulation of Wnt ligands through Akt- and ERK-mediated activation of STAT3, resulting in NSCLC cell survival in an autocrine or paracrine manner.	Adenosine Triphosphate	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
34987637-9	2022	With regards to mechanism, NCT-80 directly bound to the C-terminal ATP-binding pocket of Hsp90, disrupting the interaction between Hsp90 and STAT3 and degrading STAT3 protein.	Adenosine Triphosphate	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
34987637-9	2022	With regards to mechanism, NCT-80 directly bound to the C-terminal ATP-binding pocket of Hsp90, disrupting the interaction between Hsp90 and STAT3 and degrading STAT3 protein.	Adenosine Triphosphate	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
2507541-2	1989	Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha.	Threonine	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-182
2507541-4	1989	Mouse hsp86 and rabbit hsp90 alpha are homologous to human hsp90 alpha; both heterologous proteins are phosphorylated at the same amino-terminal threonines by the human dsDNA-activated protein kinase.	Threonine	145-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
2507541-4	1989	Mouse hsp86 and rabbit hsp90 alpha are homologous to human hsp90 alpha; both heterologous proteins are phosphorylated at the same amino-terminal threonines by the human dsDNA-activated protein kinase.	Threonine	145-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-34
2703475-4	1989	The receptor synthesized under cell-free conditions also interacts with hsp90 both in the presence and absence of ligand, as determined by sucrose gradient centrifugation.	Sucrose	139-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
2779568-7	1989	A hormone-dependent dissociation of hsp90 from the cytosolic form of the receptor complex was observed within the first hour of in vivo progesterone treatment, which could explain the lack of hsp90 in nuclear receptor complexes.	Progesterone	136-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
2779568-8	1989	In a cell-free system, hsp90 binding to receptor was stabilized by molybdate but disrupted by high salt.	molybdate	67-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
2779568-8	1989	In a cell-free system, hsp90 binding to receptor was stabilized by molybdate but disrupted by high salt.	Salts	99-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
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
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
2706628-3	1989	Differentiation induction by dimethyl sulfoxide markedly decreased the level of the hsc90 expression, but preserved the ability to preferentially express hsp90 in response to heat stress.	Dimethyl Sulfoxide	29-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
2492519-2	1989	Both hsp 90s begin with proline; the initial methionine residue is removed.	Proline	24-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-11
2647745-4	1989	The rates of both temperature- and salt-dependent dissociation of hsp90 parallel the rates of loss of hormone-binding activity.	Salts	35-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
2647745-5	1989	Molybdate and hydrogen peroxide stabilize the hsp90-receptor complex against temperature-dependent dissociation.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
2647745-5	1989	Molybdate and hydrogen peroxide stabilize the hsp90-receptor complex against temperature-dependent dissociation.	Hydrogen Peroxide	14-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
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.	molybdate	85-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
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
2492519-4	1989	The purified hsp 90 mixture contains 2 mol of phosphate/mol of polypeptide.	Phosphates	46-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-19
3355552-2	1988	The 90 kDa heat shock protein, HSP90, was identified by labeling IM-9 cells with 35S-methionine at both 37 degrees C and 42 degrees C and purified to near homogeneity by sequential chromatography through DE52 and hydroxyapatite.	35s-methionine	81-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
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
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
2844180-4	1988	Polyclonal antibodies raised against the purified glucocorticoid receptor-associated hsp90 interact with the molybdate-stabilized 9 S dioxin-receptor complex but not with the 4 S dioxin receptor monomer, as assessed by sedimentation shift analysis on sucrose gradients.	molybdate	109-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
2844180-4	1988	Polyclonal antibodies raised against the purified glucocorticoid receptor-associated hsp90 interact with the molybdate-stabilized 9 S dioxin-receptor complex but not with the 4 S dioxin receptor monomer, as assessed by sedimentation shift analysis on sucrose gradients.	Sucrose	251-258	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
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
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.	Estradiol	76-85	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	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
3355552-2	1988	The 90 kDa heat shock protein, HSP90, was identified by labeling IM-9 cells with 35S-methionine at both 37 degrees C and 42 degrees C and purified to near homogeneity by sequential chromatography through DE52 and hydroxyapatite.	Durapatite	213-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
33845380-0	2021	Discovery of novel celastrol-triazole derivatives with Hsp90-Cdc37 disruption to induce tumor cell apoptosis.	celastrol	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
3517499-11	1986	Immunoadsorption of molybdate-stabilized cytosol with antibody directed against the 98-100 kdalton steroid receptor results in the immune-specific adsorption of a 90 kdalton phosphoprotein that reacts with anti-hsp89 antibody on Western blots.	molybdate	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	211-216
33845224-7	2021	Amongst HSPs, the protein levels of HSP70 and HSP90 were affected differentially by Th-nitrate/dioxide.	th-nitrate	84-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
33845224-7	2021	Amongst HSPs, the protein levels of HSP70 and HSP90 were affected differentially by Th-nitrate/dioxide.	dioxide	95-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
33845224-8	2021	Specific inhibitors of ATM (KU55933) or HSP90 (17AAG) were found to increase the Th- cytotoxicity suggesting prosurvival role of these signaling molecules in rescuing the cells from Th-toxicity.	Thorium	81-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
33845224-8	2021	Specific inhibitors of ATM (KU55933) or HSP90 (17AAG) were found to increase the Th- cytotoxicity suggesting prosurvival role of these signaling molecules in rescuing the cells from Th-toxicity.	Thorium	182-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
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
3312247-7	1987	Molybdate, vanadate, and tungstate inhibit receptor transformation to the DNA-binding form, an effect that appears to reflect the ability of these transition metal oxyanions to stabilize the complex between the steroid receptor and hsp90.	molybdate	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
3312247-7	1987	Molybdate, vanadate, and tungstate inhibit receptor transformation to the DNA-binding form, an effect that appears to reflect the ability of these transition metal oxyanions to stabilize the complex between the steroid receptor and hsp90.	Vanadates	11-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
3312247-7	1987	Molybdate, vanadate, and tungstate inhibit receptor transformation to the DNA-binding form, an effect that appears to reflect the ability of these transition metal oxyanions to stabilize the complex between the steroid receptor and hsp90.	tungstate	25-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
3312247-7	1987	Molybdate, vanadate, and tungstate inhibit receptor transformation to the DNA-binding form, an effect that appears to reflect the ability of these transition metal oxyanions to stabilize the complex between the steroid receptor and hsp90.	Metals	158-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
3312247-8	1987	By promoting the formation of disulfide bonds, hydrogen peroxide also stabilizes the glucocorticoid receptor-hsp90 complex and prevents receptor transformation.	Disulfides	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
3312247-8	1987	By promoting the formation of disulfide bonds, hydrogen peroxide also stabilizes the glucocorticoid receptor-hsp90 complex and prevents receptor transformation.	Hydrogen Peroxide	47-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
33934008-0	2021	Ring-opening of five-membered heterocycles conjugated 4-isopropylresorcinol scaffold-based benzamides as HSP90 inhibitors suppressing tumor growth in vitro and in vivo.	4-isopropylbenzene-1,3-diol	54-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
33934008-0	2021	Ring-opening of five-membered heterocycles conjugated 4-isopropylresorcinol scaffold-based benzamides as HSP90 inhibitors suppressing tumor growth in vitro and in vivo.	Benzamides	91-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
33845380-0	2021	Discovery of novel celastrol-triazole derivatives with Hsp90-Cdc37 disruption to induce tumor cell apoptosis.	Triazoles	29-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
33845380-1	2021	To enhance the disruption of Hsp90-Cdc37, we designed and synthesized a series (27) of CEL-triazole derivatives.	cel-triazole	87-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
34041691-6	2021	The approach was demonstrated on the N-terminal domain of human HSP90, for which complete assignment of Ala-beta, Ile-delta1, Leu-delta2, Met-epsilon, Thr-gamma and Val-gamma2 methyl groups was obtained.	Alanine	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
34041691-6	2021	The approach was demonstrated on the N-terminal domain of human HSP90, for which complete assignment of Ala-beta, Ile-delta1, Leu-delta2, Met-epsilon, Thr-gamma and Val-gamma2 methyl groups was obtained.	Threonine	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
34055735-0	2021	Development and Characterization of PLGA Nanoparticles Containing 17-DMAG, an Hsp90 Inhibitor.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	66-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
34044120-4	2021	A molecular docking study of compound 37 with a HSP90 homology model indicated that its S-isomer fit well in the ATP binding site of the C-terminal domain, forming key interactions.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
33999319-0	2021	Debio-0932, a second generation oral Hsp90 inhibitor, induces apoptosis in MCF-7 and MDA-MB-231 cell lines.	CUDC 305	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
33999319-2	2021	Debio-0932 is a second-generation Hsp90 inhibitor that exhibited promising anticancer activity against a wide variety of cancer types with a strong binding affinity for Hsp90 and high oral bioavailability.	CUDC 305	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
33999319-2	2021	Debio-0932 is a second-generation Hsp90 inhibitor that exhibited promising anticancer activity against a wide variety of cancer types with a strong binding affinity for Hsp90 and high oral bioavailability.	CUDC 305	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
33999319-4	2021	Molecular docking results indicated that Debio-0932 was selectively bound to the ATP binding pocket of the Hsp90 with an estimated free energy of binding - 7.24 kcal/mol.	CUDC 305	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
33999319-4	2021	Molecular docking results indicated that Debio-0932 was selectively bound to the ATP binding pocket of the Hsp90 with an estimated free energy of binding - 7.24 kcal/mol.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
34001607-7	2021	To control the quality of these expanding proteomes, core chaperones, ranging from heat shock proteins 20 (HSP20s) that prevent aggregation to HSP60, HSP70, HSP90, and HSP100 acting as adenosine triphosphate (ATP)-fueled unfolding and refolding machines, also evolved.	Adenosine	185-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
34003451-0	2021	Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes.	Phospholipids	81-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
34055735-3	2021	In this context, heat shock protein 90 (Hsp90) could present a novel therapeutic target, as evidence suggests that Hsp90 inhibitors, such as 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-DMAG), may represent promising chemotherapeutic agents against CL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	141-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-38
34055735-3	2021	In this context, heat shock protein 90 (Hsp90) could present a novel therapeutic target, as evidence suggests that Hsp90 inhibitors, such as 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-DMAG), may represent promising chemotherapeutic agents against CL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	141-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
34055735-3	2021	In this context, heat shock protein 90 (Hsp90) could present a novel therapeutic target, as evidence suggests that Hsp90 inhibitors, such as 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-DMAG), may represent promising chemotherapeutic agents against CL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	141-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
34055735-3	2021	In this context, heat shock protein 90 (Hsp90) could present a novel therapeutic target, as evidence suggests that Hsp90 inhibitors, such as 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-DMAG), may represent promising chemotherapeutic agents against CL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	194-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-38
34055735-3	2021	In this context, heat shock protein 90 (Hsp90) could present a novel therapeutic target, as evidence suggests that Hsp90 inhibitors, such as 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-DMAG), may represent promising chemotherapeutic agents against CL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	194-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
34055735-3	2021	In this context, heat shock protein 90 (Hsp90) could present a novel therapeutic target, as evidence suggests that Hsp90 inhibitors, such as 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-DMAG), may represent promising chemotherapeutic agents against CL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	194-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
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
33986242-9	2021	In vivo xenograft models confirmed the antitumor activity and showed the upregulation of acetyl-histone H3 and HSP70, biomarkers of pan-HDAC and HSP90 inhibition, with MPT0G449 treatment.	mpt0g449	168-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
33975383-8	2022	Treating a purified ferrous heme-containing sGCbeta with ODQ or NOC12 caused it to bind with Hsp90 without showing any heme loss.	ferrous heme	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
33975383-8	2022	Treating a purified ferrous heme-containing sGCbeta with ODQ or NOC12 caused it to bind with Hsp90 without showing any heme loss.	1H-(1,2,3)oxadiazolo(4,4-a)quinoxalin-1-one	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
33975383-8	2022	Treating a purified ferrous heme-containing sGCbeta with ODQ or NOC12 caused it to bind with Hsp90 without showing any heme loss.	Heme	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
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
33903104-5	2021	As a result, we identified radicicol, a heat-shock protein 90 (Hsp90) inhibitor that effectively suppressed CHIKV replication by blocking the synthesis of both positive- and negative-strand viral RNA as well as expression of viral proteins.	monorden	27-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
33932325-3	2021	We demonstrated that DDO-6600 covalently bound to Cys598 on the Hsp90 C terminus and exhibited antiproliferative activities against multiple tumor cells without inhibiting ATPase activity.	ddo-6600	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
33932325-4	2021	Further studies showed that DDO-6600 disrupted the interaction between Hsp90 and Cdc37, which induced the degradation of kinase client proteins in multiple tumor cell lines, promoted apoptosis, and inhibited cell motility.	ddo-6600	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
33975965-3	2021	The classical Hsp90 inhibitor tanespimycin has shown potent antileishmanial activity.	tanespimycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
33991836-0	2021	Discovery of pseudolaric acid A as a new Hsp90 inhibitor uncovers its potential anticancer mechanism.	pseudolaric acid A	13-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
33760187-12	2021	CRT expression was greatest following HOCl and ONOO- treatment, whereas HOCl and H2O2 resulted in the greatest increase in HSP70 and HSP90 expression levels.	Hypochlorous Acid	72-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
33760187-12	2021	CRT expression was greatest following HOCl and ONOO- treatment, whereas HOCl and H2O2 resulted in the greatest increase in HSP70 and HSP90 expression levels.	Hydrogen Peroxide	81-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
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
33846988-2	2022	Although over 30 HSP90 inhibitors have steadily entered clinical trials, further clinical advancement has been restricted by their limited efficacy, inevitable heat shock response, and multiple side-effects, likely induced via an ATP inhibition mechanism.	Adenosine Triphosphate	230-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
33846988-3	2022	Since both ATP and various co-chaperones play essential roles in the HSP90 chaperone cycle to achieve integrated function, optimal therapeutics require an understanding of the dynamic interactions among HSP90, ATP, and cochaperones.	Adenosine Triphosphate	11-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
33846988-3	2022	Since both ATP and various co-chaperones play essential roles in the HSP90 chaperone cycle to achieve integrated function, optimal therapeutics require an understanding of the dynamic interactions among HSP90, ATP, and cochaperones.	Adenosine Triphosphate	11-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
33846988-3	2022	Since both ATP and various co-chaperones play essential roles in the HSP90 chaperone cycle to achieve integrated function, optimal therapeutics require an understanding of the dynamic interactions among HSP90, ATP, and cochaperones.	Adenosine Triphosphate	210-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
32777911-2	2021	Methods: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with TBARS assay.	Phospholipids	39-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
33824458-0	2022	C0818, a novel curcumin derivative, induces ROS-dependent cytotoxicity in human hepatocellular carcinoma cells in vitro via disruption of Hsp90 function.	c0818	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
33824458-0	2022	C0818, a novel curcumin derivative, induces ROS-dependent cytotoxicity in human hepatocellular carcinoma cells in vitro via disruption of Hsp90 function.	Curcumin	15-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
33824458-0	2022	C0818, a novel curcumin derivative, induces ROS-dependent cytotoxicity in human hepatocellular carcinoma cells in vitro via disruption of Hsp90 function.	ros	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
33824458-4	2022	Compared to curcumin, a novel derivative of curcumin, 3,5-(E)-Bis(3-methoxy-4-hydroxybenzal)-4-piperidinone hydrochloride (C0818) that is more potent in Hsp90 inhibition and antitumor activity.	Curcumin	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
33824458-4	2022	Compared to curcumin, a novel derivative of curcumin, 3,5-(E)-Bis(3-methoxy-4-hydroxybenzal)-4-piperidinone hydrochloride (C0818) that is more potent in Hsp90 inhibition and antitumor activity.	3,5-(e)-bis(3-methoxy-4-hydroxybenzal)-4-piperidinone hydrochloride	54-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
33824458-4	2022	Compared to curcumin, a novel derivative of curcumin, 3,5-(E)-Bis(3-methoxy-4-hydroxybenzal)-4-piperidinone hydrochloride (C0818) that is more potent in Hsp90 inhibition and antitumor activity.	c0818	123-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
33824458-9	2022	C0818 induced the degradation of Hsp90 client proteins as RAS, C-Raf, P-C-Raf, Erk, P-ERK, MEK, P-MEK, Akt and P-Akt, which led to subsequent inhibition of the RAS/RAF/MEK/ERK and PI3K/AKT pathways.	c0818	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
32777911-4	2021	Results: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay.	Phospholipids	47-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32777911-4	2021	Results: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay.	Phospholipids	74-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32777911-2	2021	Methods: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with TBARS assay.	Phospholipids	66-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
33164261-3	2021	PPARdelta-Y108 phosphorylation in response to EGF recruited HSP90 (heat shock protein 90) to PPARdelta resulting in increased PPARdelta stability.	y108	10-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
32777911-4	2021	Results: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay.	Thiobarbituric Acid Reactive Substances	132-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32777911-5	2021	The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 muM.	1,1-diphenyl-2-picrylhydrazyl	4-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
32777911-5	2021	The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 muM.	2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid	13-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
32777911-6	2021	The EPR spectra demonstrated Hsp90 could directly scavenge  OH and PTIO  radicals.	ptio  radicals	67-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
33838214-1	2021	PURPOSE: Recent pre-clinical studies suggest combining the HSP90 inhibitor AT13387 (Onalespib) with radiation (IR) against colon cancer and HNSCC.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
33838214-1	2021	PURPOSE: Recent pre-clinical studies suggest combining the HSP90 inhibitor AT13387 (Onalespib) with radiation (IR) against colon cancer and HNSCC.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	84-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
33838214-4	2021	Metabolomic analysis of HSP90 inhibition by AT13387 was conducted to identify metabolic biomarkers of radiosensitization and whether modulations of key proteins were involved in IR-induced tumor vasculogenesis, a process involved in tumor recurrence.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	44-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
33164261-3	2021	PPARdelta-Y108 phosphorylation in response to EGF recruited HSP90 (heat shock protein 90) to PPARdelta resulting in increased PPARdelta stability.	y108	10-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-88
33331136-0	2021	HSP90 identified by a proteomic approach as druggable target to reverse platinum-resistance in ovarian cancer.	Platinum	72-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
33331136-3	2021	Using this approach, we identified several differentially expressed proteins in platinum-resistant compared to parental-cells, and the chaperone HSP90 as a central hub of these protein networks.	Platinum	80-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
33331136-4	2021	Accordingly, up-regulation of HSP90 was observed in all platinum-resistant cells and HSP90alpha knockout re-sensitizes platinum-resistant cells to cisplatin treatment.	Platinum	56-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
33331136-4	2021	Accordingly, up-regulation of HSP90 was observed in all platinum-resistant cells and HSP90alpha knockout re-sensitizes platinum-resistant cells to cisplatin treatment.	Platinum	119-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
33331136-4	2021	Accordingly, up-regulation of HSP90 was observed in all platinum-resistant cells and HSP90alpha knockout re-sensitizes platinum-resistant cells to cisplatin treatment.	Platinum	119-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-95
33331136-4	2021	Accordingly, up-regulation of HSP90 was observed in all platinum-resistant cells and HSP90alpha knockout re-sensitizes platinum-resistant cells to cisplatin treatment.	Cisplatin	147-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
33331136-4	2021	Accordingly, up-regulation of HSP90 was observed in all platinum-resistant cells and HSP90alpha knockout re-sensitizes platinum-resistant cells to cisplatin treatment.	Cisplatin	147-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-95
33331136-5	2021	Moreover, pharmacological HSP90 inhibition using two different inhibitors (17AAG and ganetespib) synergizes with cisplatin in killing platinum resistant cells in all tested models.	tanespimycin	75-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
33331136-5	2021	Moreover, pharmacological HSP90 inhibition using two different inhibitors (17AAG and ganetespib) synergizes with cisplatin in killing platinum resistant cells in all tested models.	STA 9090	85-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
33331136-5	2021	Moreover, pharmacological HSP90 inhibition using two different inhibitors (17AAG and ganetespib) synergizes with cisplatin in killing platinum resistant cells in all tested models.	Cisplatin	113-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
33331136-5	2021	Moreover, pharmacological HSP90 inhibition using two different inhibitors (17AAG and ganetespib) synergizes with cisplatin in killing platinum resistant cells in all tested models.	Platinum	134-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
33331136-6	2021	Mechanistically, genetic or pharmacological HSP90 inhibition plus cisplatin induced apoptosis and increased DNA-damage, particularly in platinum-resistant cells.	Platinum	136-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
33331136-7	2021	Importantly, the antitumor activities of HSP90 inhibitors were confirmed both ex vivo in primary cultures derived from platinum-resistant EOC patients ascites and in vivo in a xenograft model.	Platinum	119-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
33331136-8	2021	Collectively, our data suggest an innovative antitumor strategy, based on platinum-compounds plus HSP90 inhibitors, to re-challenge platinum-resistant EOC patients that might warrant further clinical evaluation.	Platinum	132-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
33713158-0	2021	Inhibition of NF-kappaB signaling and HSP70/HSP90 proteins by newly synthesized hydrazide derivatives in arthritis model.	hydrazide	80-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
33737511-0	2021	HSP90 inhibitor NVP-BEP800 affects stability of SRC kinases and growth of T-cell and B-cell acute lymphoblastic leukemias.	NVP-BEP800	16-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
33737511-3	2021	Using cell lines, primary cells and patient-derived xenograft (PDX) models, we demonstrate that ALL cells viability is sensitive to NVP-BEP800, an ATP-competitive inhibitor of Heat shock protein 90 (HSP90).	NVP-BEP800	132-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-197
33737511-3	2021	Using cell lines, primary cells and patient-derived xenograft (PDX) models, we demonstrate that ALL cells viability is sensitive to NVP-BEP800, an ATP-competitive inhibitor of Heat shock protein 90 (HSP90).	NVP-BEP800	132-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
33737511-3	2021	Using cell lines, primary cells and patient-derived xenograft (PDX) models, we demonstrate that ALL cells viability is sensitive to NVP-BEP800, an ATP-competitive inhibitor of Heat shock protein 90 (HSP90).	Adenosine Triphosphate	147-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-197
33737511-3	2021	Using cell lines, primary cells and patient-derived xenograft (PDX) models, we demonstrate that ALL cells viability is sensitive to NVP-BEP800, an ATP-competitive inhibitor of Heat shock protein 90 (HSP90).	Adenosine Triphosphate	147-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
33147371-2	2021	For client processing, the Hsp90 dimer undergoes a series of ATP-driven conformational rearrangements.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
33855025-0	2021	Complex Crystal Structure Determination and in vitro Anti-non-small Cell Lung Cancer Activity of Hsp90 N Inhibitor SNX-2112.	SNX 2112	115-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-104
33855025-1	2021	SNX-2112, as a promising anticancer lead compound targeting heat shock protein 90 (Hsp90), absence of complex crystal structure of Hsp90 N -SNX-2112 hindered further structural optimization and understanding on molecular interaction mechanism.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
33855025-1	2021	SNX-2112, as a promising anticancer lead compound targeting heat shock protein 90 (Hsp90), absence of complex crystal structure of Hsp90 N -SNX-2112 hindered further structural optimization and understanding on molecular interaction mechanism.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
33855025-3	2021	SNX-2112 exhibited high affinity and beneficial thermodynamic changes during the binding process with its target Hsp90 N confirmed by thermal shift assay (TSA, DeltaTm, and -9.51 +- 1.00 C) and isothermal titration calorimetry (K d , 14.10 +- 1.60 nM).	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
33855025-4	2021	Based on the complex crystal structure and molecular interaction analysis, 32 novel SNX-2112 derivatives were designed, and 25 new ones displayed increased binding force with the target Hsp90 N verified by molecular docking evaluation.	SNX 2112	84-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
33743824-2	2021	In this study, combination treatments of the HSP90 inhibitor AUY922 with either the ATR inhibitor VE821 or the ATM inhibitor KU55933 were investigated for their effectiveness in Ewing"s sarcoma cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	61-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
33663544-8	2021	METHODS: Human sperm was treated with the Hsp90-specific inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) during capacitation.	tanespimycin	67-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
33621080-1	2021	The cytosolic Hsp90-selective inhibitor TAS-116 has an acceptable safety profile and promising antitumor activity in clinical trials.	TAS-116	40-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
33621080-3	2021	Analyses of the co-crystal structure of Hsp90 and inhibitor TAS-116 suggest that TAS-116 interacts with the ATP-binding pocket, the ATP lid region, and the hydrophobic pocket.	Adenosine Triphosphate	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
33621080-3	2021	Analyses of the co-crystal structure of Hsp90 and inhibitor TAS-116 suggest that TAS-116 interacts with the ATP-binding pocket, the ATP lid region, and the hydrophobic pocket.	Adenosine Triphosphate	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
33621080-5	2021	THS-510 exhibited enthalpy-driven binding to Hsp90alpha and selectively inhibited cytosolic Hsp90 activity.	Thorium	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
33621080-5	2021	THS-510 exhibited enthalpy-driven binding to Hsp90alpha and selectively inhibited cytosolic Hsp90 activity.	Thorium	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
33621080-6	2021	The heat capacity change of THS-510 binding was positive, likely due to the induced conformational rearrangement of Hsp90.	Thorium	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
33663544-8	2021	METHODS: Human sperm was treated with the Hsp90-specific inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) during capacitation.	tanespimycin	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
33663544-13	2021	RESULTS: Human sperm hyperactivation and acrosome reaction were inhibited by 17-AAG, suggesting that Hsp90 is involved in human sperm capacitation.	tanespimycin	77-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
33663544-14	2021	In addition, Co-IP experiments revealed that 17-AAG reduced the interaction between Hsp90 and Cdc37, leading to the dissociation of Erk1/2 from the Hsp90-Cdc37 protein complex.	tanespimycin	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
33663544-14	2021	In addition, Co-IP experiments revealed that 17-AAG reduced the interaction between Hsp90 and Cdc37, leading to the dissociation of Erk1/2 from the Hsp90-Cdc37 protein complex.	tanespimycin	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
34057526-6	2021	The apoptosis stimulating effect of thiazino[6,5-b]indol in A2780cis cells was associated with significant irreversible downregulation of HSP70 and HSP90 and partly with a decrease of HSP40.	thiazino[6,5-b]indol	36-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
33675818-15	2021	CONCLUSION: Epithelial cell-derived HSP70 and HSP90 improve the function of epithelial cells, but block ASMC remodeling.	asmc	104-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
33675874-0	2021	Alcohol-induced Hsp90 acetylation is a novel driver of liver sinusoidal endothelial dysfunction and alcohol-related liver disease.	Alcohols	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
33675874-0	2021	Alcohol-induced Hsp90 acetylation is a novel driver of liver sinusoidal endothelial dysfunction and alcohol-related liver disease.	Alcohols	100-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
33738259-5	2021	Hsp90 downregulation by shHsp90 or inhibitor BIIB021 increased the sensitivity of multi-drug resistant ovarian cancer cells to paclitaxel and cisplatin, and augmented the drugs-induced apoptosis.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	45-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
33738259-5	2021	Hsp90 downregulation by shHsp90 or inhibitor BIIB021 increased the sensitivity of multi-drug resistant ovarian cancer cells to paclitaxel and cisplatin, and augmented the drugs-induced apoptosis.	Paclitaxel	127-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
33738259-5	2021	Hsp90 downregulation by shHsp90 or inhibitor BIIB021 increased the sensitivity of multi-drug resistant ovarian cancer cells to paclitaxel and cisplatin, and augmented the drugs-induced apoptosis.	Cisplatin	142-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
33738259-9	2021	Furthermore, Hsp90 enhanced the AKT/GSK3beta signaling, and AKT signaling played a critical role in Hsp90-induced accumulation and transcriptional activity of beta-catenin, as well as multi-drug resistance to paclitaxel and cisplatin.	Paclitaxel	209-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
33738259-9	2021	Furthermore, Hsp90 enhanced the AKT/GSK3beta signaling, and AKT signaling played a critical role in Hsp90-induced accumulation and transcriptional activity of beta-catenin, as well as multi-drug resistance to paclitaxel and cisplatin.	Paclitaxel	209-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
33738259-9	2021	Furthermore, Hsp90 enhanced the AKT/GSK3beta signaling, and AKT signaling played a critical role in Hsp90-induced accumulation and transcriptional activity of beta-catenin, as well as multi-drug resistance to paclitaxel and cisplatin.	Cisplatin	224-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
33738259-9	2021	Furthermore, Hsp90 enhanced the AKT/GSK3beta signaling, and AKT signaling played a critical role in Hsp90-induced accumulation and transcriptional activity of beta-catenin, as well as multi-drug resistance to paclitaxel and cisplatin.	Cisplatin	224-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
33675874-7	2021	Histone deacetylase 6 (HDAC6) was overexpressed specifically in liver ECs via adeno-associated virus (AAV)-mediated gene delivery to decrease Hsp90 acetylation in ethanol-fed mice.	Ethanol	163-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
33688189-0	2021	Hybrid Nanoparticles Modified by Hyaluronic Acid Loading an HSP90 Inhibitor as a Novel Delivery System for Subcutaneous and Orthotopic Colon Cancer Therapy.	Hyaluronic Acid	33-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
33688189-2	2021	However, the significant side effects of the HSP90 inhibitor 17AAG have limited its clinical use.	tanespimycin	61-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
33569547-5	2021	In the present study we investigated the role of Hsp90 inhibitors in the H2O2-induced brain endothelium breakdown, by employing human cerebral microvascular endothelial cells (hCMEC/D3).	Hydrogen Peroxide	73-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
33359710-8	2021	Consequently, the conformation-specific Hsp90 inhibitor, 17AAG, interfered with oncogenic RAF stability and function and inhibited cell proliferation.	tanespimycin	57-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
33569547-8	2021	Treatment of the hCMEC/D3 cells with Hsp90 inhibitors counteracted those events, and reduced the generation of the hydrogen peroxide - induced reactive oxygen species.	Hydrogen Peroxide	115-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
33569547-8	2021	Treatment of the hCMEC/D3 cells with Hsp90 inhibitors counteracted those events, and reduced the generation of the hydrogen peroxide - induced reactive oxygen species.	Oxygen	152-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
33672199-1	2021	The ATP-competitive inhibitors of Hsp90 have been tested predominantly in kinase addicted cancers; however, they have had limited success.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
33370472-4	2021	As a result, geldanamycin (GA), a known inhibitor of HSP90, was identified as a potential inhibitor of ROR1.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
33370472-4	2021	As a result, geldanamycin (GA), a known inhibitor of HSP90, was identified as a potential inhibitor of ROR1.	geldanamycin	27-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
33639524-6	2021	Co-incubation of cells with either TNF or TRAIL in combination with the HSP90beta inhibitor KUNB105 but not HSP90alpha selective inhibition promotes apoptosis induction.	kunb105	92-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-81
33412331-5	2021	Among these proteins, we identified 24 tyrosine phosphorylation sites in 17 mitochondrial proteins (AKAP1, VDAC1, VDAC2, VDAC3, LonP1, Hsp90, SLP2, PHB2, MIC60, UBA1, EF-Tu, LRPPRC, ACO2, OAT, ACAT1, ETFbeta and ATP5beta) as potential substrates for intramitochondrial Src using in silico prediction of tyrosine phospho-sites.	Tyrosine	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
33672199-5	2021	The low toxicity of conglobatin further indicates a beneficial on-target toxicity profile for Hsp90/Cdc37 interface inhibitors.	conglobatin	20-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
33610655-1	2021	KW-2478 is a promising anti-cancer lead compound targeting to the molecular chaperone heat shock protein 90 N (Hsp90N).	KW-2478	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-109
33672529-3	2021	In the present study, we investigated the inhibitory effect of penisuloxazin A (PNSA), a novel C- terminal inhibitor of HSP90, on metastasis of breast cancer cells and related mechanism in vitro.	penisuloxazin a	63-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
33672529-3	2021	In the present study, we investigated the inhibitory effect of penisuloxazin A (PNSA), a novel C- terminal inhibitor of HSP90, on metastasis of breast cancer cells and related mechanism in vitro.	pnsa	80-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
33672529-7	2021	Comparatively, the N-terminal inhibitor of HSP90 17-allyl-17-demethoxygeldanamycin (17-AAG) had no effect on EMT of MDA-MB-231 cells.	17-allyl-17-demethoxygeldanamycin	49-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
33672529-7	2021	Comparatively, the N-terminal inhibitor of HSP90 17-allyl-17-demethoxygeldanamycin (17-AAG) had no effect on EMT of MDA-MB-231 cells.	tanespimycin	84-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
33610655-1	2021	KW-2478 is a promising anti-cancer lead compound targeting to the molecular chaperone heat shock protein 90 N (Hsp90N).	KW-2478	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-117
33610655-3	2021	Herein, a high-resolution complex crystal structure of Hsp90N-KW-2478 was determined by X-ray diffraction (XRD, resolution limit: 1.59 A; PDB ID: 6LT8) and their molecular interaction was analyzed in detail, which suggested that KW-2478 perfectly bound in the N-terminal ATP-binding pocket of Hsp90 to disable its molecular chaperone function, therefore suppressed or killed cancer cells.	Adenosine Triphosphate	271-274	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-61
33898992-3	2021	In contrast, SM253, a C-terminal Hsp90 modulator, binds to the linker region between the N and middle domains.	SM253	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
33610655-4	2021	The results from thermal shift assay (TSA, DeltaTm, 18.82 +- 0.51  C) and isothermal titration calorimetry (ITC, Kd, 7.30 +- 2.20 nM) suggested that there is an intense binding force and favorable thermodynamic changes during the process of KW-2478 binding with Hsp90N.	KW-2478	241-248	heat shock protein 90 alpha family class A member 1	Homo sapiens	262-268
33610655-6	2021	Thirty-six novel KW-2478 derivatives were designed, based on the complex crystal structure and molecular interaction analysis of Hsp90N-KW-2478 complex.	KW-2478	17-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-135
33563272-5	2021	Benzaldehyde preconditioning activates systemic cytoprotective stress responses involving DAF-16/FOXO, SKN-1/Nrf2, and Hsp90 in non-neuronal cells, which confer both physiological (increased survival) and behavioral tolerance (reduced food avoidance) to benzaldehyde exposure.	benzaldehyde	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
33583094-0	2021	The HSP90 inhibitor RGRN-305 exhibits strong immunomodulatory effects in human keratinocytes.	rgrn-305	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
33583094-2	2021	RGRN-305 is a novel HSP90 inhibitor reported to reduce psoriatic phenotypes in preclinical animal models.	rgrn-305	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
33563187-12	2021	CONCLUSION: The biological evaluation results show that 2-aminobenzimidazole scaffold could be suggested as a lead for inhibition of Hsp90.	2-aminobenzimidazole	56-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
33547294-4	2021	Here, we show that a tryptophan residue in the proximal region of the tail decelerates the ATPase by allosterically switching the conformation of the catalytic loop in Hsp90.	Tryptophan	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
33563187-10	2021	The high level of Hsp70 expression and low level of Her2 expression confirmed ZINC00173501 as an Hsp90 inhibitor.	zinc00173501	78-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
33221456-1	2021	PURPOSE: With the ambition of improving the management of pancreatic neuroendocrine tumors (P-NETs), we developed and preliminary validated a novel fluorine-18 labelled HSP90 ligand.	Fluorine	148-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
32669028-0	2021	Columbamine suppresses proliferation and invasion of melanoma cell A375 via HSP90-mediated STAT3 activation.	columbamine	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
32669028-9	2021	Phosphorylation of STAT3 and expression of HSP90 was also repressed by columbamine in a concentration-dependent manner.	columbamine	71-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
32669028-10	2021	Overexpression of HSP90 attenuated the inhibition of cell proliferation, migration and invasion induced by columbamine.	columbamine	107-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
32669028-11	2021	CONCLUSION: Columbamine inhibited melanoma cell proliferation, migration, and invasion in A375 cells through inactivation of STAT3, which is mediated by HSP90.	columbamine	12-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
33416122-0	2021	Heat shock protein 90 as a molecular target for therapy in oral squamous cell carcinoma: Inhibitory effects of 17-DMAG and ganetespib on tumor cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	111-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33416122-0	2021	Heat shock protein 90 as a molecular target for therapy in oral squamous cell carcinoma: Inhibitory effects of 17-DMAG and ganetespib on tumor cells.	STA 9090	123-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33444025-3	2021	We recently described resorcylate aminopyrazoles (RAPs) as the first class of Hsp90 inhibitors capable of discriminating between fungal (Cryptococcus neoformans, Candida albicans) and human isoforms of Hsp90 in biochemical assays.	aminopyrazoles	34-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
33444025-3	2021	We recently described resorcylate aminopyrazoles (RAPs) as the first class of Hsp90 inhibitors capable of discriminating between fungal (Cryptococcus neoformans, Candida albicans) and human isoforms of Hsp90 in biochemical assays.	aminopyrazoles	34-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	202-207
33444025-3	2021	We recently described resorcylate aminopyrazoles (RAPs) as the first class of Hsp90 inhibitors capable of discriminating between fungal (Cryptococcus neoformans, Candida albicans) and human isoforms of Hsp90 in biochemical assays.	raps	50-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
33444025-3	2021	We recently described resorcylate aminopyrazoles (RAPs) as the first class of Hsp90 inhibitors capable of discriminating between fungal (Cryptococcus neoformans, Candida albicans) and human isoforms of Hsp90 in biochemical assays.	raps	50-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	202-207
33510287-12	2021	An MTT assay and quantitative real-time polymerase chain reaction (qRT-PCR) and Western blotting analyses demonstrated that the flavonoids of SCST revealed anti-hepatic fibrosis effects via anti-proliferation and increases in the Stat1, Pparg, Hsp90aa1 genes and STAT1 and PPARG proteins in LX-2 cells.	Flavonoids	128-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	244-252
33603951-9	2021	HSPs are multifunctional proteins because they closely interact with the antioxidant and the nitric oxide generation systems, such as HSP70/HSP90/NOS.	Nitric Oxide	93-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
33569349-0	2020	A Novel Mechanism of 17-AAG Therapeutic Efficacy on HSP90 Inhibition in MYCN-Amplified Neuroblastoma Cells.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
33569349-4	2020	Methods: We used cellular bio-functional (proliferation, migration/invasion, apoptosis, viability and stem-cell self-renewal) assays and Western blot analysis to elucidate the therapeutic efficacy of HSP90 inhibition with 17-AAG.	tanespimycin	222-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
33220262-0	2021	ATP impedes the inhibitory effect of Hsp90 on Abeta40 fibrillation.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
33220262-1	2021	Heat shock protein 90 (Hsp90) is a molecular chaperone that assists protein folding in an Adenosine triphosphate (ATP)-dependent way.	Adenosine	90-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33220262-1	2021	Heat shock protein 90 (Hsp90) is a molecular chaperone that assists protein folding in an Adenosine triphosphate (ATP)-dependent way.	Adenosine	90-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
33220262-1	2021	Heat shock protein 90 (Hsp90) is a molecular chaperone that assists protein folding in an Adenosine triphosphate (ATP)-dependent way.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33220262-1	2021	Heat shock protein 90 (Hsp90) is a molecular chaperone that assists protein folding in an Adenosine triphosphate (ATP)-dependent way.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
33220262-6	2021	ATP impedes this interaction, presumably by modulating Hsp90"s conformational dynamics and reducing its hydrophobic surface.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
33275968-0	2021	Visualizing the dynamics of a protein folding machinery: the mechanism of asymmetric ATP processing in Hsp90 and its implications for client remodelling.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
33537004-12	2020	Conclusions: The HSP90 inhibitor 17-AAG reduced the viability and secretory function of human pituitary ACTH-secreting tumor cells, and tumor cells carrying the USP8 mutant were more sensitive to 17-AAG than tumor cells carrying wild-type USP8.	tanespimycin	196-202	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
33109397-7	2021	Both in vitro and in vivo assays confirmed DDO-5994 as a promising inhibitor to exhibit ideal antitumor efficacy through blocking HSP90-CDC37 PPI.	ddo-5994	43-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
33537004-12	2020	Conclusions: The HSP90 inhibitor 17-AAG reduced the viability and secretory function of human pituitary ACTH-secreting tumor cells, and tumor cells carrying the USP8 mutant were more sensitive to 17-AAG than tumor cells carrying wild-type USP8.	tanespimycin	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
33189438-2	2021	Natural product aconitine is a potential Hsp90 inhibitor reported in our previous work.	Aconitine	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
33189438-3	2021	In this study, we designed and synthesized a series of 2-((1-phenyl-1H-1,2,3-triazol-4-yl)methyl)-2-azabicyclo[3.2.1]octan-3-one derivatives as potent Hsp90 inhibitors by simplifying and modifying aconitine scaffold.	2-((1-phenyl-1h-1,2,3-triazol-4-yl)methyl)-2-azabicyclo[3.2.1]octan-3-one	55-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
33242760-3	2021	Viral growth kinetics assays show that Hsp90 inhibitor geldanamycin (GA) abrogates PRV replication at the post-penetration step.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
33440739-0	2021	HSP90alpha Mediates Sorafenib Resistance in Human Hepatocellular Carcinoma by Necroptosis Inhibition under Hypoxia.	Sorafenib	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
33242760-3	2021	Viral growth kinetics assays show that Hsp90 inhibitor geldanamycin (GA) abrogates PRV replication at the post-penetration step.	geldanamycin	69-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
33440739-7	2021	HSP90alpha binds with the necrosome complex and promotes chaperone-mediated autophagy (CMA) degradation, which leads necroptosis blocking and results in Sorafenib resistance.	Sorafenib	153-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
33440739-10	2021	All the results emphasized that HSP90alpha plays a critical role in Sorafenib resistance under hypoxia and 17-AAG combined with Sorafenib is a promising therapy for hepatocellular carcinoma.	Sorafenib	68-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-42
33439458-4	2021	Proteasome inhibitor MG132 but not autophagy inhibitor chloroquine could suppress the Hsp90 inhibitor STA-9090-induced reduction of Ikaros, which is accompanied with the increased ubiquitination of Ikaros.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	21-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
33439458-4	2021	Proteasome inhibitor MG132 but not autophagy inhibitor chloroquine could suppress the Hsp90 inhibitor STA-9090-induced reduction of Ikaros, which is accompanied with the increased ubiquitination of Ikaros.	STA 9090	102-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
33407570-4	2021	RESULTS: Near-infrared photosensitizer (IR780) and gambogic acid (GA, Hsp90 inhibitor) were encapsulated into albumin nanoparticles via hydrophobic interaction, which was further deposited MnO2 on the surface to form IGM nanoparticles.	gambogic acid	51-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
33490651-4	2021	In silico findings reveal its strong binding affinity with NOX5 C terminal HSP90 binding site that disrupts NOX5 stability and its ability to generate ROS, leading to restoration antioxidant enzymes activities.	Reactive Oxygen Species	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
33414495-6	2021	Hsp90 correlated positively with C-reactive protein and negatively with pulmonary function tests: forced vital capacity and diffusing capacity for carbon monoxide (DLCO).	Carbon Monoxide	147-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
33414495-12	2021	Baseline plasma Hsp90 predicts the 12-month change in DLCO in SSc-ILD patients treated with cyclophosphamide.	Cyclophosphamide	92-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
33407570-4	2021	RESULTS: Near-infrared photosensitizer (IR780) and gambogic acid (GA, Hsp90 inhibitor) were encapsulated into albumin nanoparticles via hydrophobic interaction, which was further deposited MnO2 on the surface to form IGM nanoparticles.	manganese dioxide	189-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
33407570-7	2021	In addition, the release of GA was promoted by irradiation to bind with Hsp90, which could reduce cell tolerance to heat for PTT enhancement.	gambogic acid	28-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
33407570-7	2021	In addition, the release of GA was promoted by irradiation to bind with Hsp90, which could reduce cell tolerance to heat for PTT enhancement.	Bialaphos	125-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
32404982-0	2021	DCZ5248, a novel dual inhibitor of Hsp90 and autophagy, exerts antitumor activity against colon cancer.	dcz5248	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
32404982-3	2021	In this study, we identified DCZ5248, a triazine derivative, was a dual inhibitor of both Hsp90 and late-autophagy with potent antitumor activity against colon cancer cells in vitro and in vivo.	dcz5248	29-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
32404982-3	2021	In this study, we identified DCZ5248, a triazine derivative, was a dual inhibitor of both Hsp90 and late-autophagy with potent antitumor activity against colon cancer cells in vitro and in vivo.	Triazines	40-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
32404982-4	2021	We showed that DCZ5248 (0.1-10 muM) induced dose-dependent degradation of Hsp90 client proteins (AKT, CDK4, CDK6 and RAF-1) in HCT 116 colon cancer cells through a proteasome-dependent pathway.	dcz5248	15-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
32404982-8	2021	Importantly, inhibition of both Hsp90 function and autophagy by DCZ5248 induced G1-phase cell cycle arrest, apoptosis, and exerted potent antitumor activity against colon cancer cells both in vitro and in vivo.	dcz5248	64-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
32404982-9	2021	These findings demonstrate that DCZ5248 is a novel dual inhibitor of Hsp90 and autophagy with potential for colon cancer therapy.	dcz5248	32-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
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
32656999-4	2021	MATERIALS AND METHODS: We examined the effects of H-89 (a protein kinase A [PKA] inhibitor) and Go6983 (a protein kinase C [PKC] inhibitor) on the phosphorylation of serine, threonine, and tyrosine residues in Hsp90; the effect of 17-allylamino-17-demethoxygeldanamycin (17-AAG, Hsp90 inhibitor) on Y416-Src phosphorylation; and the effects of 17-AAG and geldanamycin on threonine phosphorylation during human sperm capacitation.	Serine	166-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-215
33080246-3	2021	This study investigated the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-specific inhibitor, on Bombyx mori nucleopolyhedrovirus (BmNPV) infection.	tanespimycin	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
33404528-0	2021	Complex crystal structure determination and anti-non-small-cell lung cancer activity of the Hsp90N inhibitor Debio0932.	CUDC 305	109-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-98
33404528-1	2021	Debio0932 is a promising lead compound in phase I clinical trials targeting the N-terminal ATP-binding pocket of the molecular chaperone heat-shock protein 90 (Hsp90N).	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-166
33404528-3	2021	Here, a high-resolution crystal structure of the Hsp90N-Debio0932 complex was successfully determined (resolution limit 2.20 A; PDB entry 6lr9) by X-ray diffraction and the molecular-interaction mechanism was analysed in detail, which suggested that Debio0932 suppresses cancer cells by accommodating itself in the ATP-binding pocket of Hsp90N, disabling its molecular-chaperone capability.	Adenosine Triphosphate	315-318	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-55
32656999-4	2021	MATERIALS AND METHODS: We examined the effects of H-89 (a protein kinase A [PKA] inhibitor) and Go6983 (a protein kinase C [PKC] inhibitor) on the phosphorylation of serine, threonine, and tyrosine residues in Hsp90; the effect of 17-allylamino-17-demethoxygeldanamycin (17-AAG, Hsp90 inhibitor) on Y416-Src phosphorylation; and the effects of 17-AAG and geldanamycin on threonine phosphorylation during human sperm capacitation.	Serine	166-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	279-284
32656999-6	2021	During human sperm capacitation, Hsp90 phosphorylation at serine, threonine, and tyrosine residues was inhibited by H-89 and Go6983.	Serine	58-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
32656999-6	2021	During human sperm capacitation, Hsp90 phosphorylation at serine, threonine, and tyrosine residues was inhibited by H-89 and Go6983.	Threonine	66-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
32656999-6	2021	During human sperm capacitation, Hsp90 phosphorylation at serine, threonine, and tyrosine residues was inhibited by H-89 and Go6983.	Tyrosine	81-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
32656999-6	2021	During human sperm capacitation, Hsp90 phosphorylation at serine, threonine, and tyrosine residues was inhibited by H-89 and Go6983.	N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide	116-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
32656999-6	2021	During human sperm capacitation, Hsp90 phosphorylation at serine, threonine, and tyrosine residues was inhibited by H-89 and Go6983.	2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimide	125-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
32656999-8	2021	DISCUSSION AND CONCLUSION: Taken together, our data showed that the interaction of Hsp90 with Cdc37 regulates total protein threonine phosphorylation and Src phosphorylation via its serine, threonine, and tyrosine phosphorylation, which are controlled by PKA and PKC during human sperm capacitation.	Threonine	124-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
32656999-8	2021	DISCUSSION AND CONCLUSION: Taken together, our data showed that the interaction of Hsp90 with Cdc37 regulates total protein threonine phosphorylation and Src phosphorylation via its serine, threonine, and tyrosine phosphorylation, which are controlled by PKA and PKC during human sperm capacitation.	Serine	182-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
32656999-8	2021	DISCUSSION AND CONCLUSION: Taken together, our data showed that the interaction of Hsp90 with Cdc37 regulates total protein threonine phosphorylation and Src phosphorylation via its serine, threonine, and tyrosine phosphorylation, which are controlled by PKA and PKC during human sperm capacitation.	Threonine	190-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
32656999-8	2021	DISCUSSION AND CONCLUSION: Taken together, our data showed that the interaction of Hsp90 with Cdc37 regulates total protein threonine phosphorylation and Src phosphorylation via its serine, threonine, and tyrosine phosphorylation, which are controlled by PKA and PKC during human sperm capacitation.	Tyrosine	205-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
33162400-11	2021	Altogether, our results demonstrate that SUV39H1 is a new client protein of Hsp90 degradated by Chaetocin as a novel C-terminal inhibitor of Hsp90.	chaetocin	96-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
33162400-0	2021	SUV39H1 is a New Client Protein of Hsp90 Degradated by Chaetocin as a Novel C-Terminal Inhibitor of Hsp90.	chaetocin	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
33162400-11	2021	Altogether, our results demonstrate that SUV39H1 is a new client protein of Hsp90 degradated by Chaetocin as a novel C-terminal inhibitor of Hsp90.	chaetocin	96-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
33162400-0	2021	SUV39H1 is a New Client Protein of Hsp90 Degradated by Chaetocin as a Novel C-Terminal Inhibitor of Hsp90.	chaetocin	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
33162400-12	2021	The study establishes a new relationship of Chaetocin and SUV39H1, and paves an avenue for exploring a new strategy to target SUV39H1 by inhibition of Hsp90 in leukemia.	chaetocin	44-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
33162400-4	2021	Herein, we find that Chaetocin is an inhibitor of Hsp90 which binds to the C-terminal of Hsp90alpha.	chaetocin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
31820701-0	2021	Network Pharmacology Approach uncovering Pathways involved in targeting Hsp90 through Curcumin and Epigallocatechin to control Inflammation.	Curcumin	86-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
33162400-4	2021	Herein, we find that Chaetocin is an inhibitor of Hsp90 which binds to the C-terminal of Hsp90alpha.	chaetocin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-99
33162400-5	2021	Chaetocin inhibited a variety of Hsp90 client proteins including AMl1-ETO and BCL-ABL, the mutant fusion-protein in the K562 and HL-60 cells.	chaetocin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
33162400-7	2021	We found that inhibition of Hsp90 by Chaetocin and 17-AAG had ability to induce degradation of SUV39H1 through proteasome pathway.	chaetocin	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
33162400-10	2021	Moreover, Chaetocin was able to induce cell differentiation in the two cells in the concentration range of Hsp90 inhibition.	chaetocin	10-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
32869129-3	2021	In this study, we investigated this phenomenon in various cell lines and found that HSP90 was cleaved by treatment with SAHA or MG132 in 6 out of 16 solid tumor cell lines.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	128-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
32869129-4	2021	To further investigate the effects of HSP90 cleavage on cells, we introduced mutations to the potential cleavage sites of HSP90beta and found that the 294th aspartic acid residue of the protein was mainly cleaved.	Aspartic Acid	157-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
32869129-4	2021	To further investigate the effects of HSP90 cleavage on cells, we introduced mutations to the potential cleavage sites of HSP90beta and found that the 294th aspartic acid residue of the protein was mainly cleaved.	Aspartic Acid	157-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-131
32869129-5	2021	In the K562 and Mia-PaCa-2 cell lines expressing HSP90beta D294A, the cleavage of HSP90 by the treatment with SAHA or MG132 was reduced compared with the K562 and Mia-PaCa-2 cell lines expressing HSP90beta WT.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	118-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-58
32869129-5	2021	In the K562 and Mia-PaCa-2 cell lines expressing HSP90beta D294A, the cleavage of HSP90 by the treatment with SAHA or MG132 was reduced compared with the K562 and Mia-PaCa-2 cell lines expressing HSP90beta WT.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	118-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
32869129-5	2021	In the K562 and Mia-PaCa-2 cell lines expressing HSP90beta D294A, the cleavage of HSP90 by the treatment with SAHA or MG132 was reduced compared with the K562 and Mia-PaCa-2 cell lines expressing HSP90beta WT.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	118-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-205
33326835-6	2021	Isocotoin inhibits HEV replication through interference with heat shock protein 90 (HSP90), a host factor not previously known to be involved in HEV replication.	isocotoin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
33037995-2	2021	Hsp90 and a cohort of interacting proteins called cochaperones interact with clients in an ATP-dependent cycle.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31820701-0	2021	Network Pharmacology Approach uncovering Pathways involved in targeting Hsp90 through Curcumin and Epigallocatechin to control Inflammation.	gallocatechol	99-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
31820701-4	2021	Curcumin and EGC were also found to bind -N and -C terminal domain of Hsp90 respectively.	Curcumin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
31820701-6	2021	Hsp90 associated gene targets of Curcumin and EGC were collected from databases, and gene ontology studies were done.	Curcumin	33-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31820701-10	2021	Main proteins involved were identified as key regulators in Pkcdelta-Nrf2 and Tlr4 pathway for controlling expression of Hsp90 from Curcumin and EGC in inflammation.	Curcumin	132-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
31820701-11	2021	Docking was performed on main proteins, Hsp90, Pkcdelta and Tlr4 with Curcumin and EGC, significant binding energy was obtained for docked complexes.	Curcumin	70-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
31820701-13	2021	Present study is an attempt to unravel common pathways mediated in intervention of Curcumin and EGC for suppression of Hsp90 associated with inflammation.	Curcumin	83-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
33037138-7	2021	Treatment of immortalized and primary patient PSC/CAF with the Hsp90 inhibitor XL888 decreased IL-6, a key cytokine that orchestrates immune changes in PDAC at the transcript and protein level in vitro.	XL 888	79-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
33388604-4	2021	We show that the conformation specific Hsp90 inhibitor, 17AAG decreases the total cellular E2F levels more selectively in cancer cells than transformed cells.	tanespimycin	56-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
33866334-1	2021	OBJECTIVE: We investigated whether heat shock protein 90alpha (HSP90alpha) expression is associated with fluorine-18-labeled fluoro-2-deoxy-D-glucose (18F-FDG) uptake and whether 18F-FDG positron emission tomography/computed tomography (PET/CT) can be used to predict the status of HSP90alpha expression in colorectal cancer (CRC).	Fluorine	105-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-73
33866334-1	2021	OBJECTIVE: We investigated whether heat shock protein 90alpha (HSP90alpha) expression is associated with fluorine-18-labeled fluoro-2-deoxy-D-glucose (18F-FDG) uptake and whether 18F-FDG positron emission tomography/computed tomography (PET/CT) can be used to predict the status of HSP90alpha expression in colorectal cancer (CRC).	Glucose	142-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-73
33866334-1	2021	OBJECTIVE: We investigated whether heat shock protein 90alpha (HSP90alpha) expression is associated with fluorine-18-labeled fluoro-2-deoxy-D-glucose (18F-FDG) uptake and whether 18F-FDG positron emission tomography/computed tomography (PET/CT) can be used to predict the status of HSP90alpha expression in colorectal cancer (CRC).	Fluorodeoxyglucose F18	151-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-73
33866334-7	2021	There was a significant correlation between HSP90alpha expression and 18F-FDG uptake (r=0.354, P=0.011).	Fluorodeoxyglucose F18	70-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-54
33866334-10	2021	CONCLUSION: The expression status of HSP90alpha was significantly related to 18F-FDG uptake in CRC.	Fluorodeoxyglucose F18	77-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-47
33181440-2	2021	Heat shock protein 90 (Hsp90) was reported to inhibit superoxide generation from nNOS protein.	Superoxides	54-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33181440-2	2021	Heat shock protein 90 (Hsp90) was reported to inhibit superoxide generation from nNOS protein.	Superoxides	54-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
33181440-6	2021	In the present work, purified recombinant human Hsp90alpha, in its native dimeric state, was used in electron paramagnetic resonance (EPR) spin trapping experiments to study the effects of Hsp90alpha on superoxide generation from nNOS splice variants nNOSmu and nNOSalpha.	Superoxides	203-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-58
33181440-7	2021	Human Hsp90alpha was found to significantly increase superoxide generation from nNOSmu and nNOSalpha proteins under l-Arg-depleted conditions and Hsp90alpha influenced superoxide production by nNOSmu and nNOSalpha at varying degrees.	Superoxides	53-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-16
33181440-7	2021	Human Hsp90alpha was found to significantly increase superoxide generation from nNOSmu and nNOSalpha proteins under l-Arg-depleted conditions and Hsp90alpha influenced superoxide production by nNOSmu and nNOSalpha at varying degrees.	Arginine	116-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-16
33181440-7	2021	Human Hsp90alpha was found to significantly increase superoxide generation from nNOSmu and nNOSalpha proteins under l-Arg-depleted conditions and Hsp90alpha influenced superoxide production by nNOSmu and nNOSalpha at varying degrees.	Superoxides	168-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-16
33181440-7	2021	Human Hsp90alpha was found to significantly increase superoxide generation from nNOSmu and nNOSalpha proteins under l-Arg-depleted conditions and Hsp90alpha influenced superoxide production by nNOSmu and nNOSalpha at varying degrees.	Superoxides	168-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-156
33181440-8	2021	Imidazole suppressed the spin adduct signal, indicating that superoxide was produced at the heme site of nNOS in the presence of Hsp90alpha, whereas l-Arg repletion diminished superoxide production by the nNOS-Hsp90alpha.	imidazole	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-139
33181440-8	2021	Imidazole suppressed the spin adduct signal, indicating that superoxide was produced at the heme site of nNOS in the presence of Hsp90alpha, whereas l-Arg repletion diminished superoxide production by the nNOS-Hsp90alpha.	imidazole	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-220
33181440-8	2021	Imidazole suppressed the spin adduct signal, indicating that superoxide was produced at the heme site of nNOS in the presence of Hsp90alpha, whereas l-Arg repletion diminished superoxide production by the nNOS-Hsp90alpha.	Superoxides	61-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-139
33181440-8	2021	Imidazole suppressed the spin adduct signal, indicating that superoxide was produced at the heme site of nNOS in the presence of Hsp90alpha, whereas l-Arg repletion diminished superoxide production by the nNOS-Hsp90alpha.	Superoxides	61-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-220
33181440-8	2021	Imidazole suppressed the spin adduct signal, indicating that superoxide was produced at the heme site of nNOS in the presence of Hsp90alpha, whereas l-Arg repletion diminished superoxide production by the nNOS-Hsp90alpha.	Heme	92-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-139
33181440-8	2021	Imidazole suppressed the spin adduct signal, indicating that superoxide was produced at the heme site of nNOS in the presence of Hsp90alpha, whereas l-Arg repletion diminished superoxide production by the nNOS-Hsp90alpha.	Superoxides	176-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-220
33181440-9	2021	Moreover, NADPH consumption rate values exhibited a similar trend/difference as a function of Hsp90alpha and l-Arg.	NADP	10-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-104
33181440-10	2021	Together, these EPR spin trapping and NADPH oxidation kinetics results demonstrated noticeable Hsp90alpha-induced increases in superoxide production by nNOS and a distinguishable effect of Hsp90alpha on nNOSmu and nNOSalpha proteins.	NADP	38-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-105
33181440-10	2021	Together, these EPR spin trapping and NADPH oxidation kinetics results demonstrated noticeable Hsp90alpha-induced increases in superoxide production by nNOS and a distinguishable effect of Hsp90alpha on nNOSmu and nNOSalpha proteins.	Superoxides	127-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-105
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-91
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-91
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
33457406-4	2020	Under simulated hypoxic conditions, curcumin combined with Glu-GNPs can significantly improve the ROS level of MCF-7 and MDA-MB-231 mammospheres; reduce the expression of HIF-1alpha and HSP90, thereby inhibiting the tumor cells" own stress ability; promote the apoptosis of tumor stem cells; and enhance the sensitivity of radiotherapy.	Curcumin	36-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-91
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
33202406-2	2021	17-Allylamino-17-demethoxygeldanamycin (17-AAG) blocks ATP binding to heat shock protein 90 (Hsp90), resulting in destabilization of Hsp90-client protein complexes.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
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
33457406-4	2020	Under simulated hypoxic conditions, curcumin combined with Glu-GNPs can significantly improve the ROS level of MCF-7 and MDA-MB-231 mammospheres; reduce the expression of HIF-1alpha and HSP90, thereby inhibiting the tumor cells" own stress ability; promote the apoptosis of tumor stem cells; and enhance the sensitivity of radiotherapy.	Glutamic Acid	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
33390934-4	2020	SNX-2112 is an Hsp90 inhibitor.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
33317068-0	2020	Structural Basis for Design of New Purine-Based Inhibitors Targeting the Hydrophobic Binding Pocket of Hsp90.	purine	35-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
33317068-2	2020	BIIB021 is a highly potent Hsp90 inhibitor with remarkable anticancer activity; however, its clinical application is limited by lack of potency and response.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
33317068-3	2020	In this study, we aimed to investigate the impact of replacing the hydrophobic moiety of BIIB021, 4-methoxy-3,5-dimethylpyridine, with various five-membered ring structures on the binding to Hsp90.	4-Methoxy-3,5-dimethylpyridine	98-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
33317068-4	2020	A focused array of N7/N9-substituted purines, featuring aromatic and non-aromatic rings, was designed, considering the size of hydrophobic pocket B in Hsp90 to obtain insights into their binding modes within the ATP binding site of Hsp90 in terms of pi-pi stacking interactions in pocket B as well as outer alpha-helix 4 configurations.	Purines	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
33317068-4	2020	A focused array of N7/N9-substituted purines, featuring aromatic and non-aromatic rings, was designed, considering the size of hydrophobic pocket B in Hsp90 to obtain insights into their binding modes within the ATP binding site of Hsp90 in terms of pi-pi stacking interactions in pocket B as well as outer alpha-helix 4 configurations.	Purines	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
33317068-4	2020	A focused array of N7/N9-substituted purines, featuring aromatic and non-aromatic rings, was designed, considering the size of hydrophobic pocket B in Hsp90 to obtain insights into their binding modes within the ATP binding site of Hsp90 in terms of pi-pi stacking interactions in pocket B as well as outer alpha-helix 4 configurations.	Adenosine Triphosphate	212-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
33317068-6	2020	Among the tested compounds, the isoxazole derivatives 6b and 6c, and the sole six-membered derivative 14 showed favorable Hsp90alpha inhibitory activity, with IC50 values of 1.76 microM, 0.203 microM, and 1.00 microM, respectively.	Isoxazoles	32-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-132
32949584-0	2020	Fungal Mycotoxin Penisuloxazin A, A Novel C-terminal Hsp90 Inhibitor and Characteristics of Its Analogues on Hsp90 Function Related to Binding Sites.	penisuloxazin a	17-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
32949584-0	2020	Fungal Mycotoxin Penisuloxazin A, A Novel C-terminal Hsp90 Inhibitor and Characteristics of Its Analogues on Hsp90 Function Related to Binding Sites.	penisuloxazin a	17-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
32949584-4	2020	PNSA bound to cysteine residues C572/C598 of CT-Hsp90 with disulfide bonds and inhibits Hsp90 activity, resulting in apoptosis and growth inhibition of HCT116 cells in vitro and in vivo.	Cysteine	14-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
32949584-4	2020	PNSA bound to cysteine residues C572/C598 of CT-Hsp90 with disulfide bonds and inhibits Hsp90 activity, resulting in apoptosis and growth inhibition of HCT116 cells in vitro and in vivo.	Disulfides	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
33179566-5	2020	First, an Hsp90 inhibitor, 17-AAG, significantly suppressed MERS-CoV propagation in cell lines and physiological-relevant human intestinal organoids.	tanespimycin	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
33369029-9	2020	Compared with the other three HDAC inhibitors, chidamide had minimal cytotoxicity in vitro at clinically relevant concentrations and showed mechanistically superior effects on non-histone proteins, including HSP90, NF-kappaB and AP-1.	N-(2-amino-5-fluorobenzyl)-4-(N-(pyridine-3-acrylyl)aminomethyl)benzamide	47-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-213
33040396-3	2020	Co-chaperones influence Hsp90"s activity in different ways, among which the Hsp organizing protein (Hop) was found to inhibit its ATP hydrolysis upon binding.	Adenosine Triphosphate	130-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
33238553-2	2020	These adenosine triphosphate dependent chaperones were classified based on their molecular mass that ranges between 10-100 kDA, including; HSP10, HSP40, HSP70, HSP90, HSPB1, HSPD, and HSPH1 family.	Adenosine	6-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
33150887-1	2020	An intelligent nitric oxide gas-releasing nanoplatform based on CuS-nanoplates has been designed to overcome the heat endurance of tumor cells by the inhibition of HSP90 expression with the released NO gas in mitochondria and thereby realize enhanced PTT under mild temperature conditions.	Nitric Oxide	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
33094816-2	2020	Our previous research has demonstrated that USP19 up-regulates the protein level and aggregation of polyQ-expanded huntingtin through the involvement of heat shock protein 90 (HSP90).	polyglutamine	100-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-174
33094816-2	2020	Our previous research has demonstrated that USP19 up-regulates the protein level and aggregation of polyQ-expanded huntingtin through the involvement of heat shock protein 90 (HSP90).	polyglutamine	100-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
33094816-6	2020	A</protein-id> mechanism of auto-inhibition of USP19 and activation by HSP90 is proposed, on which USP19 modulates the protein level of polyQ-expanded huntingtin in cells.	polyglutamine	136-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
33167494-6	2020	Preincubation with HSP90i or HDACi 48h prior to cisplatin enhanced the cisplatin potency significantly in all cell lines via apoptosis induction and affected the expression of apoptosis-relevant genes and proteins.	Cisplatin	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
33167494-6	2020	Preincubation with HSP90i or HDACi 48h prior to cisplatin enhanced the cisplatin potency significantly in all cell lines via apoptosis induction and affected the expression of apoptosis-relevant genes and proteins.	Cisplatin	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
32585150-1	2020	17-N-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) is an inhibitor of heat shock protein 90 (Hsp90), which has been studied in the treatment of cancer such as leukemia or solid tumors.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32585150-1	2020	17-N-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) is an inhibitor of heat shock protein 90 (Hsp90), which has been studied in the treatment of cancer such as leukemia or solid tumors.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32585150-1	2020	17-N-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) is an inhibitor of heat shock protein 90 (Hsp90), which has been studied in the treatment of cancer such as leukemia or solid tumors.	tanespimycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32585150-1	2020	17-N-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) is an inhibitor of heat shock protein 90 (Hsp90), which has been studied in the treatment of cancer such as leukemia or solid tumors.	tanespimycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
33109551-0	2020	Heat Shock Protein 90 Inhibitors AUY922, BIIB021 and SNX5422 Induce Bim-mediated Death of Thyroid Carcinoma Cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33109551-0	2020	Heat Shock Protein 90 Inhibitors AUY922, BIIB021 and SNX5422 Induce Bim-mediated Death of Thyroid Carcinoma Cells.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	41-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33109551-0	2020	Heat Shock Protein 90 Inhibitors AUY922, BIIB021 and SNX5422 Induce Bim-mediated Death of Thyroid Carcinoma Cells.	SNX-5422	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
33022580-2	2020	Inhibition of Hsp90 by Hsp90 inhibitor, geldanamycin (GA) significantly suppresses BmNPV proliferation in Bombyx mori, while the functional mechanism is not clear.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
33022580-2	2020	Inhibition of Hsp90 by Hsp90 inhibitor, geldanamycin (GA) significantly suppresses BmNPV proliferation in Bombyx mori, while the functional mechanism is not clear.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
33022580-2	2020	Inhibition of Hsp90 by Hsp90 inhibitor, geldanamycin (GA) significantly suppresses BmNPV proliferation in Bombyx mori, while the functional mechanism is not clear.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
32497199-4	2020	In the present study we screened 155 chemicals from a microbial natural product library and found Geldanamycin, an HSP90 inhibitor, profoundly rescued THP-1 cells from pyroptosis induced by LPS plus Nigericin treatment.	geldanamycin	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
32497199-5	2020	Consistently, other HSP90 inhibitors, including Radicicol, 17-DMAG and 17-AAG, all ameliorated pyroptosis in THP-1 cells by suppressing the inflammasome/Caspase-1/GSDMD signal pathway in pyroptosis.	monorden	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32497199-5	2020	Consistently, other HSP90 inhibitors, including Radicicol, 17-DMAG and 17-AAG, all ameliorated pyroptosis in THP-1 cells by suppressing the inflammasome/Caspase-1/GSDMD signal pathway in pyroptosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	59-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32497199-5	2020	Consistently, other HSP90 inhibitors, including Radicicol, 17-DMAG and 17-AAG, all ameliorated pyroptosis in THP-1 cells by suppressing the inflammasome/Caspase-1/GSDMD signal pathway in pyroptosis.	tanespimycin	71-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32868290-0	2020	Geldanamycin-Derived HSP90 Inhibitors Are Synthetic Lethal with NRF2.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
32868290-6	2020	Mechanistically, we show that products of NRF2 target genes metabolize the quinone-containing geldanamycin compounds into more potent HSP90 inhibitors, which enhances their cytotoxicity while simultaneously restricting the synthetic lethal effect to cells with aberrant NRF2 activity.	quinone	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
32868290-6	2020	Mechanistically, we show that products of NRF2 target genes metabolize the quinone-containing geldanamycin compounds into more potent HSP90 inhibitors, which enhances their cytotoxicity while simultaneously restricting the synthetic lethal effect to cells with aberrant NRF2 activity.	geldanamycin	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
32544514-0	2020	Direct targeting of HSP90 with daurisoline destabilizes beta-catenin to suppress lung cancer tumorigenesis.	daurisoline	31-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32942617-0	2020	HSP90 Inhibitor, 17-DMAG, Alone and in Combination with Lapatinib Attenuates Acquired Lapatinib-Resistance in ER-positive, HER2-Overexpressing Breast Cancer Cell Line.	Lapatinib	86-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32942617-6	2020	Analysis of the protein interaction network in two resistant cell lines with different lapatinib resistance mechanisms showed that HSP90 protein was commonly increased.	Lapatinib	87-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
32942617-9	2020	These results suggest that HSP90 inhibitors in patients with lapatinib-resistant Estrogen Receptor (ER) (+) HER2 (+) breast cancer are promising therapeutics for future clinical trials.	Lapatinib	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
32327714-9	2020	ML364 potentiates the pro-degradation effects of HSP90 inhibitors on ErbB2 and hence sensitizes ErbB2-positive breast cancer cells to HSP90 inhibition.	ML364	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
32327714-9	2020	ML364 potentiates the pro-degradation effects of HSP90 inhibitors on ErbB2 and hence sensitizes ErbB2-positive breast cancer cells to HSP90 inhibition.	ML364	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
32327714-9	2020	ML364 potentiates the pro-degradation effects of HSP90 inhibitors on ErbB2 and hence sensitizes ErbB2-positive breast cancer cells to HSP90 inhibition.	Proline	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
32505743-5	2020	We also determined whether genetic disruption of HSP90 protein quality control pathway genes implicated in human BA altered biliatresone toxicity in zebrafish and human cholangiocytes.	biliatresone	124-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
32505743-8	2020	Disruption of human BA-implicated HSP90 pathway genes sensitized zebrafish and human cholangiocytes to biliatresone-induced injury independent of glutathione.	biliatresone	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
32672902-0	2020	Hsp90 inhibition and co-incubation with pertuzumab induce internalization and degradation of trastuzumab: Implications for use of T-DM1.	t-dm1	130-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32585246-12	2020	Moreover, Hsp90 inhibition by gedunin did not cause upregulation of Hsp70 expression.	gedunin	30-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
32585246-13	2020	SIGNIFICANCE: Gedunin induces apoptosis in lung cancer cells by disrupting Hsp90:Beclin-1:Bcl-2 interaction and autophagy downregulation, thus making gedunin a good drug lead for targeting lung cancer.	gedunin	14-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
32738790-5	2020	We identified a mode of dynamic regulatory control over NOX5 activity through modulation of its heme saturation and oligomeric state by intracellular heme levels and Hsp90 binding.	Heme	96-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
32785323-5	2020	Then, gambogic acid, a natural inhibitor of Hsp90, was efficiently loaded onto the BZ nanomaterial via physical mixing.	gambogic acid	6-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
32785323-5	2020	Then, gambogic acid, a natural inhibitor of Hsp90, was efficiently loaded onto the BZ nanomaterial via physical mixing.	3-quinuclidinyl 4-fluoromethylbenzilate	83-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
32785323-10	2020	The BZ nanomaterial loaded with GA caused tumor shrinkage as well as disappearance and effectively downregulated Hsp90 expression in tumors in vivo.	3-quinuclidinyl 4-fluoromethylbenzilate	4-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
32785323-10	2020	The BZ nanomaterial loaded with GA caused tumor shrinkage as well as disappearance and effectively downregulated Hsp90 expression in tumors in vivo.	Gallium	32-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
32631523-4	2020	Our strategy is based on the preparation of paramagnetic analogs of KU-596, an investigational new drug that is currently undergoing clinical trials for the treatment of neuropathy and interacts with the Hsp90 C-terminal domain.	KU-596	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
32631523-5	2020	In particular, we report the design and synthesis of three novel paramagnetic analogs of KU-596, which will be used to obtain long range distances for NMR structural studies of Hsp90 in complex with C-terminal ligands.	KU-596	89-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
32776519-6	2020	In addition, Apigenin specifically inhibited the activation of RIG-I signaling via promoting the ubiquitin-mediated degradation of RIG-I, which may cause by the disrupting its interaction with Hsp90alpha.	Apigenin	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-203
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Adenosine Triphosphate	349-352	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Adenosine Triphosphate	349-352	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Reactive Oxygen Species	414-437	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Reactive Oxygen Species	414-437	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Reactive Oxygen Species	439-442	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Reactive Oxygen Species	439-442	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Reactive Oxygen Species	460-463	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Reactive Oxygen Species	460-463	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Malondialdehyde	468-483	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
32850811-6	2020	Furthermore, we found that elevated expression of HSP90 was involved in compression-induced NPSCs death, and inhibiting HSP90 could dramatically attenuate compression-induced necroptosis of NPSCs via regulating the expression and activity of RIPK1/RIPK3/MLKL, and alleviating the mitochondrial dysfunction (mitochondrial membrane potential loss and ATP depletion) and oxidative stress [production of mitochondrial reactive oxygen species (ROS), cellular total ROS and malondialdehyde, and downregulation of superoxide dismutase 2].	Malondialdehyde	468-483	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
32167602-2	2020	Heat shock protein-90 (Hsp90), a multidomain ATP driven molecular machine, is a prime representative of this family of proteins.	Adenosine Triphosphate	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
32167602-2	2020	Heat shock protein-90 (Hsp90), a multidomain ATP driven molecular machine, is a prime representative of this family of proteins.	Adenosine Triphosphate	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
32343987-0	2020	Hsp90 facilitates acquired drug resistance of tumor cells through cholesterol modulation however independent of tumor progression.	Cholesterol	66-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32343987-5	2020	The enrichment of P-gp and Hsp90 at the cholesterol-rich membrane microdomains is found obligatory for enhanced drug efflux activity.	Cholesterol	40-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
32343987-6	2020	Since inhibition of cholesterol biosynthesis is not interfering with the drug efflux activity, it is presumed that the net cholesterol redistribution mediated by Hsp90 regulates the enhanced drug efflux activity.	Cholesterol	123-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
32343987-7	2020	Our in vitro cholesterol and Hsp90 interaction studies have furthered our presumption that Hsp90 facilitates cholesterol redistribution.	Cholesterol	13-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
32343987-7	2020	Our in vitro cholesterol and Hsp90 interaction studies have furthered our presumption that Hsp90 facilitates cholesterol redistribution.	Cholesterol	109-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
32343987-7	2020	Our in vitro cholesterol and Hsp90 interaction studies have furthered our presumption that Hsp90 facilitates cholesterol redistribution.	Cholesterol	109-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
32540783-0	2020	Synthetic approaches, anticancer potential, HSP90 inhibition, multitarget evaluation, molecular modeling and apoptosis mechanistic study of thioquinazolinone skeleton: Promising antibreast cancer agent.	thioquinazolinone	140-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
32540783-1	2020	New series of compounds bearing 2-thioquinazolinone scaffold were designed, synthesized as HSP90 inhibitors.	2-thioquinazolinone	32-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
31452440-2	2020	Here, pyrazolopyranopyrimidine derivatives were characterized as new Hsp90 inhibitors.	pyrazolopyranopyrimidine	6-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
31452440-5	2020	The inhibition of Hsp90 ATPase activity of synthesized compounds revealed that para methylphenyl derivative of pyrazolopyranopyrimidine (HM3) was the most potent inhibitor (IC50 = 5.5 microM).	pyrazolopyranopyrimidine	111-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
32751221-8	2020	In addition, the gene expressions of HSP70 and HSP90 as cellular stress markers treated with cellulose, L-MFC, and lignin were quantified using real-time polymerase chain reaction (PCR) and Western blotting.	Cellulose	93-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
32751221-8	2020	In addition, the gene expressions of HSP70 and HSP90 as cellular stress markers treated with cellulose, L-MFC, and lignin were quantified using real-time polymerase chain reaction (PCR) and Western blotting.	l-mfc	104-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
32751221-8	2020	In addition, the gene expressions of HSP70 and HSP90 as cellular stress markers treated with cellulose, L-MFC, and lignin were quantified using real-time polymerase chain reaction (PCR) and Western blotting.	Lignin	115-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
32751221-11	2020	Interestingly, the lignin contained in L-MFC influenced the cell viability and the gene expression of HSP70 and HSP90 less than the same amount of lignin alone.	Lignin	19-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
32694502-0	2020	Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.	Lysine	32-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
31560394-7	2020	These disruptive effects of Hsp90 depletion could be rescued by the expression of exogenous MAP 4 or the treatment of trichostatin A that increases microtubule acetylation as well as stability.	trichostatin A	118-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
32371396-6	2020	We also observed that this interaction with 14-3-3 occludes the TOMM34 interaction interface with ATP-bound HSP70 dimers, which leaves them intact and thereby eliminates an inhibitory effect of TOMM34 on HSP70-mediated refolding in vitro In contrast, we noted that TOMM34 in complex with 14-3-3 could bind HSP90.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	306-311
32222543-7	2020	The increase in enzymatic activity with celastrol correlated with an increase in the transcriptional and proteome levels of the heat shock proteins Hsp90 and Hsp70.	celastrol	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
32222543-8	2020	The use of specific Hsp70 or Hsp90 inhibitors showed the positive effect of celastrol on PMM2 stability and activity to occur through Hsp90-driven modulation of the proteostasis network.	celastrol	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
32222543-8	2020	The use of specific Hsp70 or Hsp90 inhibitors showed the positive effect of celastrol on PMM2 stability and activity to occur through Hsp90-driven modulation of the proteostasis network.	celastrol	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
32638319-8	2020	Quercetin effectively suppressed the expression of Hsp27, Hsp70 and Hsp90.	Quercetin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
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
32608202-1	2020	PURPOSE: The current study aimed to investigate the synergistic antitumor effect of combined treatment with 17-DMAG (HSP90 inhibitor) and NVP-BEZ235 (PI3K/mTOR dual inhibitor) on cisplatin-resistant human bladder cancer cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	108-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
32608202-1	2020	PURPOSE: The current study aimed to investigate the synergistic antitumor effect of combined treatment with 17-DMAG (HSP90 inhibitor) and NVP-BEZ235 (PI3K/mTOR dual inhibitor) on cisplatin-resistant human bladder cancer cells.	Cisplatin	179-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
32608202-11	2020	CONCLUSION: HSP90 inhibitor monotherapy and in combination with the PI3K/mTOR survival pathway inhibitor NVP-BEZ235 shows a synergistic antitumor effect in cisplatin-resistant bladder cancers, eliciting cell cycle arrest at the G1 phase and induction of caspase-dependent apoptotic pathway.	dactolisib	109-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
32608202-11	2020	CONCLUSION: HSP90 inhibitor monotherapy and in combination with the PI3K/mTOR survival pathway inhibitor NVP-BEZ235 shows a synergistic antitumor effect in cisplatin-resistant bladder cancers, eliciting cell cycle arrest at the G1 phase and induction of caspase-dependent apoptotic pathway.	Cisplatin	156-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
32305165-2	2020	Among the synthesized surrogates of isoxazole and pyrazole, compounds 4a, 5e and 12b exhibited potent Hsp90 inhibition in ATPase activity and Her2 degradation assays and significant antitumor activity in A2780 and HCT116 cell lines.	Isoxazoles	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
32305165-2	2020	Among the synthesized surrogates of isoxazole and pyrazole, compounds 4a, 5e and 12b exhibited potent Hsp90 inhibition in ATPase activity and Her2 degradation assays and significant antitumor activity in A2780 and HCT116 cell lines.	pyrazole	50-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
32641992-7	2020	The GOx-mediated tumor starvation strategy would directly suppress the expression of HSP70 and HSP90, resulting in an enhanced low-temperature PTT induced by PDA nanocore.	Bialaphos	143-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
32503118-2	2020	Earlier, we demonstrated that plasma membrane-associated heparan sulfate proteoglycans (HSPGs) bind the extracellular Hsp90 and thereby promote the Hsp90-mediated motility of tumor cells.	Heparitin Sulfate	57-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
32503118-3	2020	Here, we showed that a conjugate of 2,5-dihydroxybenzoic acid with gelatin (2,5-DHBA-gelatin), a synthetic polymer with heparin-like properties, suppressed the basal (unstimulated) migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells, which was accompanied by the detachment of a fraction of Hsp90 from cell surface HSPGs.	2,5-dihydroxybenzoic acid	36-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	320-325
32503118-3	2020	Here, we showed that a conjugate of 2,5-dihydroxybenzoic acid with gelatin (2,5-DHBA-gelatin), a synthetic polymer with heparin-like properties, suppressed the basal (unstimulated) migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells, which was accompanied by the detachment of a fraction of Hsp90 from cell surface HSPGs.	2,5-dihydroxybenzoic acid	76-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	320-325
32503118-3	2020	Here, we showed that a conjugate of 2,5-dihydroxybenzoic acid with gelatin (2,5-DHBA-gelatin), a synthetic polymer with heparin-like properties, suppressed the basal (unstimulated) migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells, which was accompanied by the detachment of a fraction of Hsp90 from cell surface HSPGs.	Polymers	107-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	320-325
32503118-3	2020	Here, we showed that a conjugate of 2,5-dihydroxybenzoic acid with gelatin (2,5-DHBA-gelatin), a synthetic polymer with heparin-like properties, suppressed the basal (unstimulated) migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells, which was accompanied by the detachment of a fraction of Hsp90 from cell surface HSPGs.	Heparin	120-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	320-325
32503118-6	2020	The results demonstrate a potential of the 2,5-DHBA-gelatin polymer for the development of antimetastatic drugs targeting cell motility and a possible role of extracellular Hsp90 in the suppression of the migration and invasion of tumor cells mediated by the 2,5-DHBA-gelatin conjugate and heparin.	2,5-dihydroxybenzoic acid	259-267	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
31773452-0	2020	Long-term treatment with arsenite activates HER1 and HER2 through upregulating EGF, TGFalpha, and HSP90 in a human uroepithelial cell line.	Arsenites	25-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
33144925-9	2020	HSP90-enriched MEV-induced TAM polarization to an M2 phenotype, a transition known to support cancer progression, whereas the triple chaperone depletion attenuated this effect.	tam	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32297735-16	2020	In addition, TQ-ligation has been applied in the discovery of heat shock protein 90 (HSP90) as one of the functional target proteins for kongensin A.	kongensin A	137-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
32297735-16	2020	In addition, TQ-ligation has been applied in the discovery of heat shock protein 90 (HSP90) as one of the functional target proteins for kongensin A.	kongensin A	137-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
32297735-17	2020	We also confirmed that kongensin A covalently attaches to Cys420 within HSP90 and demonstrated that kongensin A blocks the interaction between HSP90 and CDC37 and subsequently inhibits necroptosis.	kongensin A	23-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
32297735-17	2020	We also confirmed that kongensin A covalently attaches to Cys420 within HSP90 and demonstrated that kongensin A blocks the interaction between HSP90 and CDC37 and subsequently inhibits necroptosis.	kongensin A	23-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
32297735-17	2020	We also confirmed that kongensin A covalently attaches to Cys420 within HSP90 and demonstrated that kongensin A blocks the interaction between HSP90 and CDC37 and subsequently inhibits necroptosis.	kongensin A	100-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
32397330-4	2020	The objective of the first part of this study is to investigate the putative Hsp90 inhibition activity of three novel previously synthesized quinazolines, which showed HL60 cytotoxicity and VEGFR2 and EGFR kinases inhibition activities.	Quinazolines	141-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
32397330-8	2020	Furthermore, the inhibiting effect of the Hsp90alpha gene by the combination of HAA2020 and dinaciclib was associated with increased caspase-7 and TNF-alpha, leading to apoptosis in HL60 cells.	dinaciclib	92-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-52
32397330-10	2020	The actions of HAA2020 propagated the apoptotic and cell cycle control properties of dinaciclib, showing the importance of co-targeting Hsp90 and CDK, which could lead to the better management of leukemia.	dinaciclib	85-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
32081977-0	2020	Author Correction: Targeting Hsp90 with FS-108 circumvents gefitinib resistance in EGFR mutant non-small cell lung cancer cells.	Gefitinib	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
31877402-8	2020	We also compare and contrast structural stability of three drugs namely: ezetimibe, pitavastatin and vilazodon in the Hsp90 protein.	ezetimibe	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
31877402-8	2020	We also compare and contrast structural stability of three drugs namely: ezetimibe, pitavastatin and vilazodon in the Hsp90 protein.	pitavastatin	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
32022992-7	2020	Thromboxane synthesis was impaired after exposure to inhibitors of Hsp40, Hsp90 and Grp94, but not after inhibition of Hsp70.	Thromboxanes	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
32266902-3	2020	Owing to the favorable degradability of BP, the nanosystem exhibited accelerated the release of the HSP90 inhibitor tanespimycin (17-AAG) and an apparent promotion in the reactive oxygen species (ROS) yield of PCN as well as expedited the degradation of the PCN-laden BP nanoplatforms.	Phosphorus	40-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
32266902-3	2020	Owing to the favorable degradability of BP, the nanosystem exhibited accelerated the release of the HSP90 inhibitor tanespimycin (17-AAG) and an apparent promotion in the reactive oxygen species (ROS) yield of PCN as well as expedited the degradation of the PCN-laden BP nanoplatforms.	tanespimycin	116-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
32266902-3	2020	Owing to the favorable degradability of BP, the nanosystem exhibited accelerated the release of the HSP90 inhibitor tanespimycin (17-AAG) and an apparent promotion in the reactive oxygen species (ROS) yield of PCN as well as expedited the degradation of the PCN-laden BP nanoplatforms.	tanespimycin	130-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
32295059-4	2020	Radicicol (RD) and its derivative, resorcinylic isoxazole amine NVP-AUY922 (NVP), have shown promising pharmacodynamics against Hsp90 activity.	resorcinylic isoxazole amine	35-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
32246062-0	2020	The HSP90 inhibitor Onalespib exerts synergistic anti-cancer effects when combined with radiotherapy: an in vitro and in vivo approach.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
32246062-2	2020	The HSP90 inhibitor Onalespib initiates the degradation of oncoproteins, and might also act as a radiosensitizer.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31621968-7	2020	In addition, the expression of two antiapoptosis genes, BmNPV inhibitor of apoptosis protein1 (BmNPV-iap1) and Bmiap2, was greatly decreased in GA-treated cells, whereas their expression was significantly increased in hsp90-overexpressed silkworm larvae.	geldanamycin	144-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	218-223
32068404-3	2020	Here, we generated and characterized the Hsp90 inhibitor PU-H71, conjugated to the mitochondrial delivery vehicle triphenylphosphonium (TPP) with a C10 carbon spacer, named SMTIN-C10, to enable dual binding to orthosteric and allosteric sites.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
32068404-3	2020	Here, we generated and characterized the Hsp90 inhibitor PU-H71, conjugated to the mitochondrial delivery vehicle triphenylphosphonium (TPP) with a C10 carbon spacer, named SMTIN-C10, to enable dual binding to orthosteric and allosteric sites.	3-(bromopropyl)triphenylphosphonium	114-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
32068404-3	2020	Here, we generated and characterized the Hsp90 inhibitor PU-H71, conjugated to the mitochondrial delivery vehicle triphenylphosphonium (TPP) with a C10 carbon spacer, named SMTIN-C10, to enable dual binding to orthosteric and allosteric sites.	tpp	136-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
32068404-3	2020	Here, we generated and characterized the Hsp90 inhibitor PU-H71, conjugated to the mitochondrial delivery vehicle triphenylphosphonium (TPP) with a C10 carbon spacer, named SMTIN-C10, to enable dual binding to orthosteric and allosteric sites.	Carbon	152-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
32068404-3	2020	Here, we generated and characterized the Hsp90 inhibitor PU-H71, conjugated to the mitochondrial delivery vehicle triphenylphosphonium (TPP) with a C10 carbon spacer, named SMTIN-C10, to enable dual binding to orthosteric and allosteric sites.	smtin-c10	173-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
32017918-3	2020	Here, we have identified SEW04784 as a first-in-class inhibitor of the Aha1-stimulated Hsp90 ATPase activity without inhibiting basal Hsp90 ATPase.	SEW2871	25-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
32017918-4	2020	Nuclear magnetic resonance analysis reveals that SEW84 binds to the C-terminal domain of Aha1 to weaken its asymmetric binding to Hsp90.	Carbon	68-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
32219016-7	2020	The results of western blotting and qRT-PCR assay suggest that 40 nM of TPL up-regulates the level of Annexin A5 (6.34 +- 0.07 fold) and ATP syn thase (4.08 +- 0.08 fold) and down-regulates the level of beta-Tubulin (0.11 +- 0.12 fold) and HSP90 (0.21 +- 0.09 fold).	triptolide	72-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
32179743-1	2020	The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control the folding and activation of several client proteins in the eukaryotic cell.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
32179743-1	2020	The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control the folding and activation of several client proteins in the eukaryotic cell.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
32058238-0	2020	Isoindoline scaffold-based dual inhibitors of HDAC6 and HSP90 suppressing the growth of lung cancer in vitro and in vivo.	2-(3-hydroxypropyl)isoindoline-1,3-dione	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
31513387-0	2020	Design and synthesis of fungal-selective resorcylate aminopyrazole Hsp90 inhibitors.	3-aminopyrazole	53-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
31513387-4	2020	Building on our previously-reported derivitization of resorcylate natural products to produce fungal-selective compounds, we have developed a series of synthetic aminopyrazole-substituted resorcylates with broad, potent, and fungal-selective Hsp90 inhibitory activity.	3-aminopyrazole	162-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	242-247
31663736-2	2020	Clinical Hsp90 inhibitors bind to the ATP pocket in the N-terminal domain of Hsp90 and subsequently suppress the ATPase activity of Hsp90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
31663736-2	2020	Clinical Hsp90 inhibitors bind to the ATP pocket in the N-terminal domain of Hsp90 and subsequently suppress the ATPase activity of Hsp90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31663736-2	2020	Clinical Hsp90 inhibitors bind to the ATP pocket in the N-terminal domain of Hsp90 and subsequently suppress the ATPase activity of Hsp90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31663736-2	2020	Clinical Hsp90 inhibitors bind to the ATP pocket in the N-terminal domain of Hsp90 and subsequently suppress the ATPase activity of Hsp90.	Nitrogen	56-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
31663736-2	2020	Clinical Hsp90 inhibitors bind to the ATP pocket in the N-terminal domain of Hsp90 and subsequently suppress the ATPase activity of Hsp90.	Nitrogen	56-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31663736-2	2020	Clinical Hsp90 inhibitors bind to the ATP pocket in the N-terminal domain of Hsp90 and subsequently suppress the ATPase activity of Hsp90.	Nitrogen	56-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
32156008-4	2020	Our compound, named DHP1808, was found to suppress A375 cell proliferation through apoptosis induction by activating the Fas/FasL signaling pathway; it also induced cell-cycle arrest and inhibited the cell migration and invasion of A375 cells by interfering with Hsp90-EGFR interactions and downstream signaling pathways.	dhp1808	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	263-268
32156008-5	2020	Our results indicate that DHP1808 could be a promising lead compound for the Hsp90/PI3K dual inhibitor.	dhp1808	26-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
32139666-3	2020	In this study, we find that Cdc37, a key co-chaperone of Hsp90, is downregulated in relapsed MM patients, especially after BTZ treatment, suggesting a link between Cdc37 and BTZ resistance.	Bortezomib	123-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
32139666-3	2020	In this study, we find that Cdc37, a key co-chaperone of Hsp90, is downregulated in relapsed MM patients, especially after BTZ treatment, suggesting a link between Cdc37 and BTZ resistance.	Bortezomib	174-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
32139666-4	2020	Suppression of Cdc37 or inhibition of Cdc37/Hsp90 association induces plasma cell dedifferentiation, quiescence of MM cells, and BTZ resistance in MM.	Bortezomib	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
32139682-0	2020	A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.	Lysine	13-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
32139682-1	2020	Methylation of a conserved lysine in C-terminal domain of the molecular chaperone Hsp90 was shown previously to affect its in vivo function.	Lysine	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
32139682-4	2020	Our results demonstrate that this particular lysine serves as a switch point for the regulation of Hsp90 functions by influencing its conformational cycle, ATPase activity, co-chaperone regulation, and client activation of yeast and human Hsp90.	Lysine	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	239-244
32139682-5	2020	Incorporation of the methylated lysine via genetic code expansion specifically shows that upon modification, the conformational cycle of Hsp90 is altered.	Lysine	32-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
32139682-6	2020	Molecular dynamics simulations including the methylated lysine suggest specific conformational changes that are propagated through Hsp90.	Lysine	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
32139682-7	2020	Thus, methylation of the C-terminal lysine allows a precise allosteric tuning of Hsp90 activity via long distances.	Lysine	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
32037409-4	2020	NVP-AUY922 is a heat shock protein 90 (HSP90) inhibitor with preferential tumor selectivity that is conjugated to 4-hydroxy-1,8-naphthalimide as a tumor-targeting ligand.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
32037409-4	2020	NVP-AUY922 is a heat shock protein 90 (HSP90) inhibitor with preferential tumor selectivity that is conjugated to 4-hydroxy-1,8-naphthalimide as a tumor-targeting ligand.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
32037409-4	2020	NVP-AUY922 is a heat shock protein 90 (HSP90) inhibitor with preferential tumor selectivity that is conjugated to 4-hydroxy-1,8-naphthalimide as a tumor-targeting ligand.	Naphthalimides	114-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
32037409-4	2020	NVP-AUY922 is a heat shock protein 90 (HSP90) inhibitor with preferential tumor selectivity that is conjugated to 4-hydroxy-1,8-naphthalimide as a tumor-targeting ligand.	Naphthalimides	114-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
32058968-2	2020	Both the conformational events tuned by ATP/ADP and co-chaperones and the chaperoning cycle timing are required for Hsp90"s fully functional display.	Adenosine Diphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
32058968-4	2020	In this manuscript, non-covalent allosteric modulators (SOMCL-16-171 and SOMCL-16-175) targeting Hsp90alpha"s middle domain (Hsp90M) were developed for the first time.	11-amino-N-propylnoraporphine	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-107
32058968-7	2020	Meanwhile, the binding of SOMCL-16-171 and SOMCL-16-175 to Hsp90M was demonstrated to allosterically modulate the structure and function of Hsp90alpha"s N-terminal domain.	11-amino-N-propylnoraporphine	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-150
32058968-7	2020	Meanwhile, the binding of SOMCL-16-171 and SOMCL-16-175 to Hsp90M was demonstrated to allosterically modulate the structure and function of Hsp90alpha"s N-terminal domain.	Nitrogen	153-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-150
32009391-0	2020	Ligand Conformational Bias Drives Enantioselective Modification of a Surface-Exposed Lysine on Hsp90.	tyrosyl-lysine	85-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
32009391-3	2020	Here, we employ an alternative approach for increasing kinact of a lysine-targeted covalent Hsp90 inhibitor, independent of the reversible binding affinity (Ki) or the intrinsic electrophilicity.	tyrosyl-lysine	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
32009391-4	2020	Starting with a noncovalent ligand, we appended a chiral, conformationally constrained linker, which orients an arylsulfonyl fluoride to react rapidly and enantioselectively with Lys58 on the surface of Hsp90.	Fluorides	112-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
32009391-4	2020	Starting with a noncovalent ligand, we appended a chiral, conformationally constrained linker, which orients an arylsulfonyl fluoride to react rapidly and enantioselectively with Lys58 on the surface of Hsp90.	pentalysine	179-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
31928863-0	2020	New modification strategy of matrine as Hsp90 inhibitors based on its specific L conformation for cancer treatment.	matrine	29-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
31928863-1	2020	The similarity of spatial structure between radicicol and matrine urged us to perform conformation modification of matrine, followed by L-shaped matrine derivatives, 6, 12, 21a-h and 22a-h were originally designed, synthesized and evaluated for Hsp90N inhibitors as anticancer agents.	matrine	58-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	245-251
31928863-2	2020	TSA (Thermal Shift Assay) results indicated that 21e, 22a-c and 22e-g exhibited strong binding force against Hsp90N with DeltaTm  > 3, meanwhile, MTT assay also revealed these compounds displayed potent anticancer activity with IC50 values below 25 muM against HepG2, HeLa and MDA-MB-231 cells lines.	monooxyethylene trimethylolpropane tristearate	146-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-115
31928863-5	2020	These results originally provided targeted modification strategy for matrine derivatives to serve as Hsp90 inhibitors for cancer therapy.	matrine	69-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
32104190-8	2020	Among them, alpha-viniferin was predicted to target Bcl-2, caspase-3, 8, and 9, MAPK14, CDK2, HSP90AA1, and others, reflecting CML therapeutic strategies.	alpha-viniferin	12-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-102
32104190-9	2020	In vitro, experimental data showed a nonnecrotic growth limitation of K562 cells caused by alpha-viniferin was predicted to target Bcl-2, caspase-3, 8, and 9, MAPK14, CDK2, HSP90AA1, and others, reflecting CML therapeutic strategies.	alpha-viniferin	91-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-181
32104190-10	2020	mug mL-1 at 24 h. Finally, we validated the chemotherapeutic effect of alpha-viniferin was predicted to target Bcl-2, caspase-3, 8, and 9, MAPK14, CDK2, HSP90AA1, and others, reflecting CML therapeutic strategies.	alpha-viniferin	71-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-161
32104190-12	2020	This work also predicts and validates targets in the mitochondrial signaling pathway, providing a novel strategy for CML treatment.alpha-viniferin was predicted to target Bcl-2, caspase-3, 8, and 9, MAPK14, CDK2, HSP90AA1, and others, reflecting CML therapeutic strategies.	alpha-viniferin	131-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	213-221
31928763-9	2020	We quantify the impact of genetic variation in TBP and drug class variation targeting the ATP-binding region of Hsp90 on conserved dynamics.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
31928763-10	2020	We identify regions of conserved dynamics in Hsp90 that connect the ATP binding pocket to other functional regions.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
31928763-11	2020	We also demonstrate that dynamic impacts of various Hsp90 inhibitors rank accordingly with how closely they mimic natural ATP binding.	Adenosine Triphosphate	122-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
31659567-1	2020	HSP90 (heat shock protein 90) is an ATP-dependent molecular chaperone involved in a proper folding and maturation of hundreds of proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31659567-1	2020	HSP90 (heat shock protein 90) is an ATP-dependent molecular chaperone involved in a proper folding and maturation of hundreds of proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-28
31765670-0	2020	Novel PRMT5-mediated arginine methylations of HSP90A are essential for maintenance of HSP90A function in NDRG2low ATL and various cancer cells.	Arginine	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-52
31765670-0	2020	Novel PRMT5-mediated arginine methylations of HSP90A are essential for maintenance of HSP90A function in NDRG2low ATL and various cancer cells.	Arginine	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-92
31765670-5	2020	Since knockdown of PRMT5 expression or forced expression of HSP90A with alanine replacement of R345 or R386 induced apoptosis with the degradation of client proteins in NDRG2low ATL-related and other cancer cells, we here identified that the novel arginine methylations of HSP90A are essential for maintenance of its function in NDRG2low ATL and other cancer cells.	Alanine	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-66
31765670-5	2020	Since knockdown of PRMT5 expression or forced expression of HSP90A with alanine replacement of R345 or R386 induced apoptosis with the degradation of client proteins in NDRG2low ATL-related and other cancer cells, we here identified that the novel arginine methylations of HSP90A are essential for maintenance of its function in NDRG2low ATL and other cancer cells.	Arginine	248-256	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-66
31765670-5	2020	Since knockdown of PRMT5 expression or forced expression of HSP90A with alanine replacement of R345 or R386 induced apoptosis with the degradation of client proteins in NDRG2low ATL-related and other cancer cells, we here identified that the novel arginine methylations of HSP90A are essential for maintenance of its function in NDRG2low ATL and other cancer cells.	Arginine	248-256	heat shock protein 90 alpha family class A member 1	Homo sapiens	273-279
31903741-5	2020	Therefore, it was hypothesized that autophagy could be controlled to eliminate tumors by combining exogenous light with a selective HSP90 inhibitor, for example, SNX-2112.	SNX 2112	162-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
31979118-4	2020	FN bound to the M domain of HSP90 and interacted with both the open and closed HSP90 conformations; and the interaction was reduced in the presence of sodium molybdate.	sodium molybdate(VI)	151-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
31979118-6	2020	The highest affinity interaction was with the 30-kDa (heparin-binding) FN fragment, which also showed the greatest colocalization in cells and accommodated both HSP90 and heparin in the complex.	Heparin	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
31592648-4	2020	In this strategy, the binding activity of ligands of interest is evaluated by competitive inhibition of ligand-directed N-acyl-N-alkyl sulfonamide (LDNASA) chemistry-mediated Hsp90 labeling.	1-alkyl-2-acyl-sn-glycero-3-phosphocholine	120-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
31592648-6	2020	Our system is applicable to high-throughput ligand screening, and we discovered a new small molecule candidate that binds to the N-terminal ATP binding domain of Hsp90.	Nitrogen	129-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
31592648-6	2020	Our system is applicable to high-throughput ligand screening, and we discovered a new small molecule candidate that binds to the N-terminal ATP binding domain of Hsp90.	Adenosine Triphosphate	140-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
31960173-0	2020	Biodistribution and imaging of an hsp90 ligand labelled with 111In and 67Ga for imaging of cell death.	1,4,7-triazacyclononane-N,N',N''-triacetic acid	71-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
31960173-1	2020	BACKGROUND: 4-(N-(S-glutathionylacetyl)amino) phenylarsonous acid (GSAO) when conjugated at the gamma-glutamyl residue with fluorophores and radio-isotopes is able to image dead and dying cells in vitro and in vivo by binding to intracellular 90-kDa heat shock proteins (hsp90) when cell membrane integrity is compromised.	4-(N-(S-glutathionylacetyl)amino)phenylarsenoxide	12-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
31960173-1	2020	BACKGROUND: 4-(N-(S-glutathionylacetyl)amino) phenylarsonous acid (GSAO) when conjugated at the gamma-glutamyl residue with fluorophores and radio-isotopes is able to image dead and dying cells in vitro and in vivo by binding to intracellular 90-kDa heat shock proteins (hsp90) when cell membrane integrity is compromised.	phenylarsonous acid	46-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
31960173-1	2020	BACKGROUND: 4-(N-(S-glutathionylacetyl)amino) phenylarsonous acid (GSAO) when conjugated at the gamma-glutamyl residue with fluorophores and radio-isotopes is able to image dead and dying cells in vitro and in vivo by binding to intracellular 90-kDa heat shock proteins (hsp90) when cell membrane integrity is compromised.	4-(N-(S-glutathionylacetyl)amino)phenylarsenoxide	67-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
31963688-0	2020	Aspirin Enhances the Protection of Hsp90 from Heat-Stressed Injury in Cardiac Microvascular Endothelial Cells Through PI3K-Akt and PKM2 Pathways.	Aspirin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
31963688-9	2020	ASA treatment of CMVECs induced a significant expression of Hsp90, which promoted both Akt and PKM2 signals, which are beneficial for relieving HS damage and maintaining the function of CMVECs.	Aspirin	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
31963688-11	2020	To the best of our knowledge, this is the first study to show that HS damages CMVECs and the protection mechanism of Hsp90 on it, and that ASA provides a new potential strategy for regulating cardiac microcirculation preventing HS-induced heart failure.	Aspirin	139-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
31814332-2	2020	Herein, a biodegradable nanotheranostic agent based on hollow mesoporous organosilica nanoparticles (HMONs), followed by encapsulating of heat shock protein 90 (Hsp 90) inhibitor is described.	organosilica	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-159
31814332-2	2020	Herein, a biodegradable nanotheranostic agent based on hollow mesoporous organosilica nanoparticles (HMONs), followed by encapsulating of heat shock protein 90 (Hsp 90) inhibitor is described.	organosilica	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-167
32025156-1	2020	The heat shock protein Hsp90 is a molecular chaperon that uses ATP and interacts with various co-chaperone proteins, acting as adapters, in order to carry out the maturation of its target proteins.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
31785857-0	2020	Discovery of 5-aryl-3-thiophen-2-yl-1H-pyrazoles as a new class of Hsp90 inhibitors in hepatocellular carcinoma.	5-aryl-3-thiophen-2-yl-1h-pyrazoles	13-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
31560152-6	2020	The results indicate that 20 residues in group A of the hierarchical tree are responsible for major contributions, and van der Waals interactions as well as hydrogen bonding interactions between important residues in HSP90 and key regions of inhibitors are the main force for promoting inhibitor bindings.	Hydrogen	157-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	217-222
31793427-3	2020	Due to its ability to effect phosphorylation of numerous client proteins, inhibition of Hsp90 has been an attractive anticancer approach since the early 1990"s, when researchers identified a druggable target on the amino terminus of Hsp90 for a variety of cancers.	Amino Acids	215-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
31793427-3	2020	Due to its ability to effect phosphorylation of numerous client proteins, inhibition of Hsp90 has been an attractive anticancer approach since the early 1990"s, when researchers identified a druggable target on the amino terminus of Hsp90 for a variety of cancers.	Amino Acids	215-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	233-238
31793427-4	2020	Since then, 17 Hsp90 inhibitors that target the chaperone"s N-terminal domain, have entered clinical trials.	Nitrogen	60-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
31793427-6	2020	In these trials, a major limitation observed with Hsp90 inhibition at the N-terminal domain was dose-limiting toxicities and relatively poor pharmacokinetic profiles.	Nitrogen	74-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
31655430-0	2020	N-alkyl-hydroxybenzoyl anilide hydroxamates as dual inhibitors of HDAC and HSP90, downregulating IFN-gamma induced PD-L1 expression.	n-alkyl-hydroxybenzoyl anilide hydroxamates	0-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
31956271-5	2020	Inactivation of all Hsp90 paralogs induced mitochondrial dysfunction, increased cytosolic calcium, and activated calcineurin.	Calcium	90-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
31956271-7	2020	The purine scaffold derivative DN401 inhibited all Hsp90 paralogs simultaneously and showed stronger anticancer activity than other Hsp90 inhibitors.	Purines	4-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
31956271-7	2020	The purine scaffold derivative DN401 inhibited all Hsp90 paralogs simultaneously and showed stronger anticancer activity than other Hsp90 inhibitors.	Purines	4-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
31339073-0	2020	Study of interactions energies between residues of the active site of Hsp90 and the geldanamycin analogues using Quantum Mechanics/Molecular Mechanics (QM/MM) methods.	geldanamycin	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
31339073-2	2020	An inhibitor of Hsp90 chaperone activity is the geldanamycin, a thready compound that has the power to bind to the binding of ATP in the N-terminal of Hsp90 domain site, however this reported in clinical trials hepatotoxic damage, which I pitting to its disuse.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
31339073-2	2020	An inhibitor of Hsp90 chaperone activity is the geldanamycin, a thready compound that has the power to bind to the binding of ATP in the N-terminal of Hsp90 domain site, however this reported in clinical trials hepatotoxic damage, which I pitting to its disuse.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
31339073-2	2020	An inhibitor of Hsp90 chaperone activity is the geldanamycin, a thready compound that has the power to bind to the binding of ATP in the N-terminal of Hsp90 domain site, however this reported in clinical trials hepatotoxic damage, which I pitting to its disuse.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
31339073-2	2020	An inhibitor of Hsp90 chaperone activity is the geldanamycin, a thready compound that has the power to bind to the binding of ATP in the N-terminal of Hsp90 domain site, however this reported in clinical trials hepatotoxic damage, which I pitting to its disuse.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
31339073-3	2020	On the other hand, taking advantage that the geldanamycin joins successfully Hsp90, efforts have focused on the search for similar that they have the same or better effect and both exhibited lower effects than its predecessor, as it has been the case with the similar 17-AAG and 17-DMAG.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31339073-5	2020	RESULTS: To evaluate interaction energies found that the Lys58 is essential for the union of the analogs to the active site of Hsp90, and that the activity of these will depend on if these have on the C-11 position of the macrocycle a group of small and at the same time attractor of electrons, as it is reflected with the series C-11 hydroxy and methoxy C-11.	Carbon	201-202	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
31339073-5	2020	RESULTS: To evaluate interaction energies found that the Lys58 is essential for the union of the analogs to the active site of Hsp90, and that the activity of these will depend on if these have on the C-11 position of the macrocycle a group of small and at the same time attractor of electrons, as it is reflected with the series C-11 hydroxy and methoxy C-11.	Carbon	330-331	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
31469500-8	2020	Our results showed that the hypocotyl length of bes1-D mutants was highly reduced when HSP90 was challenged by the geldanamycin (GDA) inhibitor of the ATPase activity of HSP90.	geldanamycin	115-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
31469500-8	2020	Our results showed that the hypocotyl length of bes1-D mutants was highly reduced when HSP90 was challenged by the geldanamycin (GDA) inhibitor of the ATPase activity of HSP90.	geldanamycin	115-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
31469500-8	2020	Our results showed that the hypocotyl length of bes1-D mutants was highly reduced when HSP90 was challenged by the geldanamycin (GDA) inhibitor of the ATPase activity of HSP90.	geldanamycin	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
31469500-8	2020	Our results showed that the hypocotyl length of bes1-D mutants was highly reduced when HSP90 was challenged by the geldanamycin (GDA) inhibitor of the ATPase activity of HSP90.	geldanamycin	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
31726100-5	2020	Based on our previous finding that a humanized monoclonal antibody against ROR1 increases the activity of Ibrutinib against CLL, which is currently undergoing evaluation in clinical trials for the treatment of B-cell lymphoid malignancies, we then provided evidence that treatment with HSP90 inhibitor (17-DMAG) enhances anti-CLL activity of Ibrutinib in vitro and in vivo, by down-modulating ROR1.	ibrutinib	106-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	286-291
31726100-7	2020	However, immunoblotting validation confirmed that Ibrutinib treatment dramatically deprived HSP90 inhibitors, 17-DMAG, AUY922 or PU-H71, of inducing the degradation of BTK, BLK, LCK or LYN, but not ROR1.	ibrutinib	50-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
31726100-7	2020	However, immunoblotting validation confirmed that Ibrutinib treatment dramatically deprived HSP90 inhibitors, 17-DMAG, AUY922 or PU-H71, of inducing the degradation of BTK, BLK, LCK or LYN, but not ROR1.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	110-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
31726100-8	2020	Collectively, our data suggested that depletion of ROR1 induced by targeting HSP90 might facilitate the enhancement of Ibrutinib activity against CLL.	ibrutinib	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
33270690-9	2020	At static conditions, both HSP70 and HSP90 families in CTEPH-EC are decreased.	cteph-ec	55-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
33077554-6	2020	Based on this evidence, we engineered a "chimeric" nano-therapeutic tool comprising taxanes and a cholesterol-tethered Hsp90 inhibitor, radicicol, which targets the tumor, reduces tolerance, and optimally re-primes NK cells via prolonged induction of NK-activating ligand receptors via temporal control of drug release in vitro and in vivo.	Cholesterol	98-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
33077554-6	2020	Based on this evidence, we engineered a "chimeric" nano-therapeutic tool comprising taxanes and a cholesterol-tethered Hsp90 inhibitor, radicicol, which targets the tumor, reduces tolerance, and optimally re-primes NK cells via prolonged induction of NK-activating ligand receptors via temporal control of drug release in vitro and in vivo.	monorden	136-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
33095286-0	2020	Phase 1 study of the HSP90 inhibitor onalespib in combination with AT7519, a pan-CDK inhibitor, in patients with advanced solid tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
33095286-1	2020	PURPOSE: We conducted a phase 1 trial of the HSP90 inhibitor onalespib in combination with the CDK inhibitor AT7519, in patients with advanced solid tumors to determine the safety profile and maximally tolerated dose, pharmacokinetics, preliminary antitumor activity, and to assess the pharmacodynamic (PD) effects on HSP70 expression in patient-derived PBMCs and plasma.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
32934719-3	2020	This novel class of synthetic compounds containing the isoxazole nucleus exhibited potent and selective inhibition of HSP90 in previous studies.	Isoxazoles	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
33204396-14	2020	We found seven putative genes predicted to be modulated by Rsv in the context of Doxo treatment: CCND1, CDH1, ESR1, HSP90AA1, MAPK3, PTPN11, and RPS6KB1.	Resveratrol	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-124
33204396-14	2020	We found seven putative genes predicted to be modulated by Rsv in the context of Doxo treatment: CCND1, CDH1, ESR1, HSP90AA1, MAPK3, PTPN11, and RPS6KB1.	Doxorubicin	81-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-124
33095103-7	2022	The Glide-score and Prime-MM-GBSA based binding free energy of DCZ3112, standard Hsp90-Cdc37 inhibitor were found to be -6.96 and -40.46 kcal/mol, respectively.	dcz3112	63-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
33038305-0	2020	ATP-Driven Nonequilibrium Activation of Kinase Clients by the Molecular Chaperone Hsp90.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
33038305-2	2020	Previous studies have established that the Hsp90 homodimer undergoes an ATP-driven cycle through open and closed conformations.	Adenosine Triphosphate	72-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
33038305-3	2020	Here, I propose a model of client activation by Hsp90 that predicts that this cycle enables Hsp90 to use ATP energy to drive a client out of thermodynamic equilibrium toward its active conformation.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
33038305-3	2020	Here, I propose a model of client activation by Hsp90 that predicts that this cycle enables Hsp90 to use ATP energy to drive a client out of thermodynamic equilibrium toward its active conformation.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
31917403-0	2020	Sildenafil triggers tumor lethality through altered expression of HSP90 and degradation of PKD2.	sildenafil	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
31917403-5	2020	Notably, incubation of cancer cells with Sildenafil was associated with altered expression of HSP90 chaperone followed by degradation of PKD2, a client protein previously reported to be involved in tumor growth.	sildenafil	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
31917403-6	2020	Furthermore, the involvement of low doses of PU-H71, an HSP90-inhibitor currently under clinical evaluation, in combination with low concentrations of Sildenafil, synergistically and negatively impacted on the viability of cancer cells in vivo.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
33053878-0	2020	Comparing Fragment Binding PosesPrediction Using HSP90 as a Key Study: When Bound Water Makes the Difference.	Water	82-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
33017561-7	2021	Additionally, geldanamycin, an HSP90AA1 inhibitor, reduced HMGB1 secretion.	geldanamycin	14-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-39
32544514-7	2020	Furthermore, our data from Drug Affinity Responsive Target Stability (DARTS), isothermal titration calorimetry (ITC) and a series of functional assays demonstrated that daurisoline could target HSP90 directly and disrupt its interaction with beta-catenin, therefore increasing the ubiquitin-mediated proteasomal degradation of beta-catenin.	daurisoline	169-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
32767829-6	2020	Moreover, targeting DRP1 not only reduces HSP90 expression but also enhances ROS-induced HSP90 cleavage, thus inhibiting activation of the MAPK and PI3K pathways and leading to suppressed lactate utilization and increased ROS-induced cell death.	Reactive Oxygen Species	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
32767829-6	2020	Moreover, targeting DRP1 not only reduces HSP90 expression but also enhances ROS-induced HSP90 cleavage, thus inhibiting activation of the MAPK and PI3K pathways and leading to suppressed lactate utilization and increased ROS-induced cell death.	Lactic Acid	188-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
32767829-6	2020	Moreover, targeting DRP1 not only reduces HSP90 expression but also enhances ROS-induced HSP90 cleavage, thus inhibiting activation of the MAPK and PI3K pathways and leading to suppressed lactate utilization and increased ROS-induced cell death.	Reactive Oxygen Species	222-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	Fluorouracil	46-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-264
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	Fluorouracil	46-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	266-271
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	Fluorouracil	62-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-264
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	Fluorouracil	62-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	266-271
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	Tegafur	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-264
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	Tegafur	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	266-271
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides	170-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-264
32683166-3	2020	In this study, we utilized the core structure 5-fluorouracil (5-FU) or tegafur, a 5-FU prodrug combined through different linkers with resorcinol to generate a series of fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides which inhibit potent Heat Shock Protein 90 (HSP90).	fluoropyrimidin-2,4-dihydroxy-5-isopropylbenzamides	170-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	266-271
32683166-5	2020	Compound 12c, developed by molecular docking analysis and enzymatic assays exhibits promising inhibitory activity of HSP90.	12c	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
32683166-6	2020	This compound, 12c shows the most potent HSP90 inhibitory activity with an IC50 value of 27.8 +- 4.4 nM, superior to that of reference compounds AUY-922 (Luminespib) and BIIB021 whose IC50 values are 43.0 +- 0.9 nM and 56.8 +- 4.0 nM respectively.	12c	15-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
32683166-6	2020	This compound, 12c shows the most potent HSP90 inhibitory activity with an IC50 value of 27.8 +- 4.4 nM, superior to that of reference compounds AUY-922 (Luminespib) and BIIB021 whose IC50 values are 43.0 +- 0.9 nM and 56.8 +- 4.0 nM respectively.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	145-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
31898183-0	2020	A phase 2 clinical trial of the heat shock protein 90 (HSP 90) inhibitor ganetespib in patients with refractory advanced esophagogastric cancer.	STA 9090	73-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
31898183-0	2020	A phase 2 clinical trial of the heat shock protein 90 (HSP 90) inhibitor ganetespib in patients with refractory advanced esophagogastric cancer.	STA 9090	73-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-61
31898183-2	2020	Ganetespib which is a novel triazolone heterocyclic inhibitor of HSP90, is a potentially biologically rational treatment strategy for advanced EG cancers with these gene amplification.	5-((3-(((3,5-bis(trifluoromethyl)phenyl)methyl)oxy)-2-phenylpiperidino)methyl)-3-oxo-1,2,4-triazolone	28-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
32669400-2	2020	AUY922 (luminespib), a new generation HSP90 inhibitor, exhibits potent preclinical efficacy against several cancer types including prostate cancer (PCa).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
32812680-1	2020	Although Hsp90-family chaperones have been extensively targeted with ATP-competitive inhibitors, it is unknown whether high affinity is achieved from a few highly stabilizing contacts or from many weaker contacts within the ATP-binding pocket.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	Hydrogen	79-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-36
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	Hydrogen	79-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-139
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	Hydrogen	79-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	Aspartic Acid	111-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-36
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	Aspartic Acid	111-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-139
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	Aspartic Acid	111-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	CHEMBL391805	122-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-36
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	CHEMBL391805	122-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-139
32812680-2	2020	A large-scale analysis of Hsp90alpha:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90alpha) stands out as most universal among Hsp90 inhibitors.	CHEMBL391805	122-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
32812680-7	2020	The Hsp90 Asp93 Asn substitution has long been known to abolish nucleotide binding, yet puzzlingly, native sequences of structurally similar ATPases, such as Topoisomerasese II, have an asparagine at this same crucial site.	Asparagine	186-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
32812680-8	2020	While aspartate and asparagine sidechains can both act as hydrogen bond acceptors, we show that a steric clash prevents the Hsp90 Asp93 Asn sidechain from adopting the necessary rotamer, whereas this steric restriction is absent in Topoisomerasese II.	Aspartic Acid	6-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
32812680-8	2020	While aspartate and asparagine sidechains can both act as hydrogen bond acceptors, we show that a steric clash prevents the Hsp90 Asp93 Asn sidechain from adopting the necessary rotamer, whereas this steric restriction is absent in Topoisomerasese II.	Asparagine	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
32812680-8	2020	While aspartate and asparagine sidechains can both act as hydrogen bond acceptors, we show that a steric clash prevents the Hsp90 Asp93 Asn sidechain from adopting the necessary rotamer, whereas this steric restriction is absent in Topoisomerasese II.	Hydrogen	58-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
33102211-0	2020	Overcoming Limitations of Cisplatin Therapy by Additional Treatment With the HSP90 Inhibitor Onalespib.	Cisplatin	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
33102211-0	2020	Overcoming Limitations of Cisplatin Therapy by Additional Treatment With the HSP90 Inhibitor Onalespib.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	93-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
33102211-4	2020	Cisplatin resistance can be mediated by alterations to the DNA damage response, where multiple components of the repair machinery have been described to be client proteins of HSP90.	Cisplatin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
33102211-5	2020	In the present study, we have investigated whether therapy with the novel HSP90 inhibitor onalespib can potentiate the efficacy of cisplatin and potentially reverse cisplatin resistance in ovarian and head and neck cancer cells.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	90-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
33102211-5	2020	In the present study, we have investigated whether therapy with the novel HSP90 inhibitor onalespib can potentiate the efficacy of cisplatin and potentially reverse cisplatin resistance in ovarian and head and neck cancer cells.	Cisplatin	131-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
33102211-5	2020	In the present study, we have investigated whether therapy with the novel HSP90 inhibitor onalespib can potentiate the efficacy of cisplatin and potentially reverse cisplatin resistance in ovarian and head and neck cancer cells.	Cisplatin	165-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
33102211-7	2020	Western blotting was used to assess the downregulation of HSP90 client proteins and alterations in downstream signaling proteins after exposure to cisplatin and/or onalespib.	Cisplatin	147-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
33102211-7	2020	Western blotting was used to assess the downregulation of HSP90 client proteins and alterations in downstream signaling proteins after exposure to cisplatin and/or onalespib.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	164-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
33102211-15	2020	We speculate that the increased apoptotic signaling, DNA damage as well as the downregulation of HSP90 client proteins are important mechanisms promoting increased sensitivity to cisplatin treatment.	Cisplatin	179-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
32993709-0	2020	Curcumin derivative C212 inhibits Hsp90 and eliminates both growing and quiescent leukemia cells in deep dormancy.	Curcumin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
32993709-0	2020	Curcumin derivative C212 inhibits Hsp90 and eliminates both growing and quiescent leukemia cells in deep dormancy.	c212	20-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
32993709-8	2020	The mechanisms of C212-induced apoptosis and deep dormancy, particularly associated with its inhibition of Hsp90 activity, were studied using molecular docking, protein aggregation assay, and Western blot of client proteins.	c212	18-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
32994435-2	2020	Inhibition of Hsp90 by small-molecule drugs, acting via its ATP hydrolysis site, has shown promise as a molecularly targeted cancer therapy.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
32994435-6	2020	We have designed prototype TPR ligands that mimic key native "carboxylate clamp" interactions between Hsp90 and its TPR cochaperones and show that they block binding between Hop TPR2A and the Hsp90 C-terminal MEEVD peptide.	carboxylate	62-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
32994435-6	2020	We have designed prototype TPR ligands that mimic key native "carboxylate clamp" interactions between Hsp90 and its TPR cochaperones and show that they block binding between Hop TPR2A and the Hsp90 C-terminal MEEVD peptide.	carboxylate	62-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	192-197
32679196-3	2020	The Hsp90 molecular cycle involves ATP binding and hydrolysis, which drive conformational changes.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
32663707-2	2020	X-ray structures of analogs 22 and 24 reveals an unexpected arrangement of the ansa-bridge in solid (conformer B), that is located between those of conformers A, prevailing in solution (trans-lactam), and C, crucial at binding to Hsp90 (cis-lactam).	trans-lactam	186-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-235
32663707-2	2020	X-ray structures of analogs 22 and 24 reveals an unexpected arrangement of the ansa-bridge in solid (conformer B), that is located between those of conformers A, prevailing in solution (trans-lactam), and C, crucial at binding to Hsp90 (cis-lactam).	cis-lactam	237-247	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-235
32663707-3	2020	The structure of a new-type conformer B allows to better understand the molecular recognition mechanism between the GDM analogs and the target Hsp90.	geldanamycin	116-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
32768937-0	2020	Low dose HSP90 inhibition with AUY922 blunts rapid evolution of metastatic and drug resistant phenotypes induced by TGF-beta and paclitaxel in A549 cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	31-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
32768937-0	2020	Low dose HSP90 inhibition with AUY922 blunts rapid evolution of metastatic and drug resistant phenotypes induced by TGF-beta and paclitaxel in A549 cells.	Paclitaxel	129-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
32768937-6	2020	MATERIALS AND METHODS: We explored the role of HSP90 in the evolution of metastatic and drug resistant features in NSCLC by treating A549 cells with AUY922, a clinically relevant HSP90 inhibitor, and inducing metastatic and drug resistant phenotypes via treatment with TGF-beta and paclitaxel, respectively.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	149-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
32768937-11	2020	CONCLUSION: Together our data indicates that HSP90 inhibition with AUY922 can limit the acquisition of metastatic and drug resistant phenotypes in A549 cells at low, clinically appropriate doses.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
32738983-4	2020	A molecular docking study of 80 with the homology model of a HSP90 homodimer showed that 80 fit nicely in the C-terminal domain with a higher electrostatic complementary score than that of ATP.	Adenosine Triphosphate	189-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
32526554-0	2020	Corrigendum to"Isoindoline scaffold-based dual inhibitors of HDAC6 and HSP90 suppressing the growth of lung cancer in vitro and in vivo"[Eur.	2-(3-hydroxypropyl)isoindoline-1,3-dione	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
32573772-0	2020	Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.	Flavin Mononucleotide	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
32573772-0	2020	Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.	Heme	73-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
32573772-0	2020	Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.	Nitric Oxide	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
32255264-3	2020	Therefore, we hypothesize that the novel C-terminal HSP90 inhibitors KU711 and KU758 can target TIC and represent a promising strategy for overcoming metastasis.	ku711	69-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
32255264-3	2020	Therefore, we hypothesize that the novel C-terminal HSP90 inhibitors KU711 and KU758 can target TIC and represent a promising strategy for overcoming metastasis.	ku758	79-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
32255264-4	2020	Human breast cancer cells (MDA-MB-468LN, MDA-MB-231) treated with the HSP90 inhibitors KU711, KU758, and 17-AAG showed a 50-80% decrease in TIC markers CD44 and ALDH (p<0.01) as assessed by flow cytometry.	ku711	87-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
32255264-4	2020	Human breast cancer cells (MDA-MB-468LN, MDA-MB-231) treated with the HSP90 inhibitors KU711, KU758, and 17-AAG showed a 50-80% decrease in TIC markers CD44 and ALDH (p<0.01) as assessed by flow cytometry.	ku758	94-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
32255264-4	2020	Human breast cancer cells (MDA-MB-468LN, MDA-MB-231) treated with the HSP90 inhibitors KU711, KU758, and 17-AAG showed a 50-80% decrease in TIC markers CD44 and ALDH (p<0.01) as assessed by flow cytometry.	tanespimycin	105-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
32659088-12	2020	This finding suggests that under trial Hsp90 inhibitors MPC-3100 could be a potential starting point into the development of potential anti-cancer agents with the possibility of future directions for the improvement of early existing Hsp90 inhibitors CNF-2024 and SNX-5422 as an anti-cancer agent.	1-(4-(2-(6-amino-8-((6-bromo-1,3-benzodioxol-5-yl)sulfanyl)-9H-purin-9-yl)ethyl)piperidin-1-yl)-2-hydroxypropan-1-one	56-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
32659088-12	2020	This finding suggests that under trial Hsp90 inhibitors MPC-3100 could be a potential starting point into the development of potential anti-cancer agents with the possibility of future directions for the improvement of early existing Hsp90 inhibitors CNF-2024 and SNX-5422 as an anti-cancer agent.	1-(4-(2-(6-amino-8-((6-bromo-1,3-benzodioxol-5-yl)sulfanyl)-9H-purin-9-yl)ethyl)piperidin-1-yl)-2-hydroxypropan-1-one	56-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
32659088-12	2020	This finding suggests that under trial Hsp90 inhibitors MPC-3100 could be a potential starting point into the development of potential anti-cancer agents with the possibility of future directions for the improvement of early existing Hsp90 inhibitors CNF-2024 and SNX-5422 as an anti-cancer agent.	SNX-5422	264-272	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
32799638-0	2021	Identification of the naphthoquinone derivative inhibitors binding site in heat shock protein 90: an induced-fit docking, molecular dynamics and 3D-QSAR study.	Naphthoquinones	22-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
32799638-2	2021	In this work, we used these analyses to understand the potent inhibitory effect of naphthoquinone derivatives on heat shock protein 90 (Hsp90), one of the proteins involved in many types of cancer.	Naphthoquinones	83-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-134
32799638-2	2021	In this work, we used these analyses to understand the potent inhibitory effect of naphthoquinone derivatives on heat shock protein 90 (Hsp90), one of the proteins involved in many types of cancer.	Naphthoquinones	83-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
32799638-3	2021	Molecular docking results indicated that some favorable interactions of key amino acid residues at the binding site of Hsp90 with these quinones would be responsible for the inhibition of Hsp90 activity.	Quinones	136-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
32799638-3	2021	Molecular docking results indicated that some favorable interactions of key amino acid residues at the binding site of Hsp90 with these quinones would be responsible for the inhibition of Hsp90 activity.	Quinones	136-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
32799638-7	2021	Our results provide the bases for a rational modification of new molecules based in quinone scaffold, in order to design more potent Hsp90 inhibitors, which would exhibit highly potent antitumor activity.	quinone	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
32903557-6	2020	Combining IVIgG with the HSP90 inhibitor AUY922 produced superior cell growth inhibition and correlated with HSP70-1 suppression.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
32922531-7	2020	Higher HSP90 levels were more frequent in CRC patients with hazardous or harmful alcohol consumption habits.	Alcohols	81-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-12
32922531-10	2020	The levels of HSP90 were inversely associated with short-term efficacy in GC patients who had received fluorouracil/platinum-based advanced first-line treatment.	Fluorouracil	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
32922531-10	2020	The levels of HSP90 were inversely associated with short-term efficacy in GC patients who had received fluorouracil/platinum-based advanced first-line treatment.	Platinum	116-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
32527727-6	2020	Hsp90 chaperone function is coupled to its ability to bind and hydrolyze ATP, which is tightly regulated both by co-chaperone proteins and post-translational modifications (PTMs).	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32905537-6	2020	In mRNA-hub gene analysis, HSP90AA1, EEF1A1, APP, and HSPA4 were related to recurrence in BC patients with pCR due to NAC.	nac	118-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-35
32527460-0	2020	Quinazoline Based HSP90 Inhibitors: Synthesis, Modeling Study and ADME Calculations Towards Breast Cancer Targeting.	Quinazolines	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
32527460-1	2020	A new 2-thioquinazolinones series was designed and synthesized as HSP90 inhibitors based on the structure of hit compound VII obtained by virtual screening approach.	2-thioquinazolinones	6-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
32527460-5	2020	HSP90 ATPase activity inhibition assay were conducted where compound 5d exhibited the best IC50 with 1.58 muM compared to Tanespimycin (IC50 = 2.17 muM).	tanespimycin	122-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32527460-10	2020	Molecular docking studies suggested mode of interaction to HSP90 via hydrogen bonding.	Hydrogen	69-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
32540783-4	2020	Compounds 5b, 5k and 8a showed potent HSP90 inhibitory activities with IC50 values in nanomolar range; 71.32, 25.07 and 56.78 nm, respectively, against Tanespimycin (IC50 of 86.45 nm).	tanespimycin	152-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
32408215-0	2020	Corrigendum to "N-alkyl-hydroxybenzoyl anilide hydroxamates as dual inhibitors of HDAC and HSP90, downregulating IFN-gamma induced PD-L1 expression"[Eur.	n-alkyl-hydroxybenzoyl anilide hydroxamates	16-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
32302629-3	2020	Hsp90 is ATP-dependent, participates in critical cell events and protein maturation and interacts with large numbers of co-chaperones.	Adenosine Triphosphate	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32722485-4	2020	Additionally, its inhibition, by specific HSP90 inhibitors (e.g., 17 AAG, 17 DAG, and AUY-922) has proven beneficial in different preclinical models of human disease.	tanespimycin	66-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
32722485-4	2020	Additionally, its inhibition, by specific HSP90 inhibitors (e.g., 17 AAG, 17 DAG, and AUY-922) has proven beneficial in different preclinical models of human disease.	17 dag	74-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
32722485-4	2020	Additionally, its inhibition, by specific HSP90 inhibitors (e.g., 17 AAG, 17 DAG, and AUY-922) has proven beneficial in different preclinical models of human disease.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	86-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
32627780-0	2020	NIR-controlled HSP90 inhibitor release from hollow mesoporous nanocarbon for synergistic tumor photothermal therapy guided by photoacoustic imaging.	mesoporous	51-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	41-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	41-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	56-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	56-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	Polyethylene Glycols	123-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	Polyethylene Glycols	123-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	127-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	127-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
32627780-6	2020	Interestingly, combined with hydrophobic gambogic acid (GA) which can downregulate heat shock protein 90 (HSP90), the HMCS-PEG-GA system showed a significant NIR-enhanced tumor therapeutic effect in vitro and in vivo under mild temperature conditions (~43  C), and the combination index (CI) value of HMCS-PEG-GA was found to be 0.72.	gambogic acid	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32715032-3	2020	We recently suggested that the mediating mechanism may be a down-regulation of the vitamin D co-activator heat-shock protein (Hsp)90beta.	Vitamin D	83-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-136
32715032-9	2020	Results: We initially found that whole human bile, but only together with the fatty acid butyrate, potently induced Hsp90beta expression.	Fatty Acids	78-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-125
32715032-9	2020	Results: We initially found that whole human bile, but only together with the fatty acid butyrate, potently induced Hsp90beta expression.	Butyrates	89-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-125
32715032-10	2020	In line with this, a single bile acid, e.g. glycocholic acid (GCA), in combination with butyrate, increased Hsp90beta expression (40 +- 13% vs. GCA, butyrate or vehicle alone; p < 0,001; n = 14-25).	Bile Acids and Salts	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-117
32715032-10	2020	In line with this, a single bile acid, e.g. glycocholic acid (GCA), in combination with butyrate, increased Hsp90beta expression (40 +- 13% vs. GCA, butyrate or vehicle alone; p < 0,001; n = 14-25).	Glycocholic Acid	44-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-117
32715032-10	2020	In line with this, a single bile acid, e.g. glycocholic acid (GCA), in combination with butyrate, increased Hsp90beta expression (40 +- 13% vs. GCA, butyrate or vehicle alone; p < 0,001; n = 14-25).	Glycocholic Acid	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-117
32715032-10	2020	In line with this, a single bile acid, e.g. glycocholic acid (GCA), in combination with butyrate, increased Hsp90beta expression (40 +- 13% vs. GCA, butyrate or vehicle alone; p < 0,001; n = 14-25).	Butyrates	88-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-117
32715032-10	2020	In line with this, a single bile acid, e.g. glycocholic acid (GCA), in combination with butyrate, increased Hsp90beta expression (40 +- 13% vs. GCA, butyrate or vehicle alone; p < 0,001; n = 14-25).	Butyrates	149-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-117
32304763-6	2020	The effects of the Hsp90beta inhibitor 17-N-allylamino-17-demethoxygeldanamycin (17-AAG) on morphine tolerance and dependence were studied via a hot plate test and CPP test.	Morphine	92-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-28
32304763-7	2020	KEY FINDINGS: Hsp90beta, instead of Hsp90alpha, interacted with the MOR in HEK293 cells and SH-SY5Y cells, and the interaction was augmented after morphine pretreatment.	Morphine	147-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-23
32304763-8	2020	The interaction of Hsp90beta and MOR increased the inhibition of cAMP and decreased PKA activity under opioid treatment.	Cyclic AMP	65-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-28
32304763-10	2020	17-AAG blocked Hsp90beta-MOR interactions and decreased the effect of Hsp90beta on the MOR signal transduction.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-24
32304763-10	2020	17-AAG blocked Hsp90beta-MOR interactions and decreased the effect of Hsp90beta on the MOR signal transduction.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-79
32304763-15	2020	It is conceivable that in future clinical treatments, the Hsp90beta inhibitor, 17-AAG, could decrease the tolerance and dependence in cancer patients induced by opioids.	tanespimycin	79-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-67
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
32656215-0	2020	Differential Methylation in Promoter Regions of the Genes NR3C1 and HSP90AA1, Involved in the Regulation, and Bioavailability of Cortisol in Leukocytes of Women With Preeclampsia.	Hydrocortisone	129-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-76
32832020-0	2020	From Bacteria to Cancer: A Benzothiazole-Based DNA Gyrase B Inhibitor Redesigned for Hsp90 C-Terminal Inhibition.	benzothiazole	27-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
32832020-3	2020	Novobiocin, a well characterized DNA gyrase B inhibitor, was identified as the first Hsp90 C-terminal inhibitor that manifested anticancer effects without induction of the HSR.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
32832020-4	2020	In this letter, a library of Hsp90 C-terminal inhibitors derived from a benzothiazole-based scaffold, known to inhibit DNA gyrase B, was designed, synthesized, and evaluated.	benzothiazole	72-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
32503118-0	2020	A 2,5-Dihydroxybenzoic Acid-Gelatin Conjugate Inhibits the Basal and Hsp90-Stimulated Migration and Invasion of Tumor Cells.	2,5-dihydroxybenzoic acid	2-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
32503118-2	2020	Earlier, we demonstrated that plasma membrane-associated heparan sulfate proteoglycans (HSPGs) bind the extracellular Hsp90 and thereby promote the Hsp90-mediated motility of tumor cells.	Heparitin Sulfate	57-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
32592377-0	2020	Hsp90 Inhibitor; NVP-AUY922 in Combination with Doxorubicin Induces Apoptosis and Downregulates VEGF in MCF-7 Breast Cancer Cell Line.	Doxorubicin	48-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32220496-4	2020	Here we report that the use of apigenin can suppress the HIF-1alpha expression in hypoxic tumors through the simultaneous inhibition of the AKT/p-AKT pathway and HSP90, which is beneficial for enhancing the anticancer activity of the co-administered paclitaxel.	Apigenin	31-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
32352777-1	2020	Herein, a series of HSP90 inhibitors-SN38 conjugates through ester and carbamate linkage in the 20-OH and 10-OH positions of SN38 were developed for improving the tumor-specific penetration and accumulation of SN38 via extracellular HSP90 (eHSP90)-mediated endocytosis.	Esters	61-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32352777-1	2020	Herein, a series of HSP90 inhibitors-SN38 conjugates through ester and carbamate linkage in the 20-OH and 10-OH positions of SN38 were developed for improving the tumor-specific penetration and accumulation of SN38 via extracellular HSP90 (eHSP90)-mediated endocytosis.	Esters	61-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	233-238
32352777-1	2020	Herein, a series of HSP90 inhibitors-SN38 conjugates through ester and carbamate linkage in the 20-OH and 10-OH positions of SN38 were developed for improving the tumor-specific penetration and accumulation of SN38 via extracellular HSP90 (eHSP90)-mediated endocytosis.	Carbamates	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
32352777-1	2020	Herein, a series of HSP90 inhibitors-SN38 conjugates through ester and carbamate linkage in the 20-OH and 10-OH positions of SN38 were developed for improving the tumor-specific penetration and accumulation of SN38 via extracellular HSP90 (eHSP90)-mediated endocytosis.	Carbamates	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	233-238
32466509-2	2020	In this study, we investigate the effect of 17-aminogeldanamycin, a potent HSP90 inhibitor, on nuclear factor-kappa B (NF-kappaB) activity in BRAFV600E and NRASQ61R patient-derived melanoma cell lines.	17-aminogeldanamycin	44-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
32156599-0	2020	Hsp90 inhibition aggravates adriamycin-induced podocyte injury through intrinsic apoptosis pathway.	Doxorubicin	28-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
32151689-3	2020	17-DMAG is a water soluble Hsp90 inhibitor, which was proved to be effective for advanced solid tumors and hematological malignancy.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
32151689-3	2020	17-DMAG is a water soluble Hsp90 inhibitor, which was proved to be effective for advanced solid tumors and hematological malignancy.	Water	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
32222339-4	2020	Herein we report a series of compounds by molecular hybridization PARP-1 inhibitor Olaparib (Ola) with HSP90 inhibitor C0817 (one curcumin derivative).	c0817	119-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
32222339-4	2020	Herein we report a series of compounds by molecular hybridization PARP-1 inhibitor Olaparib (Ola) with HSP90 inhibitor C0817 (one curcumin derivative).	Curcumin	130-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
32100243-6	2020	miR-485-5p overexpression dramatically reduced AKT1, HSP90, and ki-67 proteins, increased E-cadherin protein levels, and inhibited OS cell proliferation and migration.	mir-485-5p	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
32328609-2	2020	Human hepatocellular carcinoma cell line HepG2 was treated with Hsp90 N- and C-terminal inhibitors (STA9090 and Novobiocin), respectively.	STA 9090	100-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
32328609-10	2020	Whereas both STA9090 and Novobiocin inhibited Hsp90 to bind to the TFEB proximal promoter region, and decreased the activity of TFEB promoter.	STA 9090	13-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
32328609-10	2020	Whereas both STA9090 and Novobiocin inhibited Hsp90 to bind to the TFEB proximal promoter region, and decreased the activity of TFEB promoter.	Novobiocin	25-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
32212608-1	2020	Protein turnover in cells is regulated by the ATP dependent activity of the Hsp90 chaperone.	Adenosine Triphosphate	46-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
32212608-2	2020	In concert with accessory proteins, ATP hydrolysis drives the obligate Hsp90 dimer through a cycle between open and closed states that is critical for assisting the folding and stability of hundreds of proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
32295059-0	2020	Understanding the Hsp90 N-terminal Dynamics: Structural and Molecular Insights into the Therapeutic Activities of Anticancer Inhibitors Radicicol (RD) and Radicicol Derivative (NVP-YUA922).	monorden	136-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
32295059-0	2020	Understanding the Hsp90 N-terminal Dynamics: Structural and Molecular Insights into the Therapeutic Activities of Anticancer Inhibitors Radicicol (RD) and Radicicol Derivative (NVP-YUA922).	monorden	155-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
32295059-2	2020	The function of Hsp90 is highly dependent on adenosine triphosphate (ATP) binding to the N-terminal domain of the protein.	Adenosine	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
32295059-2	2020	The function of Hsp90 is highly dependent on adenosine triphosphate (ATP) binding to the N-terminal domain of the protein.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
32295059-4	2020	Radicicol (RD) and its derivative, resorcinylic isoxazole amine NVP-AUY922 (NVP), have shown promising pharmacodynamics against Hsp90 activity.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
32252465-3	2020	The mechanism of AhR transformation was examined using mutational approaches and stabilization of the AhR:hsp90 complex with sodium molybdate.	sodium molybdate(VI)	125-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
32252465-6	2020	Stabilization of AhR:hsp90 binding with sodium molybdate decreased transformation/DNA binding of the wild type AhR but had no effect on constitutively active AhR mutants.	sodium molybdate(VI)	40-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
32252465-7	2020	Interestingly, transformation of the AhR in the presence of molybdate allowed detection of an intermediate transformation ternary complex containing hsp90, AhR, and ARNT.	molybdate	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
32097779-13	2020	In addition, KBA01 disrupts the HSF1-mutant p53-Hsp90 complex and releases mutant p53 to enable its MDM2- and CHIP-mediated degradation.	kba01	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
32058968-2	2020	Both the conformational events tuned by ATP/ADP and co-chaperones and the chaperoning cycle timing are required for Hsp90"s fully functional display.	Adenosine Triphosphate	40-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
32093392-0	2020	In Vitro Inhibition of Hsp90 Protein by Benzothiazoloquinazolinequinones Is Enhanced in The Presence of Ascorbate.	benzothiazoloquinazolinequinones	40-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
32093392-0	2020	In Vitro Inhibition of Hsp90 Protein by Benzothiazoloquinazolinequinones Is Enhanced in The Presence of Ascorbate.	Ascorbic Acid	104-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
32093392-7	2020	The selected quinones were evaluated regarding their effects on cancer cell proliferation (clonogenic assay) and on Hsp90 and poly(ADPribose)polymerase (PARP) protein integrity.	Quinones	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
32093392-9	2020	In the presence of ascorbate, it induced an oxidative cleavage of Hsp90 but had no effect on PARP protein integrity.	Ascorbic Acid	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
31935086-5	2020	Both in vitro and in vivo assays revealed that 18h could efficiently block the Hsp90-Cdc37 interaction to specifically inhibit kinase clients of Hsp90.	18h	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
31935086-5	2020	Both in vitro and in vivo assays revealed that 18h could efficiently block the Hsp90-Cdc37 interaction to specifically inhibit kinase clients of Hsp90.	18h	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
32180962-10	2020	The disassociation of MMP-9 with hyper-acetylated heat shock protein 90 (Hsp90) was observed resulting in MMP-9 degradation after honokiol treatment.	honokiol	130-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-71
32180962-10	2020	The disassociation of MMP-9 with hyper-acetylated heat shock protein 90 (Hsp90) was observed resulting in MMP-9 degradation after honokiol treatment.	honokiol	130-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
32180962-12	2020	Accordingly, the results suggested that the suppression of migration and invasion activities by honokiol was through inhibiting HDAC6-mediated Hsp90/MMP-9 interaction and followed by MMP-9 degradation in lung cancer.	honokiol	96-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
31786226-0	2020	Highly effective methods for expression/purification of recombinant human HSP90 and its four distinct (N-LR-M-C) domains.	Nitrogen	103-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
31786226-1	2020	Heat shock protein 90 (HSP90) plays essential roles in the normal physiology and comprises four distinct domains, including NH2-terminal (N), charged linker region (LR), middle (M), and COOH-terminal (C) domains, all of which regulate HSP90 biological functions.	Ammonia	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
31786226-1	2020	Heat shock protein 90 (HSP90) plays essential roles in the normal physiology and comprises four distinct domains, including NH2-terminal (N), charged linker region (LR), middle (M), and COOH-terminal (C) domains, all of which regulate HSP90 biological functions.	Ammonia	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
31786226-1	2020	Heat shock protein 90 (HSP90) plays essential roles in the normal physiology and comprises four distinct domains, including NH2-terminal (N), charged linker region (LR), middle (M), and COOH-terminal (C) domains, all of which regulate HSP90 biological functions.	Nitrogen	124-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
31786226-1	2020	Heat shock protein 90 (HSP90) plays essential roles in the normal physiology and comprises four distinct domains, including NH2-terminal (N), charged linker region (LR), middle (M), and COOH-terminal (C) domains, all of which regulate HSP90 biological functions.	Nitrogen	124-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
31786226-1	2020	Heat shock protein 90 (HSP90) plays essential roles in the normal physiology and comprises four distinct domains, including NH2-terminal (N), charged linker region (LR), middle (M), and COOH-terminal (C) domains, all of which regulate HSP90 biological functions.	adenosine-5'-carboxylic acid	186-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
31786226-1	2020	Heat shock protein 90 (HSP90) plays essential roles in the normal physiology and comprises four distinct domains, including NH2-terminal (N), charged linker region (LR), middle (M), and COOH-terminal (C) domains, all of which regulate HSP90 biological functions.	adenosine-5'-carboxylic acid	186-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
31786226-3	2020	cDNAs encoding FL, N, LR, M and C domains of human HSP90alpha were amplified and cloned into pET-32b(+) expression vector.	Nitrogen	2-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-61
31786226-4	2020	All HSP90 constructs were expressed as soluble Trx-His-S tagged proteins after induction with 0.25 mM isopropyl-beta-d-thiogalactopyranoside (IPTG) at 18  C overnight and further purified by affinity chromatography using nickel-nitrilotriacetic acid (Ni-NTA) resin.	Thiogalactosides	102-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31786226-4	2020	All HSP90 constructs were expressed as soluble Trx-His-S tagged proteins after induction with 0.25 mM isopropyl-beta-d-thiogalactopyranoside (IPTG) at 18  C overnight and further purified by affinity chromatography using nickel-nitrilotriacetic acid (Ni-NTA) resin.	Thiogalactosides	142-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31808979-0	2020	Discovery of N-pyridoyl-Delta2 -pyrazolines as Hsp90 inhibitors.	n-pyridoyl-delta2 -pyrazolines	13-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
31808979-2	2020	Herein, we report the discovery of N-pyridoyl-Delta2 -pyrazoline analogs as novel Hsp90 inhibitors by integrated approaches of drug design, organic synthesis, cell biology, and qualitative proteomic analysis.	n-pyridoyl-delta2 -pyrazoline	35-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
31808979-3	2020	Novel chemical compounds were designed and optimized in the adenosine triphosphate-binding site of Hsp90; lead optimized compounds were found to have significant interactions with Asp93 and other amino acids crucial for Hsp90 inhibition.	Adenosine	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
31808979-3	2020	Novel chemical compounds were designed and optimized in the adenosine triphosphate-binding site of Hsp90; lead optimized compounds were found to have significant interactions with Asp93 and other amino acids crucial for Hsp90 inhibition.	Adenosine	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
31863779-4	2020	Based on our results, AT-533 suppressed the tube formation, cell migration, and invasion of human umbilical vein endothelial cells (HUVECs), and was more effective than the Hsp90 inhibitor, 17-AAG.	tanespimycin	190-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
31650359-0	2020	Inhibition of HSP90 overcomes melphalan resistance through downregulation of Src in multiple myeloma cells.	Melphalan	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
31650359-7	2020	In this study, we assessed the role of HSP90 in MDR using established melphalan-resistant MM cells.	Melphalan	70-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
31650359-8	2020	We found that expression of HSP90 was higher in melphalan-resistant MM cells than in parent cells and that HSP90 inhibitors KW-2478 and NUV-AUY922 restored drug sensitivity to the level observed in parent cells.	Melphalan	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
31918062-12	2020	Animal experiments indicated that the efficacy of luteolin was similar to that of 17-AAG, which both alleviated skin tissue lesions and symptoms, improved the expression of Hsp90 mRNA and protein in skin tissue, and promoted exosome secretion of Hsp90 in plasma.	tanespimycin	82-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
31918062-12	2020	Animal experiments indicated that the efficacy of luteolin was similar to that of 17-AAG, which both alleviated skin tissue lesions and symptoms, improved the expression of Hsp90 mRNA and protein in skin tissue, and promoted exosome secretion of Hsp90 in plasma.	tanespimycin	82-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
31918337-0	2020	trans, trans-2,4-Decadienal, a lipid peroxidation product, induces inflammatory responses via Hsp90- or 14-3-3zeta-dependent mechanisms.	trans, trans-2,4-decadienal	0-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
31918337-5	2020	Using click chemistry-based proteomics, we found that tt-DDE directly interacts with Hsp90 and 14-3-3zeta, which are two important proteins involved in inflammation and tumorigenesis.	tt-dde	54-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
31918337-6	2020	Furthermore, siRNA knockdown of Hsp90 or 14-3-3zeta abolished the pro-inflammatory effects of tt-DDE in macrophage cells.	tt-dde	94-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
31918337-7	2020	Together, our results support that tt-DDE increases inflammatory responses via Hsp90- and 14-3-3zeta-dependent mechanisms.	tt-dde	35-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
31662027-3	2020	Several inhibitors against the Hsp90 ATP-binding site have been developed.	Adenosine Triphosphate	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
31662027-10	2020	Such tool compounds will help to evaluate whether the toxicity profile of Hsp90/Cdc37 PPI inhibitors is in general more favorable than that of ATP-competitive Hsp90 inhibitors.	Adenosine Triphosphate	143-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
31963524-0	2020	The Major Heat Shock Proteins, Hsp70 and Hsp90, in 2-Methoxyestradiol-Mediated Osteosarcoma Cell Death Model.	2-Methoxyestradiol	51-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
31963524-6	2020	The current study aimed to determine the role of major heat shock proteins, Hsp90 and Hsp70 in 2-methoxyestradiol-induced osteosarcoma cell death.	2-Methoxyestradiol	95-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
31963524-7	2020	We focused on the implication of Hsp90 and Hsp70 in control under expression of neuronal nitric oxide synthase, localization of the enzyme, and further generation of nitro-oxidative stress.	Nitric Oxide	89-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
31963524-7	2020	We focused on the implication of Hsp90 and Hsp70 in control under expression of neuronal nitric oxide synthase, localization of the enzyme, and further generation of nitro-oxidative stress.	nitro	166-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
31963524-8	2020	To give the insight into the role of Hsp90 in regulation of anticancer efficacy of 2-methoxyestradiol, we used geldanamycin as a potent Hsp90 inhibitor.	2-Methoxyestradiol	83-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
31963524-8	2020	To give the insight into the role of Hsp90 in regulation of anticancer efficacy of 2-methoxyestradiol, we used geldanamycin as a potent Hsp90 inhibitor.	2-Methoxyestradiol	83-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
31963524-8	2020	To give the insight into the role of Hsp90 in regulation of anticancer efficacy of 2-methoxyestradiol, we used geldanamycin as a potent Hsp90 inhibitor.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
31963524-8	2020	To give the insight into the role of Hsp90 in regulation of anticancer efficacy of 2-methoxyestradiol, we used geldanamycin as a potent Hsp90 inhibitor.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
31963524-9	2020	Herein, we evidenced that inhibition of Hsp90 controls the protein expression of 2-methoxyestradiol-induced neuronal nitric oxide synthase and inhibits enzyme nuclear translocation.	2-Methoxyestradiol	81-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
31963524-9	2020	Herein, we evidenced that inhibition of Hsp90 controls the protein expression of 2-methoxyestradiol-induced neuronal nitric oxide synthase and inhibits enzyme nuclear translocation.	Nitric Oxide	117-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
31963524-10	2020	We propose that decreased level of neuronal nitric oxide synthase protein after a combined treatment with 2-methoxyestradiol and geldanamycin is directly associated with the accompanying upregulation of Hsp70 and downregulation of Hsp90.	Nitric Oxide	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-236
31963524-10	2020	We propose that decreased level of neuronal nitric oxide synthase protein after a combined treatment with 2-methoxyestradiol and geldanamycin is directly associated with the accompanying upregulation of Hsp70 and downregulation of Hsp90.	2-Methoxyestradiol	106-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-236
31963524-10	2020	We propose that decreased level of neuronal nitric oxide synthase protein after a combined treatment with 2-methoxyestradiol and geldanamycin is directly associated with the accompanying upregulation of Hsp70 and downregulation of Hsp90.	geldanamycin	129-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-236
31839539-0	2020	Discovery of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl)acetates as potent Hsp90 inhibitors with selectivity over TRAP1.	N-((2-Phenyl-2H-1,2,3-triazol-4-yl)methylene)-2-(2-(2-phenyl-2H-1,2,3-triazol-4-yl)-3-(2-((2-phenyl-2H-1,2,3-triazol-4-yl)methyleneamino)ethyl)imidazolidin-1-yl)ethanamine	13-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
31839539-3	2020	A structure-based drug design approach was applied to develop novel resorcinolyltriazole derivatives as Hsp90 inhibitors.	resorcinolyltriazole	68-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
31839539-5	2020	Click chemistry between iodoethynylresorcinol and an azido derivative was used to synthesize a new family of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl) acetates that exhibited Hsp90 binding affinities of 40-100 nM (IC50).	iodoethynylresorcinol	24-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
31839539-5	2020	Click chemistry between iodoethynylresorcinol and an azido derivative was used to synthesize a new family of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl) acetates that exhibited Hsp90 binding affinities of 40-100 nM (IC50).	3',5-diazido-2',3'-dideoxyuridine	53-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
31839539-5	2020	Click chemistry between iodoethynylresorcinol and an azido derivative was used to synthesize a new family of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl) acetates that exhibited Hsp90 binding affinities of 40-100 nM (IC50).	N-((2-Phenyl-2H-1,2,3-triazol-4-yl)methylene)-2-(2-(2-phenyl-2H-1,2,3-triazol-4-yl)-3-(2-((2-phenyl-2H-1,2,3-triazol-4-yl)methyleneamino)ethyl)imidazolidin-1-yl)ethanamine	109-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
31839539-6	2020	Among the synthesized molecules, the triazole alkyl acetates displayed the highest Hsp90 binding affinities.	Alkanesulfonates	37-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
31859027-0	2020	Identification of vibsanin A analog as a novel HSP90 inhibitor.	vibsanin A	18-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
31952268-8	2020	Pharmacological inhibition of Hsp90 with geldanamycin results in the degradation of Hakai in a lysosome-dependent manner.	geldanamycin	41-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
31915228-0	2020	Puupehenone, a Marine-Sponge-Derived Sesquiterpene Quinone, Potentiates the Antifungal Drug Caspofungin by Disrupting Hsp90 Activity and the Cell Wall Integrity Pathway.	puupehenone	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
31915228-0	2020	Puupehenone, a Marine-Sponge-Derived Sesquiterpene Quinone, Potentiates the Antifungal Drug Caspofungin by Disrupting Hsp90 Activity and the Cell Wall Integrity Pathway.	sesquiterpene quinone	37-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
31915228-15	2020	Our findings revealed a mechanism, different from previously reported caspofungin potentiators, in which potentiation is achieved by the disruption of Hsp90 activity and signaling through the cell wall integrity pathway, processes that play important roles in the adaptation to caspofungin in fungal pathogens.	Caspofungin	70-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
31915228-15	2020	Our findings revealed a mechanism, different from previously reported caspofungin potentiators, in which potentiation is achieved by the disruption of Hsp90 activity and signaling through the cell wall integrity pathway, processes that play important roles in the adaptation to caspofungin in fungal pathogens.	Caspofungin	278-289	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
31936169-0	2020	Metformin Inhibits Tumor Metastasis through Suppressing Hsp90alpha Secretion in an AMPKalpha1-PKCgamma Dependent Manner.	Metformin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
31936169-4	2020	Here we show that metformin inhibits tumor metastasis by suppressing Hsp90alpha (heat shock protein 90alpha) secretion.	Metformin	18-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-79
31936169-5	2020	Mass spectrometry (MS) analysis and functional validation identify that eHsp90alpha (extracellular Hsp90alpha) is one of the most important secreted proteins for metformin to inhibit tumor cells migration, invasion and metastasis both in vitro and in vivo.	Metformin	162-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-83
31936169-6	2020	Moreover, we find that metformin inhibits Hsp90alpha secretion in an AMPKalpha1 dependent manner.	Metformin	23-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-52
31936169-8	2020	Collectively, our results illuminate that metformin inhibits tumor metastasis by suppressing Hsp90alpha secretion in an AMPKalpha1 dependent manner.	Metformin	42-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-103
31874991-0	2019	Mitragynine, an euphoric compound inhibits hERG1a/1b channel current and upregulates the complexation of hERG1a-Hsp90 in HEK293-hERG1a/1b cells.	mitragynine	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
31874991-10	2019	In conclusion, mitragynine inhibits hERG1a/1b current through direct channel blockade at lower concentration, but at higher concentration, it upregulates the complexation of hERG1a-Hsp90 which may be inhibitory towards channel trafficking.	mitragynine	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
31725288-0	2019	Discovery of novel celastrol derivatives as Hsp90-Cdc37 interaction disruptors with antitumour activity.	celastrol	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
31697501-2	2019	Correlating simulations with experimental data from SPR kinetics measurements and X-ray crystallography on two small molecule compound libraries bound to the N-terminal domain of the chaperone Hsp90, we show that the mean non-equilibrium work computed in an ensemble of trajectories of enforced ligand unbinding is a promising predictor for ligand unbinding rates.	Nitrogen	158-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
31725288-1	2019	To develop novel and efficient heat shock protein 90-cell division cycle 37 (Hsp90-Cdc37) interaction disruptors, several lipophilic fragments were introduced into celastrol (CEL) to synthesize 48 new CEL derivatives.	celastrol	175-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31725288-1	2019	To develop novel and efficient heat shock protein 90-cell division cycle 37 (Hsp90-Cdc37) interaction disruptors, several lipophilic fragments were introduced into celastrol (CEL) to synthesize 48 new CEL derivatives.	celastrol	164-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31725288-1	2019	To develop novel and efficient heat shock protein 90-cell division cycle 37 (Hsp90-Cdc37) interaction disruptors, several lipophilic fragments were introduced into celastrol (CEL) to synthesize 48 new CEL derivatives.	celastrol	201-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
31725288-3	2019	The capability to disrupt the Hsp90-Cdc37 interaction was stronger than that of CEL.	celastrol	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
31634779-8	2019	In cell line study, Hsp90-treated cells (CNE1, 5-8 F) resulted in promoted cellular growth and proliferation.	phenylalanyl-leucyl-phenylalanyl-glutaminyl-prolyl-glutaminyl-arginyl-phenylalaninamide	47-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
31725288-6	2019	Together, 41 is a novel Hsp90-Cdc37 disruptor by binding to Cdc37 (hydrogen bond and/or covalent bond).	Hydrogen	67-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
31493740-2	2019	The ATP-dependant heat shock protein 90 (Hsp90) forms the central component of molecular chaperone machinery that predominantly governs the folding of newly synthesized peptides and their conformational maturation.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
31634779-10	2019	Followed by treatment with Hsp90 inhibitor, the NPC cells exhibited inhibited cellular proliferation and growth, induced cell apoptosis, reduced proliferative proteins of Erk1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473), Bcl-2, Ki-67, and elevated Apaf1 expression.	phosphorylleucylphenylalanine	179-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31634779-10	2019	Followed by treatment with Hsp90 inhibitor, the NPC cells exhibited inhibited cellular proliferation and growth, induced cell apoptosis, reduced proliferative proteins of Erk1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473), Bcl-2, Ki-67, and elevated Apaf1 expression.	exorphin A5	195-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31634779-10	2019	Followed by treatment with Hsp90 inhibitor, the NPC cells exhibited inhibited cellular proliferation and growth, induced cell apoptosis, reduced proliferative proteins of Erk1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473), Bcl-2, Ki-67, and elevated Apaf1 expression.	phosphorylleucylphenylalanine	216-223	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31634779-10	2019	Followed by treatment with Hsp90 inhibitor, the NPC cells exhibited inhibited cellular proliferation and growth, induced cell apoptosis, reduced proliferative proteins of Erk1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473), Bcl-2, Ki-67, and elevated Apaf1 expression.	seryl-seryl-seryl-arginine	229-235	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31634779-10	2019	Followed by treatment with Hsp90 inhibitor, the NPC cells exhibited inhibited cellular proliferation and growth, induced cell apoptosis, reduced proliferative proteins of Erk1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473), Bcl-2, Ki-67, and elevated Apaf1 expression.	Ki-67 Antigen	245-250	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31634779-11	2019	In conclusion, the current findings obtained from this study demonstrate that Hsp90 effectively promotes cell proliferation through activating carcinomatous ERK1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473) expressions in NPC cells.	phosphorylleucylphenylalanine	165-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
31634779-11	2019	In conclusion, the current findings obtained from this study demonstrate that Hsp90 effectively promotes cell proliferation through activating carcinomatous ERK1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473) expressions in NPC cells.	exorphin A5	181-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
31634779-11	2019	In conclusion, the current findings obtained from this study demonstrate that Hsp90 effectively promotes cell proliferation through activating carcinomatous ERK1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473) expressions in NPC cells.	phosphorylleucylphenylalanine	202-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
31634779-11	2019	In conclusion, the current findings obtained from this study demonstrate that Hsp90 effectively promotes cell proliferation through activating carcinomatous ERK1/2, phospho-Erk1/2 (Thr202+Tyr204), AKT, phospho-AKT (Ser473) expressions in NPC cells.	seryl-seryl-seryl-arginine	215-218	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
31493740-2	2019	The ATP-dependant heat shock protein 90 (Hsp90) forms the central component of molecular chaperone machinery that predominantly governs the folding of newly synthesized peptides and their conformational maturation.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
31493740-4	2019	In the present in silico investigation, a structure-based pharmacophore model was generated with hydrogen bond donor, hydrogen bond acceptor and hydrophobic features complementary to crucial residues Ala55, Lys58, Asp93, Ile96, Met98 and Thr184 directed at inhibiting the ATP-binding activity of Hsp90.	Hydrogen	97-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	296-301
31561045-0	2019	Discovery of 2-isoxazol-3-yl-acetamide analogues as heat shock protein 90 (HSP90) inhibitors with significant anti-HIV activity.	2-isoxazol-3-yl-acetamide	13-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
31561045-4	2019	Further characterization of anti-HIV activity of these molecules suggests that 2l has ~3.5 fold better therapeutic index than AUY922, the second generation HSP90 inhibitor.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	126-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
31533545-5	2019	Results: Inhibition of FLT3 mutant cells by drugs reported in recent literatures involves the influence of glycosylation of FLT3: 2-deoxy-D-glucose, Tunicamycin and Fluvastatin are reported to inhibit N-glycosylation of FLT3; Pim-1 inhibitors are proved to block the inhibition of Pim-1 on FLT3 Oglycosylation; HSP90 inhibitors and Tyrosine Kinase Inhibitors are shown to increase fully glycosylated form of FLT3.	Deoxyglucose	130-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	311-316
31533545-5	2019	Results: Inhibition of FLT3 mutant cells by drugs reported in recent literatures involves the influence of glycosylation of FLT3: 2-deoxy-D-glucose, Tunicamycin and Fluvastatin are reported to inhibit N-glycosylation of FLT3; Pim-1 inhibitors are proved to block the inhibition of Pim-1 on FLT3 Oglycosylation; HSP90 inhibitors and Tyrosine Kinase Inhibitors are shown to increase fully glycosylated form of FLT3.	Tunicamycin	149-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	311-316
31533545-5	2019	Results: Inhibition of FLT3 mutant cells by drugs reported in recent literatures involves the influence of glycosylation of FLT3: 2-deoxy-D-glucose, Tunicamycin and Fluvastatin are reported to inhibit N-glycosylation of FLT3; Pim-1 inhibitors are proved to block the inhibition of Pim-1 on FLT3 Oglycosylation; HSP90 inhibitors and Tyrosine Kinase Inhibitors are shown to increase fully glycosylated form of FLT3.	Fluvastatin	165-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	311-316
31533545-5	2019	Results: Inhibition of FLT3 mutant cells by drugs reported in recent literatures involves the influence of glycosylation of FLT3: 2-deoxy-D-glucose, Tunicamycin and Fluvastatin are reported to inhibit N-glycosylation of FLT3; Pim-1 inhibitors are proved to block the inhibition of Pim-1 on FLT3 Oglycosylation; HSP90 inhibitors and Tyrosine Kinase Inhibitors are shown to increase fully glycosylated form of FLT3.	Nitrogen	201-202	heat shock protein 90 alpha family class A member 1	Homo sapiens	311-316
31638190-0	2019	The HSP90 inhibitor onalespib potentiates 177Lu-DOTATATE therapy in neuroendocrine tumor cells.	lutetium Lu 177 dotatate	42-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31638190-4	2019	Consequently, the aim of this study was to investigate whether the HSP90-inhibitor onalespib could reduce NET cell growth and act as a radiosensitizer when used in combination with 177Lu-DOTATATE.	lutetium Lu 177 dotatate	181-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
30822267-0	2019	Delivering bioactive cyclic peptides that target Hsp90 as prodrugs.	Peptides, Cyclic	21-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
30957641-3	2019	Towards this goal, we utilized a 2,4-dihydroxy-5-isopropylbenzate-based Hsp90 inhibitor scaffold and thieno[2,3-d]pyrimidine-based kinase inhibitor scaffold to develop a Hsp90-inhibiting compound library.	2,4-dihydroxy-5-isopropylbenzate	33-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
30957641-3	2019	Towards this goal, we utilized a 2,4-dihydroxy-5-isopropylbenzate-based Hsp90 inhibitor scaffold and thieno[2,3-d]pyrimidine-based kinase inhibitor scaffold to develop a Hsp90-inhibiting compound library.	thieno(2,3-d)pyrimidine	101-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
31518867-0	2019	Synthesis, characterization, anti-tumor activity, photo-luminescence and BHb/HHb/Hsp90 molecular docking of zinc(II) hydroxyl-terpyridine complexes.	zinc(ii) hydroxyl-	108-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
31518867-0	2019	Synthesis, characterization, anti-tumor activity, photo-luminescence and BHb/HHb/Hsp90 molecular docking of zinc(II) hydroxyl-terpyridine complexes.	2,2':6',2''-Terpyridine	126-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
31518867-5	2019	Molecular docking studies suggest that the binding process of these compounds with heat shock protein 90 (Hsp90), BHb and HHb is a spontaneous molecular interaction process, in which van der Waals forces and hydrogen bonds play major roles, and pi-pi interaction also has influence on binding process.	bhb	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
31518867-5	2019	Molecular docking studies suggest that the binding process of these compounds with heat shock protein 90 (Hsp90), BHb and HHb is a spontaneous molecular interaction process, in which van der Waals forces and hydrogen bonds play major roles, and pi-pi interaction also has influence on binding process.	bhb	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
31518867-5	2019	Molecular docking studies suggest that the binding process of these compounds with heat shock protein 90 (Hsp90), BHb and HHb is a spontaneous molecular interaction process, in which van der Waals forces and hydrogen bonds play major roles, and pi-pi interaction also has influence on binding process.	Hydrogen	208-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
31518867-5	2019	Molecular docking studies suggest that the binding process of these compounds with heat shock protein 90 (Hsp90), BHb and HHb is a spontaneous molecular interaction process, in which van der Waals forces and hydrogen bonds play major roles, and pi-pi interaction also has influence on binding process.	Hydrogen	208-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
31694346-7	2019	Additionally, the exposure of human sperm to H2O2 resulted in a significant decrease in sperm viability and motility and an increase in the levels of HSF1, HSP90, HSP60, HSP27, and eIF2alpha; all proteins involved in sensing and response to unfolded proteins.	Water	45-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
31415812-6	2019	BPA exposure also abolished DHT-dependent dissociation of AR from its co-chaperone, 90-kDa heat shock protein (Hsp90), and resulted in the blockage of DHT-induced AR nuclear translocation.	bisphenol A	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
31415812-6	2019	BPA exposure also abolished DHT-dependent dissociation of AR from its co-chaperone, 90-kDa heat shock protein (Hsp90), and resulted in the blockage of DHT-induced AR nuclear translocation.	Dihydrotestosterone	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
31415812-7	2019	This is the first report to show that BPA inhibited the DHT-induced stabilization of AR and the DHT-induced dissociation of AR-Hsp90 complex.	bisphenol A	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
31415812-7	2019	This is the first report to show that BPA inhibited the DHT-induced stabilization of AR and the DHT-induced dissociation of AR-Hsp90 complex.	Dihydrotestosterone	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
31519378-8	2019	The best characterized class of HSP90 modulators are competitive inhibitors targeting the N-terminal ATP-binding pocket.	Adenosine Triphosphate	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
31747880-10	2019	Furthermore, either 1G6-D7 or PI3K inhibitor LY294002 suppressed the significant phosphorylation of AKT, which caused by secreted and recombinant Hsp90alpha, resulting in the restoration of epithelial barrier function.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	45-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-156
31561992-3	2020	We hypothesize that our novel C-terminal Hsp90 inhibitor KU758 can effectively target adrenocortical carcinoma cells and favorably alter long noncoding RNA expression.	ku758	57-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
31561992-12	2020	CONCLUSION: The novel C-terminal Hsp90 inhibitor KU758 is effective in the treatment of adrenocortical carcinoma cells and can significantly alter long noncoding RNA expression for tumor suppression.	ku758	49-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
31684904-8	2019	IL-6, TNF-alpha and MDA levels in the HSPN group were the highest, SOD and T-AOC levels were the lowest (P = 0.000).	Malondialdehyde	20-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-42
31684108-5	2019	However, 43% of patients suffered visual disturbances in a phase I trial of the second-generation Hsp90 inhibitor, NVP-AUY922.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	115-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
31659110-7	2019	In HCC tumor samples from patients treated with sorafenib, 73% of tumor samples had a high expression of GRP78, 18% had high 14-3-3epsilon expression and 85% had high HSP90beta expression.	Sorafenib	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-176
31501246-0	2019	NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90.	Adenosine-5'-(N-ethylcarboxamide)	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
31501246-2	2019	Hsp90 activity is driven by ATP, which binds to the N-terminal domain and induces large conformational changes that are required for client maturation.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31501246-3	2019	Inhibitors targeting the ATP-binding pocket of the N-terminal domain have anticancer effects, but most bind with similar affinity to cytosolic Hsp90alpha and Hsp90beta, endoplasmic reticulum Grp94, and mitochondrial Trap1, the four cellular hsp90 paralogs.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
31501246-9	2019	We found that derivatives that lengthen the 5" moiety of NECA improve selectivity for Grp94 over Hsp90alpha.	Adenosine-5'-(N-ethylcarboxamide)	57-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-107
31580341-3	2019	The present work introduces an Hsp90 inhibitor-mitochondria targeting indocyanine dye conjugate (IR-PU) for high PDT efficacy.	indocyanine	70-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
31547977-1	2019	BACKGROUND: Dependent on the extent of adenosine triphosphate (ATP) hydrolysis and/or ATP/ADP exchange, the stress-induced phosphoprotein 1 (STIP1) mediates molecular interaction and complex formation between the molecular chaperones heat shock protein (Hsp)70 and Hsp90.	Adenosine Triphosphate	39-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
31547977-1	2019	BACKGROUND: Dependent on the extent of adenosine triphosphate (ATP) hydrolysis and/or ATP/ADP exchange, the stress-induced phosphoprotein 1 (STIP1) mediates molecular interaction and complex formation between the molecular chaperones heat shock protein (Hsp)70 and Hsp90.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
31547977-1	2019	BACKGROUND: Dependent on the extent of adenosine triphosphate (ATP) hydrolysis and/or ATP/ADP exchange, the stress-induced phosphoprotein 1 (STIP1) mediates molecular interaction and complex formation between the molecular chaperones heat shock protein (Hsp)70 and Hsp90.	Adenosine Triphosphate	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
31547977-1	2019	BACKGROUND: Dependent on the extent of adenosine triphosphate (ATP) hydrolysis and/or ATP/ADP exchange, the stress-induced phosphoprotein 1 (STIP1) mediates molecular interaction and complex formation between the molecular chaperones heat shock protein (Hsp)70 and Hsp90.	Adenosine Diphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
31484751-6	2019	The treatment of RUBV-infected cells with the HSP90 inhibitors 17-allylamino-17-desmethoxygeldanamycin (17-AAG) and ganetespib suppressed RUBV genome replication.	17-allylamino-17-desmethoxygeldanamycin	63-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
31484751-6	2019	The treatment of RUBV-infected cells with the HSP90 inhibitors 17-allylamino-17-desmethoxygeldanamycin (17-AAG) and ganetespib suppressed RUBV genome replication.	tanespimycin	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
31655629-0	2019	Polo-like kinase 3 inhibits glucose metabolism in colorectal cancer by targeting HSP90/STAT3/HK2 signaling.	Glucose	28-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
31655629-14	2019	CONCLUSION: This study suggests that PLK3 inhibits glucose metabolism by targeting HSP90/STAT3/HK2 signaling and PLK3 may serve as a potential therapeutic target in colorectal cancer.	Glucose	51-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
31847934-2	2019	Geldanamycin is a potent inhibitor of HSP90, however therapeutic effects are often hampered due to its extreme hydrophobicity and systemic toxicity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
31847934-8	2019	Findings indicate exosomal formulations could be used for extremely hydrophobic HSP90 inhibitor geldanamycin delivery for inhibiting cancer cell proliferation.	geldanamycin	96-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
31611575-0	2019	A docking-based structural analysis of geldanamycin-derived inhibitor binding to human or Leishmania Hsp90.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
31802936-0	2019	Novel Hsp90 Inhibitor C086 Potently Inhibits Non-Small Cell Lung Cancer Cells As A Single Agent Or In Combination With Gefitinib.	gefitinib	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
31802936-5	2019	Methods: The binding of C086, gefitinib, and the combinations to Hsp90 was characterized by fluorescence quenching experiments.	gefitinib	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
31611575-7	2019	Some of these inhibitors, such as geldanamycin and its analogs, 17-AAG and 17-DMAG, bind directly to Hsp90, thereby inhibiting its activity.	geldanamycin	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
31611575-7	2019	Some of these inhibitors, such as geldanamycin and its analogs, 17-AAG and 17-DMAG, bind directly to Hsp90, thereby inhibiting its activity.	tanespimycin	64-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
31611575-7	2019	Some of these inhibitors, such as geldanamycin and its analogs, 17-AAG and 17-DMAG, bind directly to Hsp90, thereby inhibiting its activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
31611575-10	2019	Based on the results of the in silico approach used in the present study, we propose that geldanamycin, 17-AAG and 17-DMAG present an increased tendency to bind to the N-terminal domain of Leishmania amazonensis Hsp83 in comparison to human Hsp90.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
31611575-10	2019	Based on the results of the in silico approach used in the present study, we propose that geldanamycin, 17-AAG and 17-DMAG present an increased tendency to bind to the N-terminal domain of Leishmania amazonensis Hsp83 in comparison to human Hsp90.	tanespimycin	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
31611575-10	2019	Based on the results of the in silico approach used in the present study, we propose that geldanamycin, 17-AAG and 17-DMAG present an increased tendency to bind to the N-terminal domain of Leishmania amazonensis Hsp83 in comparison to human Hsp90.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	115-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
31611575-10	2019	Based on the results of the in silico approach used in the present study, we propose that geldanamycin, 17-AAG and 17-DMAG present an increased tendency to bind to the N-terminal domain of Leishmania amazonensis Hsp83 in comparison to human Hsp90.	Nitrogen	168-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
32082378-0	2019	2-Methoxyestradiol and Its Combination with a Natural Compound, Ferulic Acid, Induces Melanoma Cell Death via Downregulation of Hsp60 and Hsp90.	2-Methoxyestradiol	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
32082378-0	2019	2-Methoxyestradiol and Its Combination with a Natural Compound, Ferulic Acid, Induces Melanoma Cell Death via Downregulation of Hsp60 and Hsp90.	ferulic acid	64-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
32082378-8	2019	Herein, we have evidenced that the molecular mechanism of action of 2-methoxyestradiol and ferulic acid is partly related to the reduction of Hsp60 and Hsp90 levels and the induction of nitric oxide in the A375 melanoma cell model, while no changes were observed in Hsp70 expression after 2-methoxyestradiol and ferulic acid treatment separately or in combination.	2-Methoxyestradiol	68-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
32082378-8	2019	Herein, we have evidenced that the molecular mechanism of action of 2-methoxyestradiol and ferulic acid is partly related to the reduction of Hsp60 and Hsp90 levels and the induction of nitric oxide in the A375 melanoma cell model, while no changes were observed in Hsp70 expression after 2-methoxyestradiol and ferulic acid treatment separately or in combination.	ferulic acid	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
31411362-0	2019	Design, synthesis, and molecular docking studies of novel pyrazolyl 2-aminopyrimidine derivatives as HSP90 inhibitors.	pyrazolyl 2-aminopyrimidine	58-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
31411362-1	2019	A series of novel pyrazolyl 2-aminopyrimidine derivatives (7a-t) were designed based on scaffold hopping techniques, synthesized and biologically evaluated for their HSP90 inhibition and anticancer activity.	pyrazolyl 2-aminopyrimidine	18-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
31411362-2	2019	Several compounds exhibited potent HSP90 inhibition with IC50 values less than that of the reference standard 17-AAG (1.25 microM).	tanespimycin	110-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
31411362-6	2019	Therefore, the para-nitrophenyl ring on the central pyrazole ring along with the 2-amino group on the pyrimidine ring are the crucial features in the development of novel HSP90 inhibitors based on this scaffold for targeted anticancer therapy.	pyrazole	52-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
31411362-6	2019	Therefore, the para-nitrophenyl ring on the central pyrazole ring along with the 2-amino group on the pyrimidine ring are the crucial features in the development of novel HSP90 inhibitors based on this scaffold for targeted anticancer therapy.	pyrimidine	102-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
31326539-5	2019	Treatment with radicicol and VER155008, specific inhibitors of HSP90 and HSP70, respectively, attenuated these interactions and strongly reduced transporter presence at the cell surface, what resulted from the diminished level of the total transporter protein.	monorden	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31326539-5	2019	Treatment with radicicol and VER155008, specific inhibitors of HSP90 and HSP70, respectively, attenuated these interactions and strongly reduced transporter presence at the cell surface, what resulted from the diminished level of the total transporter protein.	VER 155008	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31141217-0	2019	Structures of Hsp90alpha and Hsp90beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.	purine	50-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-24
31349117-0	2019	Amide-tethered quinoline-resorcinol conjugates as a new class of HSP90 inhibitors suppressing the growth of prostate cancer cells.	Amides	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
31349117-0	2019	Amide-tethered quinoline-resorcinol conjugates as a new class of HSP90 inhibitors suppressing the growth of prostate cancer cells.	quinoline	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
31349117-0	2019	Amide-tethered quinoline-resorcinol conjugates as a new class of HSP90 inhibitors suppressing the growth of prostate cancer cells.	resorcinol	25-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
31349117-1	2019	The study is focused on the design and synthesis of amide tethered quinoline-resorcinol hybrid constructs as a new class of HSP90 inhibitor.	Amides	52-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
31349117-1	2019	The study is focused on the design and synthesis of amide tethered quinoline-resorcinol hybrid constructs as a new class of HSP90 inhibitor.	quinoline-resorcinol	67-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
31449053-7	2019	Furthermore, combined treatment with a hsp90 inhibitor and the MAST1 inhibitor lestaurtinib further abrogated MAST1 activity and consequently enhanced cisplatin-induced tumor growth arrest in a patient-derived xenograft model.	Cisplatin	151-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
31569342-0	2019	Radiosensitization of HSF-1 Knockdown Lung Cancer Cells by Low Concentrations of Hsp90 Inhibitor NVP-AUY922.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	97-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
31569342-6	2019	The Hsp90 inhibitor NVP-AUY922 was evaluated at low concentrations-ranging from 1-10 nM-in control and HSF-1 k.d.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31569342-12	2019	and low concentrations of the Hsp90 inhibitor NVP-AUY922 reduces the Hsp90 client protein Akt and potentiates radiosensitization, which involves an impaired homologous recombination mediated by Rad51.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
31569342-12	2019	and low concentrations of the Hsp90 inhibitor NVP-AUY922 reduces the Hsp90 client protein Akt and potentiates radiosensitization, which involves an impaired homologous recombination mediated by Rad51.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
31374481-3	2019	Based on the mesoporous Co9S8 nanoplatform, MRI-guided enhanced photothermal-immunology "double-hit" synergistic cancer therapy was achieved, through the HSP90 inhibition and immunology activation effect of the loaded epigallocatechin gallate and oxaliplatin.	co9s8	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
31376209-0	2019	The HSP90/Akt pathway may mediate artemether-induced apoptosis of Cal27 cells.	Artemether	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31376209-3	2019	The present study aimed to explore the correlation between the HSP90/Akt pathway and artemether-induced apoptosis of Cal27 cells.	Artemether	85-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31376209-6	2019	As the artemether concentration was increased, we observed downregulation of the expression of HSP90, p-Akt and p-mTOR in Cal27 cells, whereas the expression of Akt was not significantly changed.	Artemether	7-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
31376209-7	2019	We also observed a time-dependent decrease in the expression of HSP90, p-Akt and p-mTOR during exposure to 0.1 mg mL-1 artemether.	Artemether	119-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
31376209-8	2019	In conclusion, the HSP90/Akt pathway may be involved in artemether-induced apoptosis of Cal27 cells.	Artemether	56-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
30603780-4	2019	RESULTS: Incubation experiments with 0.3 nM cabazitaxel exhibited significantly reduced levels of AR and the AR-associated factors HSP90alpha, HSP40, and HSP70/HSP90 organising protein.	cabazitaxel	44-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-141
31141217-0	2019	Structures of Hsp90alpha and Hsp90beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.	purine	50-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-38
31141217-2	2019	Here, we analyzed the binding of an Hsp90alpha-selective PU compound, PU-11-trans, to the two cytosolic paralogs.	pu-11-trans	70-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-46
31141217-3	2019	We determined the co-crystal structures of Hsp90alpha and Hsp90beta bound to PU-11-trans, as well as the structure of the apo Hsp90beta NTD.	pu-11-trans	77-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-53
31141217-3	2019	We determined the co-crystal structures of Hsp90alpha and Hsp90beta bound to PU-11-trans, as well as the structure of the apo Hsp90beta NTD.	pu-11-trans	77-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-67
31141217-4	2019	The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90alpha, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
31141217-4	2019	The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90alpha, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network.	pu-11-trans	151-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
31141217-4	2019	The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90alpha, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network.	Water	173-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
31141217-4	2019	The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90alpha, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network.	Hydrogen	188-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
31141217-5	2019	Mutation of Ser52 to alanine, as found in Hsp90beta, alters the dissociation constant of Hsp90alpha for PU-11-trans to match that of Hsp90beta.	pu-11-trans	104-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-51
31141217-5	2019	Mutation of Ser52 to alanine, as found in Hsp90beta, alters the dissociation constant of Hsp90alpha for PU-11-trans to match that of Hsp90beta.	pu-11-trans	104-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-99
31141217-5	2019	Mutation of Ser52 to alanine, as found in Hsp90beta, alters the dissociation constant of Hsp90alpha for PU-11-trans to match that of Hsp90beta.	pu-11-trans	104-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-142
31141217-6	2019	Our results provide a structural explanation for the binding preference of PU inhibitors for Hsp90alpha and demonstrate that the single nonconserved residue in the ATP-binding pocket may be exploited for alpha/beta selectivity.	Adenosine Triphosphate	164-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-103
31527404-4	2019	Eleven Hsp90 inhibitors containing an isoxazolonaphtoquinone core were synthesized and evaluated in two MDR models comprised of sensitive and corresponding resistant cancer cells with P-gp overexpression (human non-small cell lung carcinoma and colorectal adenocarcinoma).	isoxazolonaphtoquinone	38-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-12
31555737-5	2019	Together, our results demonstrated DDO-5936 as an identified specific small-molecule inhibitor of the Hsp90-Cdc37 PPI that could be used to comprehensively investigate alternative approaches targeting Hsp90 chaperone cycles for cancer therapy.	DDO-5936	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
31472682-3	2019	We previously reported that FW-04-806 (conglobatin) as a novel Hsp90 inhibitor with low toxicity, capable of attenuating Hsp90/Cdc37 /clients interactions and producing antitumor action in vitro and in vivo.	conglobatin	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31552170-0	2019	Part I of GANNET53: A European Multicenter Phase I/II Trial of the Hsp90 Inhibitor Ganetespib Combined With Weekly Paclitaxel in Women With High-Grade, Platinum-Resistant Epithelial Ovarian Cancer-A Study of the GANNET53 Consortium.	STA 9090	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
31552170-0	2019	Part I of GANNET53: A European Multicenter Phase I/II Trial of the Hsp90 Inhibitor Ganetespib Combined With Weekly Paclitaxel in Women With High-Grade, Platinum-Resistant Epithelial Ovarian Cancer-A Study of the GANNET53 Consortium.	Platinum	152-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
31552170-4	2019	Preclinical synergy of the Hsp90 inhibitor ganetespib combined with paclitaxel provided the rationale for testing the combination in platinum-resistant ovarian cancer (PROC) patients in the GANNET53 trial (NCT02012192).	STA 9090	43-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31555737-2	2019	Here, we identified DDO-5936 as a small-molecule inhibitor of the Hsp90-Cdc37 protein-protein interaction (PPI) in colorectal cancer.	DDO-5936	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
31555737-3	2019	DDO-5936 disrupted the Hsp90-Cdc37 PPI both in vitro and in vivo via binding to a previously unknown site on Hsp90 involving Glu47, one of the binding determinants for the Hsp90-Cdc37 PPI, leading to selective down-regulation of Hsp90 kinase clients in HCT116 cells.	DDO-5936	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
31555737-3	2019	DDO-5936 disrupted the Hsp90-Cdc37 PPI both in vitro and in vivo via binding to a previously unknown site on Hsp90 involving Glu47, one of the binding determinants for the Hsp90-Cdc37 PPI, leading to selective down-regulation of Hsp90 kinase clients in HCT116 cells.	DDO-5936	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
31555737-3	2019	DDO-5936 disrupted the Hsp90-Cdc37 PPI both in vitro and in vivo via binding to a previously unknown site on Hsp90 involving Glu47, one of the binding determinants for the Hsp90-Cdc37 PPI, leading to selective down-regulation of Hsp90 kinase clients in HCT116 cells.	DDO-5936	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
31555737-3	2019	DDO-5936 disrupted the Hsp90-Cdc37 PPI both in vitro and in vivo via binding to a previously unknown site on Hsp90 involving Glu47, one of the binding determinants for the Hsp90-Cdc37 PPI, leading to selective down-regulation of Hsp90 kinase clients in HCT116 cells.	DDO-5936	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
31555737-4	2019	In addition, inhibition of Hsp90-Cdc37 complex formation by DDO-5936 resulted in a remarkable cyclin-dependent kinase 4 decrease and consequent inhibition of cell proliferation through Cdc37-dependent cell cycle arrest.	DDO-5936	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
31555737-5	2019	Together, our results demonstrated DDO-5936 as an identified specific small-molecule inhibitor of the Hsp90-Cdc37 PPI that could be used to comprehensively investigate alternative approaches targeting Hsp90 chaperone cycles for cancer therapy.	DDO-5936	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
31136038-4	2019	Curcumin has been shown to regulate different members of HSPs including HSP27, HSP40, HSP60, HSP70, and HSP90 in cancer.	Curcumin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
30980109-3	2019	We found that the HSP90alpha inhibitor NVP-AUY922 (922) effectively downregulated and destabilized the IGF-1Rbeta protein, substantially reduced the levels of downstream signaling molecules (p-AKT, AKT and p-ERK1/2), and resulted in growth inhibition and apoptosis in IGF-1Rbeta-overexpressing PC cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-28
31472682-3	2019	We previously reported that FW-04-806 (conglobatin) as a novel Hsp90 inhibitor with low toxicity, capable of attenuating Hsp90/Cdc37 /clients interactions and producing antitumor action in vitro and in vivo.	conglobatin	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
31472682-3	2019	We previously reported that FW-04-806 (conglobatin) as a novel Hsp90 inhibitor with low toxicity, capable of attenuating Hsp90/Cdc37 /clients interactions and producing antitumor action in vitro and in vivo.	conglobatin	39-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31472682-3	2019	We previously reported that FW-04-806 (conglobatin) as a novel Hsp90 inhibitor with low toxicity, capable of attenuating Hsp90/Cdc37 /clients interactions and producing antitumor action in vitro and in vivo.	conglobatin	39-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
31431614-2	2019	In this study, we delineate that KRAS-mutant lung cancer cells resistant to pemetrexed (MTA) and anti-MEK drug trametinib acquire an exquisite dependency on endoplasmic reticulum (ER) stress signaling, rendering resistant cancer cells selectively susceptible to blockage of HSP90, the receptor tyrosine kinase AXL, the eukaryotic translation initiation factor 4E (eIF4E), and the unfolded protein response (UPR).	Pemetrexed	76-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	274-279
31343810-9	2019	Mechanism analysis reveal that TGFbeta-PKCgamma gene signature defines a distinct pool of hyperphosphorylated Hsp90alpha at Theronine residue.	DL-Threonine	124-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-120
30773117-0	2019	HSP90 inhibition depletes DNA repair proteins to sensitize acute myelogenous leukemia to nucleoside analog chemotherapeutics.	Nucleosides	89-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31202885-1	2019	The Hsp90 family of chaperones requires ATP-driven cycling to perform their function.	Adenosine Triphosphate	40-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31202885-2	2019	The presence of two bound ATP molecules is known to favor a closed conformation of the Hsp90 dimer.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
31399576-0	2019	HSP90 inhibitors stimulate DNAJB4 protein expression through a mechanism involving N6-methyladenosine.	N-methyladenosine	83-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31271281-1	2019	Histone deacetylase 6 (HDAC6) primarily catalyzes the removal of acetyl group from the side chain of acetylated lysine residues in cytoplasmic proteins such as alpha-tubulin and HSP90.	Lysine	112-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
30989459-9	2019	Our study indicates that 17-aminogeldanamycin takes several advantages compared with other HSP90-targeting compounds, and can complement activity of BRAF/MEK inhibitors in melanoma cells of different genetic subtypes.	17-aminogeldanamycin	25-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
31113841-0	2019	Pharmacodynamic and Clinical Results from a Phase I/II Study of the HSP90 Inhibitor Onalespib in Combination with Abiraterone Acetate in Prostate Cancer.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	84-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
31113841-1	2019	PURPOSE: Onalespib is a potent, fragment-derived second-generation HSP90 inhibitor with preclinical activity in castration-resistant prostate cancer (CPRC) models.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
31175180-4	2019	The HSP90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin suppressed TWIST1 mRNA expression and promoter activity in epithelial ovarian cancer, renal clear cell cancer, and nasopharyngeal cancer cell lines.	tanespimycin	20-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31555510-11	2019	Conclusions: Hsp90 inhibitors and osimertinib exhibits a good efficiency to inhibit cell viability, colony formation and inhibits expression and activation of proteins involved in osimertinib-resistance and may represent an effective strategy for NSCLC with intrinsic resistance to osimertinib inhibition.	osimertinib	180-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
31361762-7	2019	Our results show that direct knockdown of endogenous Hsp90 significantly reduces the levels of REST and mutant Huntingtin, decreased the percentage of cells with mHtt in nucleus and rescued cells from mHtt-induced cellular cytotoxicity.	mhtt	162-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
31361762-7	2019	Our results show that direct knockdown of endogenous Hsp90 significantly reduces the levels of REST and mutant Huntingtin, decreased the percentage of cells with mHtt in nucleus and rescued cells from mHtt-induced cellular cytotoxicity.	mhtt	201-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
31361762-8	2019	Additionally Hsp90-specific inhibitors geldanamicyn and PUH71 dramatically reduced mHtt and REST levels, thereby providing neuroprotective activity.	mhtt	83-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
31263819-0	2019	Identification of HSP90 as a direct target of artemisinin for its anti-inflammatory activity via quantitative chemical proteomics.	artemisinin	46-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
31263819-3	2019	Further study revealed that ART suppressed the production of nitric oxide (NO) in macrophages via inhibiting the interaction between HSP90 and inducible NO synthase (iNOS).	Nitric Oxide	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
31051401-3	2019	The mechanism of pharmacological research indicated that 29 possessed the ability to disrupt Hsp90-Cdc37 complex which was stronger than celastrol.	celastrol	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
30982499-2	2019	In this study, nonsteroidal anti-inflammatory drugs (NSAIDs) significantly potentiated Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG)-mediated cytotoxicity through apoptotic and autophagic cell death induction, but COX-2-inhibitory function was not required for NSAID-induced autophagy in CD44-overexpressing human chronic myeloid leukemia K562 (CD44highK562) cells.	tanespimycin	103-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
31283755-0	2019	Global proteomic analyses define an environmentally contingent Hsp90 interactome and reveal chaperone-dependent regulation of stress granule proteins and the R2TP complex in a fungal pathogen.	r2tp	158-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31211865-4	2019	Recently, hormone receptor components for auxin and jasmonic acid, respectively, have been identified as clients of the HSP90 chaperone system, suggesting a direct HSP90-dependent link to hormone signaling.	Indoleacetic Acids	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
31211865-4	2019	Recently, hormone receptor components for auxin and jasmonic acid, respectively, have been identified as clients of the HSP90 chaperone system, suggesting a direct HSP90-dependent link to hormone signaling.	Indoleacetic Acids	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
31211865-4	2019	Recently, hormone receptor components for auxin and jasmonic acid, respectively, have been identified as clients of the HSP90 chaperone system, suggesting a direct HSP90-dependent link to hormone signaling.	jasmonic acid	52-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
31211865-4	2019	Recently, hormone receptor components for auxin and jasmonic acid, respectively, have been identified as clients of the HSP90 chaperone system, suggesting a direct HSP90-dependent link to hormone signaling.	jasmonic acid	52-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
31262015-4	2019	Geldanamycins interact with the Hsp-90 chaperone, a protein that has a key role in tumorigenesis of human cells.	geldanamycin	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-38
31311859-3	2019	Heme insertion into the beta1 subunit of sGC (sGCbeta) is critical for function, and heat shock protein 90 (HSP90) associates with heme-free sGCbeta (apo-sGCbeta) to drive its heme insertion.	Heme	131-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
31311859-3	2019	Heme insertion into the beta1 subunit of sGC (sGCbeta) is critical for function, and heat shock protein 90 (HSP90) associates with heme-free sGCbeta (apo-sGCbeta) to drive its heme insertion.	Heme	131-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
31311859-3	2019	Heme insertion into the beta1 subunit of sGC (sGCbeta) is critical for function, and heat shock protein 90 (HSP90) associates with heme-free sGCbeta (apo-sGCbeta) to drive its heme insertion.	Heme	176-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
31311859-3	2019	Heme insertion into the beta1 subunit of sGC (sGCbeta) is critical for function, and heat shock protein 90 (HSP90) associates with heme-free sGCbeta (apo-sGCbeta) to drive its heme insertion.	Heme	176-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
31311859-6	2019	Our findings uncover the molecular features of the cellular apo-sGCbeta-HSP90 complex and reveal its dual importance in enabling heme insertion while preventing inactive heterodimer formation during sGC maturation.	Heme	129-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
31534519-2	2019	Herein, we report that a cubic-shaped iron oxide nanoparticle (IONC) core nanobeacon is capable of delivering an HSP90alpha mRNA-specific molecular beacon (HSP90-MB) into living cells and enhancing T 2-weighted MR imaging in a tumor model.	ferric oxide	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-123
30989459-2	2019	Here, we reported that 17-aminogeldanamycin more potently activated caspase-3/7 in BRAFV600E melanoma cells than geldanamycin, another inhibitor of heat shock protein 90 (HSP90).	17-aminogeldanamycin	23-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-169
30989459-2	2019	Here, we reported that 17-aminogeldanamycin more potently activated caspase-3/7 in BRAFV600E melanoma cells than geldanamycin, another inhibitor of heat shock protein 90 (HSP90).	17-aminogeldanamycin	23-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
30989459-2	2019	Here, we reported that 17-aminogeldanamycin more potently activated caspase-3/7 in BRAFV600E melanoma cells than geldanamycin, another inhibitor of heat shock protein 90 (HSP90).	geldanamycin	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-169
30989459-2	2019	Here, we reported that 17-aminogeldanamycin more potently activated caspase-3/7 in BRAFV600E melanoma cells than geldanamycin, another inhibitor of heat shock protein 90 (HSP90).	geldanamycin	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
31071330-0	2019	AT-533, a Hsp90 inhibitor, attenuates HSV-1-induced inflammation.	at-533	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
31199053-2	2019	In the presence of stimulation by cobalt protoporphyrin (CoPP), an HO-1 inducer, apoptotic characteristics were observed, including DNA laddering, hypodiploid cells, and cleavages of caspase (Casp)-3 and poly(ADP) ribose polymerase (PARP) proteins in human colon carcinoma COLO205, HCT-15, LOVO and HT-29 cells in serum-free (SF) conditions with increased HO-1, but not heat shock protein 70 (HSP70) or HSP90.	cobaltiprotoporphyrin	34-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	403-408
31199053-2	2019	In the presence of stimulation by cobalt protoporphyrin (CoPP), an HO-1 inducer, apoptotic characteristics were observed, including DNA laddering, hypodiploid cells, and cleavages of caspase (Casp)-3 and poly(ADP) ribose polymerase (PARP) proteins in human colon carcinoma COLO205, HCT-15, LOVO and HT-29 cells in serum-free (SF) conditions with increased HO-1, but not heat shock protein 70 (HSP70) or HSP90.	cobaltiprotoporphyrin	57-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	403-408
30828931-1	2019	OBJECTIVES: Heat shock protein 90 (HSP90) contributes to cutaneous vasodilatation during exercise in the heat through nitric oxide (NO) synthase (NOS)-dependent mechanisms in young adults.	Nitric Oxide	118-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-33
30828931-1	2019	OBJECTIVES: Heat shock protein 90 (HSP90) contributes to cutaneous vasodilatation during exercise in the heat through nitric oxide (NO) synthase (NOS)-dependent mechanisms in young adults.	Nitric Oxide	118-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
31282114-3	2019	To solve these problems, a smart albumin-based tumor microenvironment-responsive nanoagent is designed via the self-assembly of human serum albumin (HSA), dc-IR825 (a cyanine dye and a photothermal agent), and gambogic acid (GA, a heat shock protein 90 (HSP90) inhibitor and an anticancer agent) to realize molecular targeting-mediated mild-temperature PTT.	dc-ir825	155-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-252
31282114-3	2019	To solve these problems, a smart albumin-based tumor microenvironment-responsive nanoagent is designed via the self-assembly of human serum albumin (HSA), dc-IR825 (a cyanine dye and a photothermal agent), and gambogic acid (GA, a heat shock protein 90 (HSP90) inhibitor and an anticancer agent) to realize molecular targeting-mediated mild-temperature PTT.	dc-ir825	155-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	254-259
31555510-0	2019	Hsp90 inhibitors enhance the antitumoral effect of osimertinib in parental and osimertinib-resistant non-small cell lung cancer cell lines.	osimertinib	51-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31555510-0	2019	Hsp90 inhibitors enhance the antitumoral effect of osimertinib in parental and osimertinib-resistant non-small cell lung cancer cell lines.	osimertinib	79-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31555510-7	2019	Hsp90 inhibitors, ganetespib and luminespib, inhibited cell viability and colony formation in H1975, PC9 and PC9-derived osimertinib-resistant cell lines and combination of these inhibitors with osimertinib achieved to enhance this cell viability and colony formation inhibition.	osimertinib	121-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31555510-7	2019	Hsp90 inhibitors, ganetespib and luminespib, inhibited cell viability and colony formation in H1975, PC9 and PC9-derived osimertinib-resistant cell lines and combination of these inhibitors with osimertinib achieved to enhance this cell viability and colony formation inhibition.	osimertinib	195-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31555510-11	2019	Conclusions: Hsp90 inhibitors and osimertinib exhibits a good efficiency to inhibit cell viability, colony formation and inhibits expression and activation of proteins involved in osimertinib-resistance and may represent an effective strategy for NSCLC with intrinsic resistance to osimertinib inhibition.	osimertinib	180-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
31370342-2	2019	To study responses to its inhibition, HSP90 was pharmacologically interrupted by geldanamycin and resorcinol derivatives or with combined inhibition of HSP90 plus HSP70 in lung adenocarcinoma cell lines.	geldanamycin	81-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
31370342-2	2019	To study responses to its inhibition, HSP90 was pharmacologically interrupted by geldanamycin and resorcinol derivatives or with combined inhibition of HSP90 plus HSP70 in lung adenocarcinoma cell lines.	resorcinol	98-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
31431614-2	2019	In this study, we delineate that KRAS-mutant lung cancer cells resistant to pemetrexed (MTA) and anti-MEK drug trametinib acquire an exquisite dependency on endoplasmic reticulum (ER) stress signaling, rendering resistant cancer cells selectively susceptible to blockage of HSP90, the receptor tyrosine kinase AXL, the eukaryotic translation initiation factor 4E (eIF4E), and the unfolded protein response (UPR).	trametinib	111-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	274-279
31431614-5	2019	In line with these findings, HSP90 inhibitors synergistically enhance antitumor effects of MTA and trametinib, validating a rational combination strategy to treat KRAS-mutant lung cancer.	trametinib	99-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
31185901-9	2019	Furthermore, the expression patterns of some genes (GSTM2, LY-6E, UMOD, ZNF593, CIRBP, HSP90) show interactive effects of temperature and corticosterone exposure, compared to each treatment alone.	Corticosterone	138-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
31163701-0	2019	Identification and Structure-Activity Studies of 1,3-Dibenzyl-2-aryl imidazolidines as Novel Hsp90 Inhibitors.	1,3-dibenzyl-2-aryl imidazolidines	49-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
31189925-1	2019	Complex conformational dynamics are essential for function of the dimeric molecular chaperone heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization that is necessary to attain ATPase competence.	Adenosine Triphosphate	146-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-115
31189925-1	2019	Complex conformational dynamics are essential for function of the dimeric molecular chaperone heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization that is necessary to attain ATPase competence.	Adenosine Triphosphate	146-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
31189925-2	2019	The intrinsic, but weak, ATP hydrolyzing activity of human Hsp90 is markedly enhanced by the co-chaperone Aha1.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
31189925-4	2019	Here we report that initial recruitment of this cochaperone to Hsp90 is markedly enhanced by phosphorylation of a highly conserved tyrosine (Y313 in Hsp90alpha) in the Hsp90 middle domain.	Tyrosine	131-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
31189925-4	2019	Here we report that initial recruitment of this cochaperone to Hsp90 is markedly enhanced by phosphorylation of a highly conserved tyrosine (Y313 in Hsp90alpha) in the Hsp90 middle domain.	Tyrosine	131-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-159
31189925-4	2019	Here we report that initial recruitment of this cochaperone to Hsp90 is markedly enhanced by phosphorylation of a highly conserved tyrosine (Y313 in Hsp90alpha) in the Hsp90 middle domain.	Tyrosine	131-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
31189925-5	2019	Importantly, phosphomimetic mutation of Y313 promotes formation of a transient complex in which both N- and C-domains of Aha1 bind to distinct surfaces of the middle domains of opposing Hsp90 protomers prior to ATP-directed N-domain dimerization.	y313	40-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
31189925-6	2019	Thus, Y313 represents a phosphorylation-sensitive conformational switch, engaged early after client loading, that affects both local and long-range conformational dynamics to facilitate initial recruitment of Aha1 to Hsp90.	y313	6-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	217-222
31163701-2	2019	In this work, a virtual screening strategy was employed, leading to the identification of a series of compounds bearing a scaffold of 1,3-dibenzyl-2-aryl imidazolidine as novel Hsp90 inhibitors.	1,3-dibenzyl-2-aryl imidazolidine	134-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
31163701-5	2019	The molecular docking study showed that these novel Hsp90 inhibitors bound to the adenosine triphosphate (ATP) binding site at the N-terminus of Hsp90.	Adenosine	82-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
31163701-5	2019	The molecular docking study showed that these novel Hsp90 inhibitors bound to the adenosine triphosphate (ATP) binding site at the N-terminus of Hsp90.	Adenosine	82-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
31163701-5	2019	The molecular docking study showed that these novel Hsp90 inhibitors bound to the adenosine triphosphate (ATP) binding site at the N-terminus of Hsp90.	Adenosine Triphosphate	106-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
31163701-5	2019	The molecular docking study showed that these novel Hsp90 inhibitors bound to the adenosine triphosphate (ATP) binding site at the N-terminus of Hsp90.	Adenosine Triphosphate	106-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
30985981-8	2019	Inhibition of Hsp90 by SNX-2112 induced the degradation of phosphorylated AKT and ERK1/2 in Caco2 and HRT18 cells.	SNX 2112	23-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
30797004-0	2019	Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: A comparative perspective.	adenosine nucleotides	57-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
30797004-5	2019	Accordingly, the goal of this work was to evaluate the interaction of either ADP or ATP with recombinant Hsp90s from different organisms (human alpha and beta isoforms, Plasmodium falciparum, Leishmania braziliensis, yeast and sugarcane) by isothermal titration calorimetry.	Adenosine Diphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
30797004-5	2019	Accordingly, the goal of this work was to evaluate the interaction of either ADP or ATP with recombinant Hsp90s from different organisms (human alpha and beta isoforms, Plasmodium falciparum, Leishmania braziliensis, yeast and sugarcane) by isothermal titration calorimetry.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
30797004-9	2019	Altogether, the data suggest that selective inhibition may be more easily achieved using analogues of the Hsp90-ADP bound state than those of Hsp90-ATP bound state.	Adenosine Diphosphate	112-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
30797004-9	2019	Altogether, the data suggest that selective inhibition may be more easily achieved using analogues of the Hsp90-ADP bound state than those of Hsp90-ATP bound state.	Adenosine Triphosphate	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
30985981-8	2019	Inhibition of Hsp90 by SNX-2112 induced the degradation of phosphorylated AKT and ERK1/2 in Caco2 and HRT18 cells.	caco2	92-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
31089638-4	2019	Additionally, inhibitory effects on human heat shock protein Hsp90alpha and bacterial heat shock protein from H. pylori HpHtpG were observed, revealing strong displacement properties for labelled ATP and demonstrating that the ATP-binding site of Hsps is the target site for the new geldanamycin derivatives.	Adenosine Triphosphate	196-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-71
31089638-4	2019	Additionally, inhibitory effects on human heat shock protein Hsp90alpha and bacterial heat shock protein from H. pylori HpHtpG were observed, revealing strong displacement properties for labelled ATP and demonstrating that the ATP-binding site of Hsps is the target site for the new geldanamycin derivatives.	Adenosine Triphosphate	227-230	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-71
31089638-4	2019	Additionally, inhibitory effects on human heat shock protein Hsp90alpha and bacterial heat shock protein from H. pylori HpHtpG were observed, revealing strong displacement properties for labelled ATP and demonstrating that the ATP-binding site of Hsps is the target site for the new geldanamycin derivatives.	geldanamycin	283-295	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-71
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Rifabutin	135-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Rifabutin	135-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Rifabutin	135-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Rifabutin	153-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Rifabutin	153-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
31113013-3	2019	HSP90 inhibitors mainly bind to the ATP binding site of HSP90 and inhibit HSP90 activity, and these inhibitors can be distinguished as ansamycin and non-ansamycin depending on the structure.	Rifabutin	153-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
30792306-0	2019	Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32.	Novobiocin	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36
31027879-5	2019	However, when Hsp90 and the adaptor protein Hop are present, p53 is transferred from Hsp70 to Hsp90, allowing restoration of the native state upon ATP hydrolysis.	Adenosine Triphosphate	147-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
31027879-5	2019	However, when Hsp90 and the adaptor protein Hop are present, p53 is transferred from Hsp70 to Hsp90, allowing restoration of the native state upon ATP hydrolysis.	Adenosine Triphosphate	147-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
30488605-0	2019	Targeting HSP90 with the small molecule inhibitor AUY922 (luminespib) as a treatment strategy against hepatocellular carcinoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	50-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
30488605-0	2019	Targeting HSP90 with the small molecule inhibitor AUY922 (luminespib) as a treatment strategy against hepatocellular carcinoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
30488605-8	2019	AUY922 treatment led to the upregulation of HSP70 and the simultaneous depletion of HSP90 client proteins.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
30857829-0	2019	Penicisulfuranol A, a novel C-terminal inhibitor disrupting molecular chaperone function of Hsp90 independent of ATP binding domain.	Penicisulfuranol A	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
30857829-1	2019	The goal of this study is to explore the mechanism of a heat shock protein 90 (Hsp90) C-terminal inhibitor, Penicisulfuranol A (PEN-A), for cancer therapy.	Penicisulfuranol A	108-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-77
30857829-1	2019	The goal of this study is to explore the mechanism of a heat shock protein 90 (Hsp90) C-terminal inhibitor, Penicisulfuranol A (PEN-A), for cancer therapy.	Penicisulfuranol A	108-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
30857829-7	2019	These inhibitory effects of PEN-A were similar to those of novobiocin, an inhibitor binding to interaction site for ATP of C-terminus of Hsp90.	Novobiocin	59-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
30857829-7	2019	These inhibitory effects of PEN-A were similar to those of novobiocin, an inhibitor binding to interaction site for ATP of C-terminus of Hsp90.	Adenosine Triphosphate	116-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
30857829-8	2019	Furthermore, our study revealed that disulfide bond was essential moiety for inhibition activity of PEN-A on Hsp90.	Disulfides	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
30857829-9	2019	This suggested that PEN-A may be bound to cysteine residues near amino acid region which was responsible for dimerization of Hsp90.	Cysteine	42-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
30989449-0	2019	HSP90 inhibitor DPB induces autophagy and more effectively apoptosis in A549 cells combined with autophagy inhibitors.	dpb	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30989449-1	2019	In our previous study, we proved that a novel Heat shock protein 90 (HSP90) inhibitor 4-(3-(7-(diethylamino)-2-oxo-2H-chromen-3-yl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl) benzoic acid (DPB) could inhibit A549 lung cancer cell growth via inducing apoptosis.	4-(3-(7-(diethylamino)-2-oxo-2h-chromen-3-yl)-5-phenyl-4,5-dihydro-1h-pyrazol-1-yl) benzoic acid	86-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
30989449-1	2019	In our previous study, we proved that a novel Heat shock protein 90 (HSP90) inhibitor 4-(3-(7-(diethylamino)-2-oxo-2H-chromen-3-yl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl) benzoic acid (DPB) could inhibit A549 lung cancer cell growth via inducing apoptosis.	4-(3-(7-(diethylamino)-2-oxo-2h-chromen-3-yl)-5-phenyl-4,5-dihydro-1h-pyrazol-1-yl) benzoic acid	86-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
30989449-1	2019	In our previous study, we proved that a novel Heat shock protein 90 (HSP90) inhibitor 4-(3-(7-(diethylamino)-2-oxo-2H-chromen-3-yl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl) benzoic acid (DPB) could inhibit A549 lung cancer cell growth via inducing apoptosis.	dpb	184-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
30989449-1	2019	In our previous study, we proved that a novel Heat shock protein 90 (HSP90) inhibitor 4-(3-(7-(diethylamino)-2-oxo-2H-chromen-3-yl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl) benzoic acid (DPB) could inhibit A549 lung cancer cell growth via inducing apoptosis.	dpb	184-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
30822403-5	2019	Both andrographolide and NCTU-322 downregulated the Bcr-Abl oncoprotein in imatinib-resistant CML cells through an Hsp90-dependent mechanism similar to that observed in imatinib-sensitive CML cells.	andrographolide	5-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
30822403-5	2019	Both andrographolide and NCTU-322 downregulated the Bcr-Abl oncoprotein in imatinib-resistant CML cells through an Hsp90-dependent mechanism similar to that observed in imatinib-sensitive CML cells.	nctu-322	25-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
30822403-6	2019	In addition, NCTU-322 had stronger effects than andrographolide on downregulation of Bcr-Abl oncoprotein, induction of Hsp90 cleavage and cytotoxicity of CML cells.	nctu-322	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
30792306-0	2019	Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32.	KU-32	95-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	KU-32	106-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	KU-32	106-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	Novobiocin	149-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	Novobiocin	149-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	Novobiocin	161-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
30792306-5	2019	Although NB and KU-32 differ only slightly in structure, we found that upon binding, they induce completely opposite conformational changes in Hsp90.	Novobiocin	9-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
30792306-5	2019	Although NB and KU-32 differ only slightly in structure, we found that upon binding, they induce completely opposite conformational changes in Hsp90.	KU-32	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
30792306-6	2019	We observed that NB and KU-32 both bind to the C-terminal domain of Hsp90, but surprisingly, KU-32 stimulated the chaperone functions of Hsp90 via allosteric modulation of its N-terminal domain, responsible for the chaperone"s ATPase activity.	Novobiocin	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
30792306-6	2019	We observed that NB and KU-32 both bind to the C-terminal domain of Hsp90, but surprisingly, KU-32 stimulated the chaperone functions of Hsp90 via allosteric modulation of its N-terminal domain, responsible for the chaperone"s ATPase activity.	Novobiocin	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
30792306-6	2019	We observed that NB and KU-32 both bind to the C-terminal domain of Hsp90, but surprisingly, KU-32 stimulated the chaperone functions of Hsp90 via allosteric modulation of its N-terminal domain, responsible for the chaperone"s ATPase activity.	KU-32	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
30792306-6	2019	We observed that NB and KU-32 both bind to the C-terminal domain of Hsp90, but surprisingly, KU-32 stimulated the chaperone functions of Hsp90 via allosteric modulation of its N-terminal domain, responsible for the chaperone"s ATPase activity.	KU-32	93-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
30792306-7	2019	In vitro and in silico studies indicated that upon KU-32 binding, Hsp90 undergoes global structural changes leading to the formation of a "partially closed" intermediate that selectively binds ATP and increases ATPase activity.	KU-32	51-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
30792306-7	2019	In vitro and in silico studies indicated that upon KU-32 binding, Hsp90 undergoes global structural changes leading to the formation of a "partially closed" intermediate that selectively binds ATP and increases ATPase activity.	Adenosine Triphosphate	193-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
30792306-8	2019	We also report that KU-32 promotes HeLa cell survival and enhances the refolding of an Hsp90 substrate inside the cell.	KU-32	20-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
30792306-9	2019	This discovery explains the effectiveness of KU-32 analogs in the management of neuropathies and may facilitate the design of molecules that promote cell survival by enhancing Hsp90 chaperone function and reducing the load of misfolded proteins in cells.	KU-32	45-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
30869872-0	2019	The Hsp90 Chaperone: 1H and 19F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme.	Hydrogen	21-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
30920570-0	2019	Polymer mediated transport of the Hsp90 inhibitor LB76, a polar cyclic peptide, produces an Hsp90 cellular phenotype.	Polymers	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
30920570-0	2019	Polymer mediated transport of the Hsp90 inhibitor LB76, a polar cyclic peptide, produces an Hsp90 cellular phenotype.	Polymers	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
30920570-0	2019	Polymer mediated transport of the Hsp90 inhibitor LB76, a polar cyclic peptide, produces an Hsp90 cellular phenotype.	lb76	50-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
30920570-0	2019	Polymer mediated transport of the Hsp90 inhibitor LB76, a polar cyclic peptide, produces an Hsp90 cellular phenotype.	lb76	50-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
30920570-1	2019	LB76 is a cyclic peptide that shows great promise as a selective heat shock protein 90 (Hsp90) inhibitor.	lb76	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-86
30920570-1	2019	LB76 is a cyclic peptide that shows great promise as a selective heat shock protein 90 (Hsp90) inhibitor.	lb76	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
30920570-5	2019	Treatment of human colon cancer HCT116 cells with nanoparticles laden with LB76 produces the typical phenotype associated with Hsp90 inhibition, providing evidence of a therapeutically active payload.	lb76	75-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
30869872-2	2019	Binding and hydrolysis of ATP by dimeric Hsp90 drive a conformational cycle characterized by fluctuations between a compact, N- and C-terminally dimerized catalytically competent closed state and a less compact open state that is largely C-terminally dimerized.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
30869872-3	2019	We used 19F and 1H dynamic nuclear magnetic resonance (NMR) spectroscopy to study the opening and closing kinetics of Hsp90 and to determine the kcat for ATP hydrolysis.	Hydrogen	16-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
30970250-5	2019	Testing the top candidates in C. elegans, we identified two Hsp90 inhibitors, monorden and tanespimycin, which extended the animals" lifespan and improved their health.	tanespimycin	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
30948782-3	2019	We show that the Hsp90 inhibitor 17-AAG eliminates R248Q by stimulating macroautophagy under normal growth conditions.	tanespimycin	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
30952716-2	2019	Ganetespib is a second-generation HSP90 inhibitor with a potent antitumor effect against various cancer types.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
30730850-0	2019	177Lu-octreotate therapy for neuroendocrine tumours is enhanced by Hsp90 inhibition.	177Lu-octreotate	0-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
30730850-6	2019	The potential for Hsp90 inhibitor ganetespib to enhance the anti-tumour effect of 177Lu-octreotate in an in vivo setting was studied in the somatostatin receptor-expressing GOT1 xenograft model.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
30730850-6	2019	The potential for Hsp90 inhibitor ganetespib to enhance the anti-tumour effect of 177Lu-octreotate in an in vivo setting was studied in the somatostatin receptor-expressing GOT1 xenograft model.	177Lu-octreotate	82-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
30730850-11	2019	We conclude that Hsp90 inhibitors enhance the tumour-killing effect of 177Lu-octreotate therapy synergistically in SINET tumour models and suggest that this potentially promising combination should be further evaluated.	177Lu-octreotate	71-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
30827868-5	2019	The molecular modeling of 57 demonstrated that 57 bound well to the C-terminal ATP-binding pocket in the open conformation of the hHSP90 homodimer with hydrogen bonding and pi-cation interactions.	Adenosine Triphosphate	79-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-136
30827868-5	2019	The molecular modeling of 57 demonstrated that 57 bound well to the C-terminal ATP-binding pocket in the open conformation of the hHSP90 homodimer with hydrogen bonding and pi-cation interactions.	Hydrogen	152-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-136
30015413-8	2019	Bclaf1 interacts with the C-terminal domain of Hsp90alpha, and this interaction is disrupted by the C-terminal domain inhibitor, novobiocin (NB), resulting in proteasome-dependent degradation of Bclaf1.	Novobiocin	129-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-57
30015413-8	2019	Bclaf1 interacts with the C-terminal domain of Hsp90alpha, and this interaction is disrupted by the C-terminal domain inhibitor, novobiocin (NB), resulting in proteasome-dependent degradation of Bclaf1.	Novobiocin	141-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-57
30015413-9	2019	Moreover, NB-induced disruption of Hsp90alpha-Bclaf1 interaction dampened the production of mature c-MYC mRNA and attenuated tumor cell growth in vitro and in vivo.	Novobiocin	10-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-45
30335904-6	2019	Interestingly, increased levels of NA in the presence of Hsp90 was observed, which tends to decrease if adenosine triphosphatase activity of Hsp90 is inhibited using 17-N-allylamino-17-demethoxygeldanamycin (17AAG).	tanespimycin	166-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
30335904-6	2019	Interestingly, increased levels of NA in the presence of Hsp90 was observed, which tends to decrease if adenosine triphosphatase activity of Hsp90 is inhibited using 17-N-allylamino-17-demethoxygeldanamycin (17AAG).	tanespimycin	166-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
30335904-6	2019	Interestingly, increased levels of NA in the presence of Hsp90 was observed, which tends to decrease if adenosine triphosphatase activity of Hsp90 is inhibited using 17-N-allylamino-17-demethoxygeldanamycin (17AAG).	tanespimycin	208-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
30335904-6	2019	Interestingly, increased levels of NA in the presence of Hsp90 was observed, which tends to decrease if adenosine triphosphatase activity of Hsp90 is inhibited using 17-N-allylamino-17-demethoxygeldanamycin (17AAG).	tanespimycin	208-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
30976475-3	2019	In this study, we designed and synthesized a series of novel triazine derivatives (A1-26, B1-13, C1-23) as Hsp90 inhibitors.	Triazines	61-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
30866043-7	2019	Cotreatment of neferine and imatinib significantly decreased the expression of BCR-ABL protein and its molecular chaperone heat shock protein 90 (Hsp90) mRNA and protein levels, and further decreased phospho-extracellular regulated protein kinase 1/2 (p-Erk1/2) and myeloid cell leukemia (Mcl-1) expression.	neferine	15-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
30866043-7	2019	Cotreatment of neferine and imatinib significantly decreased the expression of BCR-ABL protein and its molecular chaperone heat shock protein 90 (Hsp90) mRNA and protein levels, and further decreased phospho-extracellular regulated protein kinase 1/2 (p-Erk1/2) and myeloid cell leukemia (Mcl-1) expression.	Imatinib Mesylate	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-144
30866043-7	2019	Cotreatment of neferine and imatinib significantly decreased the expression of BCR-ABL protein and its molecular chaperone heat shock protein 90 (Hsp90) mRNA and protein levels, and further decreased phospho-extracellular regulated protein kinase 1/2 (p-Erk1/2) and myeloid cell leukemia (Mcl-1) expression.	Imatinib Mesylate	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
30796972-0	2019	Inhibition of thymidine phosphorylase expression by Hsp90 inhibitor potentiates the cytotoxic effect of salinomycin in human non-small-cell lung cancer cells.	salinomycin	104-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
30796972-4	2019	In this study, we report whether Hsp90 inhibitor 17-AAG could enhance salinomycin-induced cytotoxicity in NSCLC cells through modulating TP expression in two non-small-cell lung cancer (NSCLC) cell lines, A549 and H1975.	salinomycin	70-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
30796972-8	2019	Moreover, Hsp90 inhibitor 17-AAG enhanced cytotoxicity and cell growth inhibition of salinomycin in NSCLC cells, which were associated with down-regulation of TP expression and inactivation of p38 MAPK.	salinomycin	85-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
30796972-9	2019	Together, the Hsp90 inhibition induced TP down-regulation involved in enhancing the salinomycin-induced cytotoxicity in A549 and H1975 cells.	salinomycin	84-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
30925862-0	2019	PGK1 facilities cisplatin chemoresistance by triggering HSP90/ERK pathway mediated DNA repair and methylation in endometrial endometrioid adenocarcinoma.	Cisplatin	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
30925862-14	2019	CONCLUSIONS: We propose that PGK1 mediates DNA repair and methylation through the HSP90/ERK pathway, and eventually enhances the chemoresistance to cisplatin.	Cisplatin	148-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
31019655-0	2019	Hsp90 Inhibitor SNX-2112 Enhances TRAIL-Induced Apoptosis of Human Cervical Cancer Cells via the ROS-Mediated JNK-p53-Autophagy-DR5 Pathway.	SNX 2112	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31217782-0	2019	The effect of heat shock protein 90 inhibitors on histone 4 lysine 20 methylation in bladder cancer.	Lysine	60-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
31217782-1	2019	Heat shock protein 90 (HSP90), an ATP-dependent molecular chaperone required for the stability and function of numerous oncogenic signaling, is one of the hallmarks of cancer.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
31217782-1	2019	Heat shock protein 90 (HSP90), an ATP-dependent molecular chaperone required for the stability and function of numerous oncogenic signaling, is one of the hallmarks of cancer.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
30866043-7	2019	Cotreatment of neferine and imatinib significantly decreased the expression of BCR-ABL protein and its molecular chaperone heat shock protein 90 (Hsp90) mRNA and protein levels, and further decreased phospho-extracellular regulated protein kinase 1/2 (p-Erk1/2) and myeloid cell leukemia (Mcl-1) expression.	neferine	15-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-144
31019655-0	2019	Hsp90 Inhibitor SNX-2112 Enhances TRAIL-Induced Apoptosis of Human Cervical Cancer Cells via the ROS-Mediated JNK-p53-Autophagy-DR5 Pathway.	Reactive Oxygen Species	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
31019655-4	2019	In this study, we combined TRAIL with SNX-2112, an Hsp90 inhibitor we previously developed, to explore the effect and mechanism that SNX-2112 enhanced TRAIL-induced apoptosis in cervical cancer cells.	SNX 2112	38-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
30858416-0	2019	Physical plasma-triggered ROS induces tumor cell death upon cleavage of HSP90 chaperone.	ros	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
30858416-3	2019	Here we report that treatment of cancer cells with cold physical plasma, an emerging and less aggressive tumor therapy, resulted in ROS generation which subsequently triggered the cleavage of HSP90.	ros	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	192-197
30718432-4	2019	In this study, we identified 2-amino-5-chloro-N,3-dimethylbenzamide (CDDO), a compound known to inhibit heat shock protein 90 (HSP90), as an inhibitor of necroptosis that could also inhibit ferroptosis.	2-Amino-5-Chloro-N,3-Dimethylbenzamide	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-125
30679388-0	2019	First-in-Human Phase I Study of an Oral HSP90 Inhibitor, TAS-116, in Patients with Advanced Solid Tumors.	TAS-116	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
30679388-2	2019	This study was conducted to define the MTD, safety, pharmacokinetics, pharmacodynamics, and preliminary antitumor efficacy of TAS-116, a novel class, orally available, highly selective inhibitor of HSP90.	TAS-116	126-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
30679388-13	2019	TAS-116 had an acceptable safety profile with some antitumor activity, supporting further development of this HSP90 inhibitor.This is a result from a first-in-human study, in which the HSP90 inhibitor TAS-116 demonstrated preliminary antitumor efficacy in patients with advanced solid tumors, including those with heavily pretreated GIST.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
30679388-13	2019	TAS-116 had an acceptable safety profile with some antitumor activity, supporting further development of this HSP90 inhibitor.This is a result from a first-in-human study, in which the HSP90 inhibitor TAS-116 demonstrated preliminary antitumor efficacy in patients with advanced solid tumors, including those with heavily pretreated GIST.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
30679388-13	2019	TAS-116 had an acceptable safety profile with some antitumor activity, supporting further development of this HSP90 inhibitor.This is a result from a first-in-human study, in which the HSP90 inhibitor TAS-116 demonstrated preliminary antitumor efficacy in patients with advanced solid tumors, including those with heavily pretreated GIST.	TAS-116	201-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
30679388-13	2019	TAS-116 had an acceptable safety profile with some antitumor activity, supporting further development of this HSP90 inhibitor.This is a result from a first-in-human study, in which the HSP90 inhibitor TAS-116 demonstrated preliminary antitumor efficacy in patients with advanced solid tumors, including those with heavily pretreated GIST.	TAS-116	201-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
30639261-6	2019	At the molecular level, YZ129 directly engaged HSP90 to antagonize its chaperoning effect on calcineurin to abrogate NFAT nuclear translocation, and also suppressed other proto-oncogenic pathways including hypoxia, glycolysis, and the PI3K/AKT/mTOR signaling axis.	YZ129	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
30536958-2	2019	Functional HSP90 is required for the stability of AKT, a serine-threonine kinase phosphorylated in response to growth factor stimulation.	Serine	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
30536958-6	2019	We show that in vitro treatment of PML/RARA expressing cells with all-trans retinoic acid (ATRA) up-regulates HSP90 expression and stabilizes AKT.	Tretinoin	76-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
30536958-6	2019	We show that in vitro treatment of PML/RARA expressing cells with all-trans retinoic acid (ATRA) up-regulates HSP90 expression and stabilizes AKT.	Tretinoin	91-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
30536958-7	2019	Addition of the HSP90-inhibitor 17-(allylamino)-17-demethoxygeldanamycin in combination with ATRA, blocks upregulation of AKT protein, indicating that HSP90 is necessary for ATRA action on AKT.	tanespimycin	32-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
30536958-7	2019	Addition of the HSP90-inhibitor 17-(allylamino)-17-demethoxygeldanamycin in combination with ATRA, blocks upregulation of AKT protein, indicating that HSP90 is necessary for ATRA action on AKT.	tanespimycin	32-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
30536958-7	2019	Addition of the HSP90-inhibitor 17-(allylamino)-17-demethoxygeldanamycin in combination with ATRA, blocks upregulation of AKT protein, indicating that HSP90 is necessary for ATRA action on AKT.	Tretinoin	93-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
30536958-7	2019	Addition of the HSP90-inhibitor 17-(allylamino)-17-demethoxygeldanamycin in combination with ATRA, blocks upregulation of AKT protein, indicating that HSP90 is necessary for ATRA action on AKT.	Tretinoin	174-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
30536958-7	2019	Addition of the HSP90-inhibitor 17-(allylamino)-17-demethoxygeldanamycin in combination with ATRA, blocks upregulation of AKT protein, indicating that HSP90 is necessary for ATRA action on AKT.	Tretinoin	174-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
30659446-3	2019	Here, we demonstrated that the digestion of heparan sulfate (HS) moieties of HSPGs with a heparinase I/III blend and the metabolic inhibition of the sulfation of HS chains by sodium chlorate considerably impair the migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells stimulated by extracellular native Hsp90.	Heparitin Sulfate	44-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	331-336
30659446-3	2019	Here, we demonstrated that the digestion of heparan sulfate (HS) moieties of HSPGs with a heparinase I/III blend and the metabolic inhibition of the sulfation of HS chains by sodium chlorate considerably impair the migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells stimulated by extracellular native Hsp90.	Heparitin Sulfate	61-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	331-336
30659446-3	2019	Here, we demonstrated that the digestion of heparan sulfate (HS) moieties of HSPGs with a heparinase I/III blend and the metabolic inhibition of the sulfation of HS chains by sodium chlorate considerably impair the migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells stimulated by extracellular native Hsp90.	Heparitin Sulfate	77-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	331-336
30659446-3	2019	Here, we demonstrated that the digestion of heparan sulfate (HS) moieties of HSPGs with a heparinase I/III blend and the metabolic inhibition of the sulfation of HS chains by sodium chlorate considerably impair the migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells stimulated by extracellular native Hsp90.	sodium chlorate	175-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	331-336
30659446-4	2019	Heparin, a polysaccharide closely related to HS, also reduced the Hsp90-stimulated migration and invasion of cells.	Heparin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
30659446-4	2019	Heparin, a polysaccharide closely related to HS, also reduced the Hsp90-stimulated migration and invasion of cells.	Polysaccharides	11-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
30659446-6	2019	On the other hand, the downstream phosphorylation of AKT in response to extracellular Hsp90 was substantially impaired in heparinase- and chlorate-treated cells as compared to untreated cells.	Chlorates	138-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
30988998-4	2019	In this study, the expression of HSP90 isoforms including HSP90alpha and HSP90beta in breast cancer cell lines before and after treatment with doxorubicin (DOX) was assessed.	Doxorubicin	143-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
30988998-4	2019	In this study, the expression of HSP90 isoforms including HSP90alpha and HSP90beta in breast cancer cell lines before and after treatment with doxorubicin (DOX) was assessed.	Doxorubicin	156-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
30988998-9	2019	The immunofluorescence results indicated that the expression of HSP90alpha in both cell lines decreased after exposure to DOX.	Doxorubicin	122-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-74
30988998-11	2019	Conclusion: The obtained results suggested that HSP90alpha and HSP90beta expression levels were reduced in the MCF-7 cells after exposure to DOX.	Doxorubicin	141-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-58
30718432-4	2019	In this study, we identified 2-amino-5-chloro-N,3-dimethylbenzamide (CDDO), a compound known to inhibit heat shock protein 90 (HSP90), as an inhibitor of necroptosis that could also inhibit ferroptosis.	2-Amino-5-Chloro-N,3-Dimethylbenzamide	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
30718432-4	2019	In this study, we identified 2-amino-5-chloro-N,3-dimethylbenzamide (CDDO), a compound known to inhibit heat shock protein 90 (HSP90), as an inhibitor of necroptosis that could also inhibit ferroptosis.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	69-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-125
30718432-4	2019	In this study, we identified 2-amino-5-chloro-N,3-dimethylbenzamide (CDDO), a compound known to inhibit heat shock protein 90 (HSP90), as an inhibitor of necroptosis that could also inhibit ferroptosis.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	69-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
30718432-6	2019	We showed that inhibition of HSP90 by CDDO blocked necroptosis by inhibiting the activation of RIPK1 kinase.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	38-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
30694071-4	2019	The synthetic utility of this protocol is demonstrated by a gram-scale reaction and syntheses toward indole alkaloids and a HSP90 inhibitor.	Indole Alkaloids	101-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
30733455-6	2019	We probe the open conformation of human Hsp90alpha for druggable sites that overlap with these allosteric control elements, and identify three putative natural compound allosteric modulators: Cephalostatin 17, 20(29)-Lupene-3beta-isoferulate and 3"-Bromorubrolide F.	cephalostatin	192-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-50
30733455-6	2019	We probe the open conformation of human Hsp90alpha for druggable sites that overlap with these allosteric control elements, and identify three putative natural compound allosteric modulators: Cephalostatin 17, 20(29)-Lupene-3beta-isoferulate and 3"-Bromorubrolide F.	lupene-3beta-isoferulate	217-241	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-50
30733455-6	2019	We probe the open conformation of human Hsp90alpha for druggable sites that overlap with these allosteric control elements, and identify three putative natural compound allosteric modulators: Cephalostatin 17, 20(29)-Lupene-3beta-isoferulate and 3"-Bromorubrolide F.	3''-bromorubrolide F	246-265	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-50
30548820-3	2019	Based on our previous discovery that marine alkaloid analogues with a 4,5,6,7-tetrahydrobenzo[1,2-d]thiazole-2-amine structure show inhibition of HCV replication and binding to Hsp90, a series of twelve novel compounds based on this scaffold was designed and synthesized.	4,5,6,7-tetrahydrobenzo[1,2-d]thiazole-2-amine	70-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
30677285-3	2019	The material was then loaded with phenolic epigallocatechin 3-gallate (EGCG), which is a natural heat-shock protein 90 (HSP90) inhibitor.	phenolic epigallocatechin 3-gallate	34-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-118
30677285-3	2019	The material was then loaded with phenolic epigallocatechin 3-gallate (EGCG), which is a natural heat-shock protein 90 (HSP90) inhibitor.	phenolic epigallocatechin 3-gallate	34-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
30677285-3	2019	The material was then loaded with phenolic epigallocatechin 3-gallate (EGCG), which is a natural heat-shock protein 90 (HSP90) inhibitor.	epigallocatechin gallate	71-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-118
30677285-3	2019	The material was then loaded with phenolic epigallocatechin 3-gallate (EGCG), which is a natural heat-shock protein 90 (HSP90) inhibitor.	epigallocatechin gallate	71-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
30677285-4	2019	Upon near infrared irradiation, EGCG was released from the Lu:Nd@NiS2-EGCG, which bound HSP90 and reduced cell tolerance to heat, resulting in a better therapeutic effect at the same elevated temperature.	epigallocatechin gallate	32-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
30677285-4	2019	Upon near infrared irradiation, EGCG was released from the Lu:Nd@NiS2-EGCG, which bound HSP90 and reduced cell tolerance to heat, resulting in a better therapeutic effect at the same elevated temperature.	nis2	65-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
30677285-4	2019	Upon near infrared irradiation, EGCG was released from the Lu:Nd@NiS2-EGCG, which bound HSP90 and reduced cell tolerance to heat, resulting in a better therapeutic effect at the same elevated temperature.	epigallocatechin gallate	70-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
30575826-3	2019	Compound LB76, which was created from an Hsp90 co-chaperone, selectively pulls down Hsp90 from cell lysates, binds to Hsp90"s C-terminal domain, and blocks the interactions between Hsp90 and TPR-containing co-chaperones.	lb76	9-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
30640172-0	2019	HSP90 inhibitor geldanamycin reverts IL-13- and IL-17-induced airway goblet cell metaplasia.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30640172-3	2019	A perturbation-response profile connectivity approach identified geldanamycin, an inhibitor of heat shock protein 90 (HSP90) as a candidate therapeutic target.	geldanamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-116
30640172-3	2019	A perturbation-response profile connectivity approach identified geldanamycin, an inhibitor of heat shock protein 90 (HSP90) as a candidate therapeutic target.	geldanamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
30660959-6	2019	Here, we demonstrate that upon oxidative stress Hsp90 loses its function in a highly specific non-enzymatic iron-catalyzed oxidation event and its breakdown product, a cleaved form of Hsp90 (Hsp90cl), acquires a new function in mediating the accumulation of actin aggregates.	Iron	108-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
30660959-6	2019	Here, we demonstrate that upon oxidative stress Hsp90 loses its function in a highly specific non-enzymatic iron-catalyzed oxidation event and its breakdown product, a cleaved form of Hsp90 (Hsp90cl), acquires a new function in mediating the accumulation of actin aggregates.	Iron	108-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
30660959-6	2019	Here, we demonstrate that upon oxidative stress Hsp90 loses its function in a highly specific non-enzymatic iron-catalyzed oxidation event and its breakdown product, a cleaved form of Hsp90 (Hsp90cl), acquires a new function in mediating the accumulation of actin aggregates.	Iron	108-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-198
30267260-3	2019	Here, these two variants were mainly retained in cytoplasm with HSP90 and importin alpha in the presence of dihydrotestosterone (DHT), and their levels in nucleus were significantly reduced, according to the immunofluorescence staining.	Dihydrotestosterone	108-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
30267260-3	2019	Here, these two variants were mainly retained in cytoplasm with HSP90 and importin alpha in the presence of dihydrotestosterone (DHT), and their levels in nucleus were significantly reduced, according to the immunofluorescence staining.	Dihydrotestosterone	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
30267260-5	2019	However, the binding affinities of two AR variants for HSP90 were increased in the absence of DHT compared with WT-AR, which functioned to maintain spatial structural stability, particularly for the deletion-AR (Del-AR).	Dihydrotestosterone	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
30699359-4	2019	We show that casein kinase-2 phosphorylation of the co-chaperone folliculin-interacting protein 1 (FNIP1) on priming serine-938 and subsequent relay phosphorylation on serine-939, 941, 946, and 948 promotes its gradual interaction with Hsp90.	Serine	168-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
30699359-7	2019	This process antagonizes phosphorylation of FNIP1, preventing its interaction with Hsp90, and consequently promotes FNIP1 lysine-1119 ubiquitination and proteasomal degradation.	Lysine	122-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
30570197-0	2019	Synthesis of the seco-Limonoid BCD Ring System Identifies a Hsp90 Chaperon Machinery (p23) Inhibitor.	seco-limonoid	17-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
30570197-1	2019	D-Ring-seco-limonoids (tetranortriterpenoids), such as gedunin and xylogranin B display anti-cancer activity, acting via inhibition of Hsp90 and/or associated chaperon machinery (e.g., p23).	Limonins	11-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
30570197-1	2019	D-Ring-seco-limonoids (tetranortriterpenoids), such as gedunin and xylogranin B display anti-cancer activity, acting via inhibition of Hsp90 and/or associated chaperon machinery (e.g., p23).	Limonins	23-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
30678647-4	2019	METHODS: We developed models of acquired resistance to HSP90i by prolonged exposure of TNBC cells to HSP90i (ganetespib) in vitro.	STA 9090	109-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
30788006-0	2019	HSP90 inhibitor 17-DMAG effectively alleviated the progress of thoracic aortic dissection by suppressing smooth muscle cell phenotypic switch.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	16-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30788006-5	2019	In a beta-aminopropionitrile fumarate-induced AD mice model, 17-DMAG, a HSP90-inhibitor, effectively reduced the incidence and mortality of TAD.	beta-aminopropionitrile fumarate	5-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
30788006-5	2019	In a beta-aminopropionitrile fumarate-induced AD mice model, 17-DMAG, a HSP90-inhibitor, effectively reduced the incidence and mortality of TAD.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
30625143-8	2019	Finally, combining all the data, we calculated a ranked list of drugs that identified tanespimycin, an inhibitor of HSP-90, as the top-ranked novel anti-ageing candidate.	tanespimycin	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-122
30625143-9	2019	We experimentally validated the pro-longevity effect of tanespimycin through its HSP-90 target in Caenorhabditis elegans.	tanespimycin	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-87
30391349-2	2019	Pentamidine, an antiprotozoal drug, causes QT prolongation/Torsades de Pointes (TdP) via hERG trafficking inhibition, but 17-AAG, a geldanamycin derivative heat shock protein 90 (Hsp90) inhibitor, has not shown torsadogenic potential clinically, despite Hsp90 inhibitors generally being hypothesized to cause TdP by hERG trafficking inhibition.	Pentamidine	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	254-259
30391349-2	2019	Pentamidine, an antiprotozoal drug, causes QT prolongation/Torsades de Pointes (TdP) via hERG trafficking inhibition, but 17-AAG, a geldanamycin derivative heat shock protein 90 (Hsp90) inhibitor, has not shown torsadogenic potential clinically, despite Hsp90 inhibitors generally being hypothesized to cause TdP by hERG trafficking inhibition.	geldanamycin	132-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-177
31642416-0	2019	Effect of the Hsp90 Inhibitor KW-2478 on HepG2 Cells.	KW-2478	30-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
30485473-0	2019	Fe3 O4 nanoparticles mediated synthesis of novel spirooxindole-dihydropyrimidinone molecules as Hsp90 inhibitors.	spirooxindole-dihydropyrimidinone	49-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
30485473-2	2019	The current study illustrates the synthesis of novel spirooxindole-dihydropyrimidinones (4a-j) by Fe3 O4 nanoparticles intervened synthesis and their Hsp90 ATPase inhibitory activity was investigated by the malachite green assay.	spirooxindole-dihydropyrimidinones	53-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
30575826-3	2019	Compound LB76, which was created from an Hsp90 co-chaperone, selectively pulls down Hsp90 from cell lysates, binds to Hsp90"s C-terminal domain, and blocks the interactions between Hsp90 and TPR-containing co-chaperones.	lb76	9-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
30575826-3	2019	Compound LB76, which was created from an Hsp90 co-chaperone, selectively pulls down Hsp90 from cell lysates, binds to Hsp90"s C-terminal domain, and blocks the interactions between Hsp90 and TPR-containing co-chaperones.	lb76	9-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
30575826-3	2019	Compound LB76, which was created from an Hsp90 co-chaperone, selectively pulls down Hsp90 from cell lysates, binds to Hsp90"s C-terminal domain, and blocks the interactions between Hsp90 and TPR-containing co-chaperones.	lb76	9-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
30575826-4	2019	Through these interactions, LB76 inhibits the protein-folding function of Hsp90.	lb76	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
31486323-0	2019	C-Terminal HSP90 Inhibitors Block the HIF-1 Hypoxic Response by Degrading HIF-1alpha through the Oxygen-Dependent Degradation Pathway.	Oxygen	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
30602623-0	2019	Correction: Silencing of HSP90 Cochaperone AHA1 Expression Decreases Client Protein Activation and Increases Cellular Sensitivity to the HSP90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin.	tanespimycin	153-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
30602623-0	2019	Correction: Silencing of HSP90 Cochaperone AHA1 Expression Decreases Client Protein Activation and Increases Cellular Sensitivity to the HSP90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin.	tanespimycin	153-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
31486323-4	2019	SM molecules are HSP90 inhibitors that bind to the C-terminus of HSP90 and do not induce a heat shock response.	Samarium	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
31486323-4	2019	SM molecules are HSP90 inhibitors that bind to the C-terminus of HSP90 and do not induce a heat shock response.	Samarium	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
31486323-12	2019	Surprisingly, we found that when the C-terminal of HSP90 is inhibited, HIF-1alpha degradation occurs through the proteasome and prolyl hydroxylases in an oxygen-dependent manner even in very low levels of oxygen (tumor hypoxia levels).	Oxygen	154-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
31486323-12	2019	Surprisingly, we found that when the C-terminal of HSP90 is inhibited, HIF-1alpha degradation occurs through the proteasome and prolyl hydroxylases in an oxygen-dependent manner even in very low levels of oxygen (tumor hypoxia levels).	Oxygen	205-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
31244417-4	2019	Recently, it has motivated an interest in Hsp90 inhibitors that bind to the N-terminal or C-terminal ATP pocket as antitumor drugs.	Adenosine Triphosphate	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
30067876-5	2019	Combining catalytic suppression by the F-TKI BGJ398 with HSP90 blockade by ganetespib suppressed FGFR2-TACC3 (transforming acidic coiled-coil containing protein 3) signaling in cultured cells more effectively than either BGJ398 or ganetespib in isolation.	STA 9090	75-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
30067876-5	2019	Combining catalytic suppression by the F-TKI BGJ398 with HSP90 blockade by ganetespib suppressed FGFR2-TACC3 (transforming acidic coiled-coil containing protein 3) signaling in cultured cells more effectively than either BGJ398 or ganetespib in isolation.	STA 9090	231-241	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
30448425-4	2019	Here, we aim to investigate the effect of the HSP90 inhibitor ganetespib on microglial pro-inflammatory responses following heat shock.	STA 9090	62-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
30448425-9	2019	Taken together, our findings demonstrate that the HSP90 inhibitor ganetespib blocks pro-inflammatory responses in heat shock-treated N9 cells via a signalling mechanism involving HSP90beta and STAT3.	STA 9090	66-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
30745823-0	2019	Verteporfin blocks Clusterin which is required for survival of gastric cancer stem cell by modulating HSP90 function.	Verteporfin	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
30745823-7	2019	Furthermore, by screening a collection of drugs/inhibitors, we found that verteporfin (VP), a phototherapy drug, blocked clusterin gene expression, decreased the HSP90 client proteins and caused cell death of GCSC.	Verteporfin	74-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
30745823-7	2019	Furthermore, by screening a collection of drugs/inhibitors, we found that verteporfin (VP), a phototherapy drug, blocked clusterin gene expression, decreased the HSP90 client proteins and caused cell death of GCSC.	Verteporfin	87-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
29374544-6	2019	Using isothermal titration calorimetry it could be demonstrated that phosphorylation reduces the binding affinity of OM64 to Hsp90.	om64	117-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
30365122-0	2019	Vorinostat enhances gefitinib-induced cell death through reactive oxygen species-dependent cleavage of HSP90 and its clients in non-small cell lung cancer with the EGFR mutation.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
30365122-0	2019	Vorinostat enhances gefitinib-induced cell death through reactive oxygen species-dependent cleavage of HSP90 and its clients in non-small cell lung cancer with the EGFR mutation.	Gefitinib	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
30365122-0	2019	Vorinostat enhances gefitinib-induced cell death through reactive oxygen species-dependent cleavage of HSP90 and its clients in non-small cell lung cancer with the EGFR mutation.	Reactive Oxygen Species	57-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
30365122-5	2019	The addition of 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, a scavenger of reactive oxygen species (ROS), inhibited the degradation of HSP90 client proteins and HSP90 cleavage that was induced by co-treatment as well as the cleavage of caspase-3, caspase-8, and caspase-9 and cell death.	4-(2-aminoethyl)benzenesulfonylfluoride	16-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
30365122-5	2019	The addition of 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, a scavenger of reactive oxygen species (ROS), inhibited the degradation of HSP90 client proteins and HSP90 cleavage that was induced by co-treatment as well as the cleavage of caspase-3, caspase-8, and caspase-9 and cell death.	4-(2-aminoethyl)benzenesulfonylfluoride	16-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
30365122-5	2019	The addition of 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, a scavenger of reactive oxygen species (ROS), inhibited the degradation of HSP90 client proteins and HSP90 cleavage that was induced by co-treatment as well as the cleavage of caspase-3, caspase-8, and caspase-9 and cell death.	Reactive Oxygen Species	88-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
30365122-5	2019	The addition of 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, a scavenger of reactive oxygen species (ROS), inhibited the degradation of HSP90 client proteins and HSP90 cleavage that was induced by co-treatment as well as the cleavage of caspase-3, caspase-8, and caspase-9 and cell death.	Reactive Oxygen Species	88-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
30365122-5	2019	The addition of 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, a scavenger of reactive oxygen species (ROS), inhibited the degradation of HSP90 client proteins and HSP90 cleavage that was induced by co-treatment as well as the cleavage of caspase-3, caspase-8, and caspase-9 and cell death.	Reactive Oxygen Species	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
30365122-5	2019	The addition of 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, a scavenger of reactive oxygen species (ROS), inhibited the degradation of HSP90 client proteins and HSP90 cleavage that was induced by co-treatment as well as the cleavage of caspase-3, caspase-8, and caspase-9 and cell death.	Reactive Oxygen Species	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
30365122-7	2019	These results revealed that co-treatment with vorinostat and gefitinib induced ROS-dependent caspase activation, leading to the downregulation of HSP90 clients through HSP90 cleavage.	Vorinostat	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
30365122-7	2019	These results revealed that co-treatment with vorinostat and gefitinib induced ROS-dependent caspase activation, leading to the downregulation of HSP90 clients through HSP90 cleavage.	Vorinostat	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
30365122-7	2019	These results revealed that co-treatment with vorinostat and gefitinib induced ROS-dependent caspase activation, leading to the downregulation of HSP90 clients through HSP90 cleavage.	Gefitinib	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
30365122-7	2019	These results revealed that co-treatment with vorinostat and gefitinib induced ROS-dependent caspase activation, leading to the downregulation of HSP90 clients through HSP90 cleavage.	Gefitinib	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
30365122-7	2019	These results revealed that co-treatment with vorinostat and gefitinib induced ROS-dependent caspase activation, leading to the downregulation of HSP90 clients through HSP90 cleavage.	Reactive Oxygen Species	79-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
30929564-5	2019	Here, we tested the hypothesis that targeted inhibition of HSP90 with a small-molecule inhibitor ganetespib would sensitize non-BRCA mutant ovarian carcinoma (OC) cells to PARP inhibition by talazoparib.	STA 9090	97-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
30929564-5	2019	Here, we tested the hypothesis that targeted inhibition of HSP90 with a small-molecule inhibitor ganetespib would sensitize non-BRCA mutant ovarian carcinoma (OC) cells to PARP inhibition by talazoparib.	talazoparib	191-202	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
30929564-7	2019	Ganetespib treatment destabilized HSP90 client proteins involved in DNA damage response and cell cycle checkpoint, and disrupted gamma-irradiation-induced DNA repair.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
30262098-3	2019	In this work, a novel immunoaffinity probe, Fe3O4@TpBD-DSS-Ab-MEG, based on magnetic COFs with ordered arrangement of anchored antibodies has been developed and applied for the first time to detection of a cancer biomarker, heat shock protein 90alpha (Hsp90alpha).	ferryl iron	44-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	252-262
30262098-5	2019	Fe3O4@TpBD-DSS-Ab-MEG demonstrated low detection limit (50 pg/mL), high selectivity (Hsp90alpha:BSA = 1:1000), desirable repeatability and good stability for Hsp90alpha immunocapture.	ferryl iron	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-95
30262098-5	2019	Fe3O4@TpBD-DSS-Ab-MEG demonstrated low detection limit (50 pg/mL), high selectivity (Hsp90alpha:BSA = 1:1000), desirable repeatability and good stability for Hsp90alpha immunocapture.	ferryl iron	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-168
33093687-0	2019	The succinct synthesis of AT13387, a clinically relevant Hsp90 inhibitor.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	26-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
30647839-0	2018	MEK-inhibitor PD184352 enhances the radiosensitizing effect of the Hsp90 inhibitor NVP-AUY922: the role of cell type and drug-irradiation schedule.	2-(2-chloro-4-iodophenylamino)-N-cyclopropylmethoxy-3,4-difluorobenzamide	14-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
30528977-0	2018	Radiosynthesis, biological evaluation and preliminary microPET study of 18F-labeled 5-resorcinolic triazolone derivative based on ganetespib targeting HSP90.	5-((3-(((3,5-bis(trifluoromethyl)phenyl)methyl)oxy)-2-phenylpiperidino)methyl)-3-oxo-1,2,4-triazolone	99-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
30528977-2	2018	Ganetespib, a most promising candidate among several HSP90 inhibitors under clinical trials, has entered Phase III clinical trials for cancer therapy.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
30528977-7	2018	Blocking of HSP90 by the pretreatment of ganetespib exhibited significantly decreased accumulation of [18F]PTP-Ganetespib in MDA-MB-231 and MCF-7 cells, indicating the specific binding of [18F]PTP-Ganetespib to MDA-MB-231 and MCF-7 cells with high HSP90 expression.	STA 9090	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
30528977-7	2018	Blocking of HSP90 by the pretreatment of ganetespib exhibited significantly decreased accumulation of [18F]PTP-Ganetespib in MDA-MB-231 and MCF-7 cells, indicating the specific binding of [18F]PTP-Ganetespib to MDA-MB-231 and MCF-7 cells with high HSP90 expression.	STA 9090	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	248-253
30365122-7	2019	These results revealed that co-treatment with vorinostat and gefitinib induced ROS-dependent caspase activation, leading to the downregulation of HSP90 clients through HSP90 cleavage.	Reactive Oxygen Species	79-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
30154228-8	2018	CONCLUSIONS: The report confirms that EGFR exon 20 mutations are dependent on Hsp90 and are readily inhibited by the Hsp90 inhibitor luminespib; a treatment strategy that has been pursued in a confirmatory clinical trial (NCT01854034) for this group of lung adenocarcinomas that currently represent an unmet clinical need in precision oncology.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	133-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
30154228-6	2018	We exploit this vulnerability to show that the nongeldanamycin Hsp90 inhibitor luminespib (formerly AUY922) degrades EGFR exon 20 mutations, downstream targets, and induces apoptosis.	nongeldanamycin	47-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
30154228-6	2018	We exploit this vulnerability to show that the nongeldanamycin Hsp90 inhibitor luminespib (formerly AUY922) degrades EGFR exon 20 mutations, downstream targets, and induces apoptosis.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	79-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
30462492-4	2018	After loading indocyanine green (ICG), the heat-shock protein 90 (Hsp 90) inhibitor, and 17AAG and modification with polyethylene glycol (NH2-PEG), the resulting ICG-17AAG@HMONs-Gem-PEG exhibited a precisely controlled release of ICG and 17AAG and low-temperature photothermal therapy (PTT) (~41  C) with excellent tumor destruction efficacy.	Polyethylene Glycols	117-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-72
30462492-4	2018	After loading indocyanine green (ICG), the heat-shock protein 90 (Hsp 90) inhibitor, and 17AAG and modification with polyethylene glycol (NH2-PEG), the resulting ICG-17AAG@HMONs-Gem-PEG exhibited a precisely controlled release of ICG and 17AAG and low-temperature photothermal therapy (PTT) (~41  C) with excellent tumor destruction efficacy.	tanespimycin	166-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-72
30588010-10	2018	Mechanistically, we found that mTOR is a client of Hsp90-Cdc37 chaperone complex, and celastrol disrupts mTOR interaction with chaperone Hsp90 while promoting mTOR association with cochaperone Cdc37.	celastrol	86-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
30588010-10	2018	Mechanistically, we found that mTOR is a client of Hsp90-Cdc37 chaperone complex, and celastrol disrupts mTOR interaction with chaperone Hsp90 while promoting mTOR association with cochaperone Cdc37.	celastrol	86-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
30154228-8	2018	CONCLUSIONS: The report confirms that EGFR exon 20 mutations are dependent on Hsp90 and are readily inhibited by the Hsp90 inhibitor luminespib; a treatment strategy that has been pursued in a confirmatory clinical trial (NCT01854034) for this group of lung adenocarcinomas that currently represent an unmet clinical need in precision oncology.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	133-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
30279146-3	2018	However, the absence of an ATP binding domain, that is, instead, present in other HSPs such as HSP90 and HSP70, hampers the development of small molecules as inhibitors of HSP27.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
30591093-0	2018	HSP90 inhibitor, AUY922, debilitates intrinsic and acquired lapatinib-resistant HER2-positive gastric cancer cells.	Lapatinib	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30591093-7	2018	Dual inhibition of the HSP90 and HER2 signaling pathways could represent a potent therapeutic strategy to treat HER2-positive gastric cancer with intrinsic and acquired resistance to lapatinib.	Lapatinib	183-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
30211813-13	2018	Hsp90 inhibition with ganetespib resulted in modest clinical benefit on two dosing schedules and was associated with significant, although manageable, gastrointestinal toxicity.	STA 9090	22-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30316059-0	2018	Discovery of novel NO-releasing celastrol derivatives with Hsp90 inhibition and cytotoxic activities.	celastrol	32-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
30316059-4	2018	Further pharmacological studies showed that 11b induced dysregulations of the Hsp90 clients (Akt and Cdk4), apoptosis, and cell cycle arrested at G0/G1 phase against A549 cells.	11b	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
30211813-0	2018	Results from phase II trial of HSP90 inhibitor, STA-9090 (ganetespib), in metastatic uveal melanoma.	STA 9090	48-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
30211813-0	2018	Results from phase II trial of HSP90 inhibitor, STA-9090 (ganetespib), in metastatic uveal melanoma.	STA 9090	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
30107464-0	2018	Hsp90 inhibitor AT-533 blocks HSV-1 nuclear egress and assembly.	at-533	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30107464-5	2018	Treatment with the Hsp90 inhibitor AT-533 significantly decreased the intracellular and extracellular virus titers, and strongly inhibited nucleocapsid egress from the nucleus.	at-533	35-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
30508278-6	2018	Knockdown of HSP90 by small-interfering RNA (siHSP90) causes significant changes in levels of HSP70, alpha-tubulin, beta-actin, vimentin, and calpain-1, all of which are calcium oxalate (CaOx) crystal-binding proteins that play significant roles in kidney stone formation.	Calcium Oxalate	170-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
30467317-7	2018	Fifteen human CRPC LuCaP PDX-derived organoid models were assayed for responses to 110 drugs, and HSP90 inhibitors (ganetespib and onalespib) were among the select group of drugs (<10%) that demonstrated broad activity (>75% of models) at high potency (IC50 <1 microM).	STA 9090	116-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
30137596-8	2018	Pretreatment of arsenite-exposed cells with exogenous EGF, TGFalpha, NRG1, and HSP90 could promote, whereas exogenous IL-6 and NDRG1 could suppress, the phosphorylation of HER2.	arsenite	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
30500824-4	2018	Geldanamycin (GA), a Hsp90 inhibitor, enhances association of IKKbeta with Keap1 through the binding site in KD, and translocates IKKbeta to detergent-insoluble fractions leading to its autophagic degradation.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
30500824-4	2018	Geldanamycin (GA), a Hsp90 inhibitor, enhances association of IKKbeta with Keap1 through the binding site in KD, and translocates IKKbeta to detergent-insoluble fractions leading to its autophagic degradation.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
30477473-11	2018	CONCLUSIONS: Through its ability to inhibit Hsp90alpha/uPA/MMP2 signaling and suppress TRPM7 expression, we showed that Waixenicin A is a potential anticancer therapeutic agent for treating malignant lung cancer.	waixenicin A	120-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-54
30463299-5	2018	We find that inhibition of Hsp90 by geldanamycin (GA) induces the depletion of mammalian SIRT1 protein in a concentration and time dependent manner in COS-7 and HepG2 cells.	geldanamycin	36-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
30463299-5	2018	We find that inhibition of Hsp90 by geldanamycin (GA) induces the depletion of mammalian SIRT1 protein in a concentration and time dependent manner in COS-7 and HepG2 cells.	geldanamycin	50-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
30463299-5	2018	We find that inhibition of Hsp90 by geldanamycin (GA) induces the depletion of mammalian SIRT1 protein in a concentration and time dependent manner in COS-7 and HepG2 cells.	carbonyl sulfide	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
30463299-8	2018	Moreover, we observe a GA-sensitive physical interaction between SIRT1 and Hsp90 by immunoprecipitation.	geldanamycin	23-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
30453475-5	2018	Consistently, treatment of Burkitt lymphoma cell lines with HSP90 inhibitors (17-AAG or 17-DMAG) was accompanied by downregulation of canonical MYC target genes.	tanespimycin	78-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
30453475-5	2018	Consistently, treatment of Burkitt lymphoma cell lines with HSP90 inhibitors (17-AAG or 17-DMAG) was accompanied by downregulation of canonical MYC target genes.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	88-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
30453475-6	2018	Combination treatment with 17-DMAG and the proteasome inhibitor, MG-132, led to accumulation of MYC protein, indicating that upon HSP90 inhibition, MYC is degraded by the proteasome.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	27-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
30453475-6	2018	Combination treatment with 17-DMAG and the proteasome inhibitor, MG-132, led to accumulation of MYC protein, indicating that upon HSP90 inhibition, MYC is degraded by the proteasome.	Magnesium	65-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
29674508-2	2018	Preclinical studies demonstrated that resistance could be overcome using concurrent treatment with the HSP90 inhibitor XL888.Patients and Methods: Vemurafenib (960 mg p.o.	XL 888	119-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
30625276-6	2018	The HSP90alpha level was significantly correlated with SES-CD, CRP, and faecal calprotectin, but not with HBI.	ses-cd	55-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-14
30625276-7	2018	Linear regression analysis revealed that HSP90alpha was significantly associated with SES-CD (r2 = 0.27, p &lt; .001) and with CRP (r2 = 0.18, p = .002).	ses-cd	86-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-51
30625276-8	2018	HSP90alpha concentrations were significantly higher in the 10 patients with the highest SES-CD scores compared to the 10 patients with the lowest SES-CD scores.	ses-cd	88-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
30625276-8	2018	HSP90alpha concentrations were significantly higher in the 10 patients with the highest SES-CD scores compared to the 10 patients with the lowest SES-CD scores.	ses-cd	146-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
30625276-9	2018	CONCLUSIONS: Objective measures of disease activity and inflammation in Crohn"s disease - SES-CD and CRP - were closely associated with HSP90alpha concentrations in plasma, suggesting that HSP90alpha may be a biomarker of Crohn"s disease.	ses-cd	90-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-199
30483129-11	2018	Moreover, the present study reveals that combination of radicicol, VER-155008, cyclosporine A, and FK506, which are specific pharmacological inhibitors of Hsp90, Hsp70, Cyps, and FKBPs, respectively, resulted in a stronger inhibition of intoxication of cells with C2 toxin compared to application of the single inhibitors.	monorden	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
30483129-11	2018	Moreover, the present study reveals that combination of radicicol, VER-155008, cyclosporine A, and FK506, which are specific pharmacological inhibitors of Hsp90, Hsp70, Cyps, and FKBPs, respectively, resulted in a stronger inhibition of intoxication of cells with C2 toxin compared to application of the single inhibitors.	VER 155008	67-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
30483129-11	2018	Moreover, the present study reveals that combination of radicicol, VER-155008, cyclosporine A, and FK506, which are specific pharmacological inhibitors of Hsp90, Hsp70, Cyps, and FKBPs, respectively, resulted in a stronger inhibition of intoxication of cells with C2 toxin compared to application of the single inhibitors.	Cyclosporine	79-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
30483129-11	2018	Moreover, the present study reveals that combination of radicicol, VER-155008, cyclosporine A, and FK506, which are specific pharmacological inhibitors of Hsp90, Hsp70, Cyps, and FKBPs, respectively, resulted in a stronger inhibition of intoxication of cells with C2 toxin compared to application of the single inhibitors.	Tacrolimus	99-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
30382094-5	2018	Within the ternary Hsp90/FKBP51/Tau complex, Hsp90 serves as a scaffold that traps the PPIase and nucleates multiple conformations of Tau"s proline-rich region next to the PPIase catalytic pocket in a phosphorylation-dependent manner.	Proline	140-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
30136746-0	2018	Expedient Access to 2-Benzazepines by Palladium-Catalyzed C-H Activation: Identification of a Unique Hsp90 Inhibitor Scaffold.	2-benzazepines	20-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
30136746-0	2018	Expedient Access to 2-Benzazepines by Palladium-Catalyzed C-H Activation: Identification of a Unique Hsp90 Inhibitor Scaffold.	Palladium	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
30136746-3	2018	The benzotriazolodiazepinones were identified as new heat shock protein 90 (Hsp90) inhibiting lead compounds, with considerable potential for anti-cancer applications.	benzotriazolodiazepinones	4-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-74
30136746-3	2018	The benzotriazolodiazepinones were identified as new heat shock protein 90 (Hsp90) inhibiting lead compounds, with considerable potential for anti-cancer applications.	benzotriazolodiazepinones	4-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
30248409-3	2018	Since the chaperone activity requires ATP hydrolysis, molecules able to occupy the ATP binding pocket in the protein N-terminal domain (NTD) act as Hsp90 inhibitors.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
30248409-3	2018	Since the chaperone activity requires ATP hydrolysis, molecules able to occupy the ATP binding pocket in the protein N-terminal domain (NTD) act as Hsp90 inhibitors.	Adenosine Triphosphate	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
30248409-11	2018	This finding strongly suggests that Arg97 in LbNTD and more generally the conserved arginine residue in parasite Hsp90s are not exploitable for the development of selective inhibitors.	Arginine	84-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
30213552-6	2018	Our results show that cadmium downregulates HSF1, leading to HSP90, HSP70 and HSP27 gene expression downregulation in BF SN56 cholinergic neurons.	Cadmium	22-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
30213552-7	2018	In addition, cadmium induced Abeta and total and phosphorylated Tau proteins generation, mediated partially by HSP90, HSP70 and HSP27 disruption, leading to cell death.	Cadmium	13-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
29853657-1	2018	LESSONS LEARNED: The combination of the antiangiogenic agent ziv-aflibercept and the heat shock protein 90 inhibitor ganetespib was associated with several serious and unexpected adverse events and was not tolerable on the dosing schedule tested.Studies such as these emphasize the importance of considering overlapping toxicities when designing novel treatment combination regimens.	STA 9090	117-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
30382094-5	2018	Within the ternary Hsp90/FKBP51/Tau complex, Hsp90 serves as a scaffold that traps the PPIase and nucleates multiple conformations of Tau"s proline-rich region next to the PPIase catalytic pocket in a phosphorylation-dependent manner.	Proline	140-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
30166341-10	2018	Importantly, steady-state levels of capped mRNAs decreased in cells treated with the HSP90 inhibitor geldanamycin, raising the possibility that the cytotoxic effect of these drugs may partially be due to a general reduction in translatable mRNAs.	geldanamycin	101-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
30367157-3	2018	Here, we show that the MR and other members of the mineralocorticoid signalling pathway including HSP90 and FKBP4, possess anti-viral activity against HSV-1 independent of their effect on sodium transport, as shown by sodium channel inhibitors.	Sodium	218-224	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
30305268-1	2018	Activation of MYC, a bona fide client of HSP90, contributes to intrinsic ibrutinib resistance in mantle cell lymphoma.	ibrutinib	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
30378153-3	2018	Here, we showed that 17-allylamino-17-demethoxygeldanamycin (17-AAG, HSP90 inhibitor) affects the efficacy of chemotherapy through antioxidant activation-induced resistance.	tanespimycin	21-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
30338762-4	2018	Finally, we have compared the effect of CoCl2 with an effect of the pre-treatment of the cells with 17-AAG, an inhibitor of Hsp90 that is capable to induce expression of Hsp70, or with IOX2, an inhibitor of isoform 2 of prolyl hydroxylase that increases stability of hypoxia inducible factor 1alpha (HIF1alpha).	tanespimycin	100-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
30190324-2	2018	HSP90 relies on ATP hydrolysis for powering a conformational circuit that helps fold the client protein.	Adenosine Triphosphate	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30190324-3	2018	To that end, HSP90 binds to co-chaperone proteins that regulate ATP hydrolysis rate or interaction with client proteins.	Adenosine Triphosphate	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
30017966-0	2018	DCZ3112, a novel Hsp90 inhibitor, exerts potent antitumor activity against HER2-positive breast cancer through disruption of Hsp90-Cdc37 interaction.	dcz3112	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
30017966-0	2018	DCZ3112, a novel Hsp90 inhibitor, exerts potent antitumor activity against HER2-positive breast cancer through disruption of Hsp90-Cdc37 interaction.	dcz3112	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
30017966-3	2018	In this study, we discovered a new Hsp90 inhibitor, DCZ3112, with a novel mechanism of action.	dcz3112	52-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
30017966-4	2018	DCZ3112 directly bound to the N-terminal domain of Hsp90 and inhibited Hsp90-Cdc37 interaction without inhibiting ATPase activity.	dcz3112	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
30017966-4	2018	DCZ3112 directly bound to the N-terminal domain of Hsp90 and inhibited Hsp90-Cdc37 interaction without inhibiting ATPase activity.	dcz3112	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
30017966-5	2018	DCZ3112 inhibited the proliferation predominantly in HER2-positive breast cancer cells, including those resistant to the classical Hsp90 inhibitor geldanamycin, which mainly targets ATPase.	dcz3112	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
30017966-5	2018	DCZ3112 inhibited the proliferation predominantly in HER2-positive breast cancer cells, including those resistant to the classical Hsp90 inhibitor geldanamycin, which mainly targets ATPase.	geldanamycin	147-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
30341316-0	2018	HSP90-incorporating chaperome networks as biosensor for disease-related pathways in patient-specific midbrain dopamine neurons.	Dopamine	110-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30410862-1	2018	Dicarboxylate clamp tetratricopeptide repeat (dcTPR) motif-containing proteins are well-known partners of the heat shock protein (Hsp) 70 and Hsp90 molecular chaperones.	malonic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
30351341-2	2018	We report the final results of a phase II trial evaluating the activity of the Hsp90 inhibitor luminespib (AUY922) in NSCLC patients with EGFR ins20.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	95-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
30098331-7	2018	When combined with 17-AAG, PMA had additive effect on ErbB2 internalization indicating that Hsp90 inhibition and PKC activation induce internalization by alternative mechanisms.	Tetradecanoylphorbol Acetate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
29566599-1	2018	OBJECTIVE: This study aimed to investigate synergistic effects of recombinant mutant human tumor necrosis factor-related apoptosis-inducing ligand (rmhTRAIL) and heat-shock protein 90 (HSP90) inhibitor (geldanamycin derivative 17 -allylamino- 17-demethoxy -geldanamycin, 17-AAG) on the proliferation and apoptosis of multiple myeloma (MM) cells.	geldanamycin	203-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-183
29566599-1	2018	OBJECTIVE: This study aimed to investigate synergistic effects of recombinant mutant human tumor necrosis factor-related apoptosis-inducing ligand (rmhTRAIL) and heat-shock protein 90 (HSP90) inhibitor (geldanamycin derivative 17 -allylamino- 17-demethoxy -geldanamycin, 17-AAG) on the proliferation and apoptosis of multiple myeloma (MM) cells.	geldanamycin	203-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
29566599-1	2018	OBJECTIVE: This study aimed to investigate synergistic effects of recombinant mutant human tumor necrosis factor-related apoptosis-inducing ligand (rmhTRAIL) and heat-shock protein 90 (HSP90) inhibitor (geldanamycin derivative 17 -allylamino- 17-demethoxy -geldanamycin, 17-AAG) on the proliferation and apoptosis of multiple myeloma (MM) cells.	tanespimycin	227-269	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-183
29566599-1	2018	OBJECTIVE: This study aimed to investigate synergistic effects of recombinant mutant human tumor necrosis factor-related apoptosis-inducing ligand (rmhTRAIL) and heat-shock protein 90 (HSP90) inhibitor (geldanamycin derivative 17 -allylamino- 17-demethoxy -geldanamycin, 17-AAG) on the proliferation and apoptosis of multiple myeloma (MM) cells.	tanespimycin	227-269	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
30304567-3	2018	In this study, we explored the effects of HSP90 inhibitor, GA, on tumor necrosis factor (TNF)-alpha-induced proliferation and apoptosis of RAFLS, and the underlying mechanism.	geldanamycin	59-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
30351341-2	2018	We report the final results of a phase II trial evaluating the activity of the Hsp90 inhibitor luminespib (AUY922) in NSCLC patients with EGFR ins20.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
30344940-10	2018	Interestingly, the efficacies of HSP90 inhibitors in QR cells are reversely correlated with that of quizartib, but not to gilteritinib and midostaurin.	quizartib	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
30224681-3	2018	Here we show the efficacy and biological mechanism of a Hsp90 inhibitor NCT-50, a novobiocin-deguelin analog hybridizing the pharmacophores of these known Hsp90 inhibitors.	Novobiocin	82-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
30194165-1	2018	BACKGROUND/AIM: Selective heat shock protein 90 (Hsp90) inhibitor SNX-2112 exhibits antitumor activity in multiple cancer cell types.	SNX 2112	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-47
30194165-1	2018	BACKGROUND/AIM: Selective heat shock protein 90 (Hsp90) inhibitor SNX-2112 exhibits antitumor activity in multiple cancer cell types.	SNX 2112	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
30021337-0	2018	17-DMAG-loaded nanofibrous scaffold for effective growth inhibition of lung cancer cells through targeting HSP90 gene expression.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
30021337-3	2018	The present study aimed to evaluate the efficiency of implantable 17-dimethylaminoethylamino-17-demethoxy geldanamycin (17-DMAG)-loaded Poly(caprolactone)-poly(ethylene glycol) (PCL/PEG) nanofibers to increase the anti-cancer effects via inhibition of HSP90 expression and telomerase activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	66-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	252-257
30021337-3	2018	The present study aimed to evaluate the efficiency of implantable 17-dimethylaminoethylamino-17-demethoxy geldanamycin (17-DMAG)-loaded Poly(caprolactone)-poly(ethylene glycol) (PCL/PEG) nanofibers to increase the anti-cancer effects via inhibition of HSP90 expression and telomerase activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	120-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	252-257
30021337-3	2018	The present study aimed to evaluate the efficiency of implantable 17-dimethylaminoethylamino-17-demethoxy geldanamycin (17-DMAG)-loaded Poly(caprolactone)-poly(ethylene glycol) (PCL/PEG) nanofibers to increase the anti-cancer effects via inhibition of HSP90 expression and telomerase activity.	polycaprolactone	136-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	252-257
30021337-9	2018	This finding was associated with reduction of HSP90 mRNA expression and telomerase activity in the cells seeded on 17-DMAG-loaded PCL/PEG nanofibers in relative to free 17-DMAG.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	115-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
30021337-9	2018	This finding was associated with reduction of HSP90 mRNA expression and telomerase activity in the cells seeded on 17-DMAG-loaded PCL/PEG nanofibers in relative to free 17-DMAG.	Polyethylene Glycols	134-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
30021337-10	2018	In conclusion, the findings demonstrated that 17-DMAG-loaded PCL/PEG nanofibers are more effectual than free 17-DMAG against A549 lung cancer cells via modulation of Hsp90 expression and inhibition of telomerase activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	46-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
30021337-10	2018	In conclusion, the findings demonstrated that 17-DMAG-loaded PCL/PEG nanofibers are more effectual than free 17-DMAG against A549 lung cancer cells via modulation of Hsp90 expression and inhibition of telomerase activity.	Polyethylene Glycols	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
30224681-7	2018	Further biochemical and in silico studies revealed that NCT-50 downregulated Hsp90 function by interacting with the C-terminal ATP-binding pocket of Hsp90, leading to decrease in the interaction with Hsp90 client proteins.	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
30224681-7	2018	Further biochemical and in silico studies revealed that NCT-50 downregulated Hsp90 function by interacting with the C-terminal ATP-binding pocket of Hsp90, leading to decrease in the interaction with Hsp90 client proteins.	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
30224681-7	2018	Further biochemical and in silico studies revealed that NCT-50 downregulated Hsp90 function by interacting with the C-terminal ATP-binding pocket of Hsp90, leading to decrease in the interaction with Hsp90 client proteins.	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
30031951-0	2018	In silico identification and analysis of the binding site for aminocoumarin type inhibitors in the C-terminal domain of Hsp90.	Aminocoumarins	62-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
30224681-3	2018	Here we show the efficacy and biological mechanism of a Hsp90 inhibitor NCT-50, a novobiocin-deguelin analog hybridizing the pharmacophores of these known Hsp90 inhibitors.	Novobiocin	82-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
29915147-6	2018	Parallel to its broad-spectrum inhibition of Sec61-mediated protein translocation, mycolactone rapidly induced cytosolic chaperones Hsp70/Hsp90.	mycolactone	83-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
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
29941666-8	2018	To that effect, we have tested whether the unique phosphorylation of Hsp90alpha at threonines 5 and 7 that occurs during DNA damage repair affects its chaperone activity.	Threonine	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-79
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
30181335-0	2018	Retraction: Potentiation of Paclitaxel Activity by the HSP90 Inhibitor 17-allylamino-17-demethoxygeldanamycin in Human Ovarian Carcinoma Cell Lines with High Levels of Activated AKT.	Paclitaxel	28-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
30181335-0	2018	Retraction: Potentiation of Paclitaxel Activity by the HSP90 Inhibitor 17-allylamino-17-demethoxygeldanamycin in Human Ovarian Carcinoma Cell Lines with High Levels of Activated AKT.	tanespimycin	71-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
30015848-4	2018	In the present study, we evaluated the expression of AHR/HSP-90 in 25 formalin-fixed, paraffin-embedded human oral cancer specimens by IHC analysis.	Formaldehyde	70-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-63
30015848-4	2018	In the present study, we evaluated the expression of AHR/HSP-90 in 25 formalin-fixed, paraffin-embedded human oral cancer specimens by IHC analysis.	Paraffin	86-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-63
29991590-0	2018	Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity.	Calcium	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
29991590-0	2018	Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity.	Magnesium	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
29991590-1	2018	The Hsp90 molecular chaperones are ATP-dependent enzymes that maintain protein homeostasis and regulate many essential cellular processes.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
29991590-7	2018	In the presence of magnesium, ATP hydrolysis by TRAP1, as with other Hsp90s, was noncooperative, whereas calcium binding resulted in cooperative hydrolysis by the two protomers within the Hsp90 dimer.	Magnesium	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
29991590-7	2018	In the presence of magnesium, ATP hydrolysis by TRAP1, as with other Hsp90s, was noncooperative, whereas calcium binding resulted in cooperative hydrolysis by the two protomers within the Hsp90 dimer.	Magnesium	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
29991590-7	2018	In the presence of magnesium, ATP hydrolysis by TRAP1, as with other Hsp90s, was noncooperative, whereas calcium binding resulted in cooperative hydrolysis by the two protomers within the Hsp90 dimer.	Adenosine Triphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
29991590-7	2018	In the presence of magnesium, ATP hydrolysis by TRAP1, as with other Hsp90s, was noncooperative, whereas calcium binding resulted in cooperative hydrolysis by the two protomers within the Hsp90 dimer.	Calcium	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
30115641-0	2018	Activation of MYC, a bona fide client of HSP90, contributes to intrinsic ibrutinib resistance in mantle cell lymphoma.	ibrutinib	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
30115641-15	2018	As a client protein of HSP90, MYC can be inhibited via PU-H71 to overcome primary ibrutinib resistance.	ibrutinib	82-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
30153855-11	2018	RESULTS: Doxorubicin, cisplatin, and methotrexate, which are commonly used in chemotherapy, each induced HSP90AA1 upregulation in human osteosarcoma cells.	Doxorubicin	9-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-113
30153855-11	2018	RESULTS: Doxorubicin, cisplatin, and methotrexate, which are commonly used in chemotherapy, each induced HSP90AA1 upregulation in human osteosarcoma cells.	Cisplatin	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-113
30153855-11	2018	RESULTS: Doxorubicin, cisplatin, and methotrexate, which are commonly used in chemotherapy, each induced HSP90AA1 upregulation in human osteosarcoma cells.	Methotrexate	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-113
30045873-0	2018	Stimulation of the ATPase activity of Hsp90 by zerumbone modification of its cysteine residues destabilizes its clients and causes cytotoxicity.	zerumbone	47-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
30045873-0	2018	Stimulation of the ATPase activity of Hsp90 by zerumbone modification of its cysteine residues destabilizes its clients and causes cytotoxicity.	Cysteine	77-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
30045873-1	2018	Hsp90 is an ATP-dependent molecular chaperone that assists folding and conformational maturation/maintenance of many proteins.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
30045873-5	2018	Zerumbone enhanced the ATPase activity of cyanobacterial Hsp90 (Hsp90SE), yeast Hsp90, and human Hsp90alpha.	zerumbone	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-107
30045873-6	2018	It also enhanced the catalytic efficiency of Hsp90SE by greatly increasing kcat Mass analysis showed that zerumbone binds to cysteine side chains of Hsp90SE covalently.	zerumbone	106-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-52
30045873-6	2018	It also enhanced the catalytic efficiency of Hsp90SE by greatly increasing kcat Mass analysis showed that zerumbone binds to cysteine side chains of Hsp90SE covalently.	zerumbone	106-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-156
30045873-6	2018	It also enhanced the catalytic efficiency of Hsp90SE by greatly increasing kcat Mass analysis showed that zerumbone binds to cysteine side chains of Hsp90SE covalently.	Cysteine	125-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-52
30045873-6	2018	It also enhanced the catalytic efficiency of Hsp90SE by greatly increasing kcat Mass analysis showed that zerumbone binds to cysteine side chains of Hsp90SE covalently.	Cysteine	125-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-156
30045873-7	2018	Mutational studies identified 3 cysteine residues (one per each domain of Hsp90SE) that are involved in the enhancement, suggesting the presence of allosteric sites in the middle and C-terminal domains of Hsp90SE Treatment of cyanobacterial cells with zerumbone caused them to become very temperature-sensitive, a phenotype reminiscent of cyanobacterial Hsp90 mutants, and also decreased the cellular level of linker polypeptides that are clients for Hsp90SE Zerumbone showed cellular toxicity on cancer-derived mammalian cells by inducing apoptosis.	Cysteine	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-81
30045873-7	2018	Mutational studies identified 3 cysteine residues (one per each domain of Hsp90SE) that are involved in the enhancement, suggesting the presence of allosteric sites in the middle and C-terminal domains of Hsp90SE Treatment of cyanobacterial cells with zerumbone caused them to become very temperature-sensitive, a phenotype reminiscent of cyanobacterial Hsp90 mutants, and also decreased the cellular level of linker polypeptides that are clients for Hsp90SE Zerumbone showed cellular toxicity on cancer-derived mammalian cells by inducing apoptosis.	Cysteine	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-212
30045873-7	2018	Mutational studies identified 3 cysteine residues (one per each domain of Hsp90SE) that are involved in the enhancement, suggesting the presence of allosteric sites in the middle and C-terminal domains of Hsp90SE Treatment of cyanobacterial cells with zerumbone caused them to become very temperature-sensitive, a phenotype reminiscent of cyanobacterial Hsp90 mutants, and also decreased the cellular level of linker polypeptides that are clients for Hsp90SE Zerumbone showed cellular toxicity on cancer-derived mammalian cells by inducing apoptosis.	Cysteine	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
30045873-7	2018	Mutational studies identified 3 cysteine residues (one per each domain of Hsp90SE) that are involved in the enhancement, suggesting the presence of allosteric sites in the middle and C-terminal domains of Hsp90SE Treatment of cyanobacterial cells with zerumbone caused them to become very temperature-sensitive, a phenotype reminiscent of cyanobacterial Hsp90 mutants, and also decreased the cellular level of linker polypeptides that are clients for Hsp90SE Zerumbone showed cellular toxicity on cancer-derived mammalian cells by inducing apoptosis.	Cysteine	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-212
30045873-8	2018	In addition, zerumbone inhibited the binding of Hsp90/Cdc37 to client kinases.	zerumbone	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
30045873-9	2018	Altogether, we conclude that modification of cysteine residues of Hsp90 by zerumbone enhances its ATPase activity and inhibits physiological Hsp90 function.	Cysteine	45-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
30045873-9	2018	Altogether, we conclude that modification of cysteine residues of Hsp90 by zerumbone enhances its ATPase activity and inhibits physiological Hsp90 function.	Cysteine	45-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
30210681-4	2018	Anacardic acid (AA), which is commonly seen in natural plants of Anacardiaceae, exhibits potent Hsp90 ATPase inhibition activity.	anacardic acid	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
29798805-3	2018	crude extract, using Hsp 90alpha-functionalized mesoporous silica nanoparticle (MSN)-InP/ZnS quantum dot (QD) nanocomposites as a support material.	Silicon Dioxide	59-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-32
29752628-7	2018	Moreover, TNF-alpha and Hsp90 in T2DM patients correlated positively with fasting blood glucose (FBG).	Glucose	88-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
29396630-0	2018	The HSP90 inhibitor NVP-AUY922 inhibits growth of HER2 positive and trastuzumab-resistant breast cancer cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	24-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
29684503-2	2018	The recent crystal structures of the mitochondrial Hsp90 isoform TRAP1 in complexes with ATP analogs have provided first evidence of significant asymmetry in the closed dimerized state that triggers independent activity of the chaperone protomers, whereby preferential hydrolysis of the buckled protomer is followed by conformational flipping between protomers and hydrolysis of the second protomer.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
29549560-5	2018	Mechanistically, Cr(VI) interfered with the expression of two components of the stress response pathway: heat shock proteins Hsp72 and Hsp90alpha.	Chromium	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-145
29797762-4	2018	We improve in vitro models of tissue conditions by a biological matrix-based three-dimensional (3D) tissue culture that allows in vitro drug testing: It correctly shows a strong drug response upon gefitinib (Gef) treatment in a cell line harboring an EGFR-activating mutation (HCC827), but no clear drug response upon treatment with the HSP90 inhibitor 17AAG in two cell lines with KRAS mutations (H441, A549).	Gefitinib	197-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	337-342
29860649-3	2018	To establish whether pseudocontact shifts can be used to characterize ligand binding and the effects on methyl groups, the N-terminal domain of HSP90 was tagged with caged lanthanoid NMR probe 5 at three positions and titrated with a ligand.	Lanthanoid Series Elements	172-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
29665050-7	2018	Besides, co-treatment of HSP90 inhibitor (PU-H71) and HDAC6 inhibitor (tubastatin A) induced a stronger cell migration inhibition compared to administration of either drug alone.	tubastatin A	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
29797762-4	2018	We improve in vitro models of tissue conditions by a biological matrix-based three-dimensional (3D) tissue culture that allows in vitro drug testing: It correctly shows a strong drug response upon gefitinib (Gef) treatment in a cell line harboring an EGFR-activating mutation (HCC827), but no clear drug response upon treatment with the HSP90 inhibitor 17AAG in two cell lines with KRAS mutations (H441, A549).	Gefitinib	208-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	337-342
29800308-5	2018	Addition of 2 microM 17-allylamino-17-demethoxygeldanamycin (17-AAG), the Hsp90 inhibitor, to in vitro mature cumulus-oocyte complexes (COC) significantly decreased Hsp90alpha protein level (P &lt; 0.05), delayed germinal vesicle breakdown (GVBD) (P &lt; 0.05), and impeded the first polar body (PB1) extrusion (P &lt; 0.01) of porcine oocytes.	tanespimycin	21-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
29800308-5	2018	Addition of 2 microM 17-allylamino-17-demethoxygeldanamycin (17-AAG), the Hsp90 inhibitor, to in vitro mature cumulus-oocyte complexes (COC) significantly decreased Hsp90alpha protein level (P &lt; 0.05), delayed germinal vesicle breakdown (GVBD) (P &lt; 0.05), and impeded the first polar body (PB1) extrusion (P &lt; 0.01) of porcine oocytes.	tanespimycin	21-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-175
29904758-0	2018	Correction: 2-Aroylquinoline-5,8-diones as potent anticancer agents displaying tubulin and heat shock protein 90 (HSP90) inhibition.	2-aroylquinoline-5,8-dione	12-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-112
30061663-2	2018	We have previously demonstrated that FN interacts directly with Hsp90, as well as showing that the Hsp90 inhibitor novobiocin results in FN turnover via a receptor mediated process.	Novobiocin	115-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
30061663-5	2018	FN, LRP1 and Hsp90 could be isolated in a common complex, and inhibition of Hsp90 by novobiocin increased the colocalisation of FN and LRP1.	Novobiocin	85-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
30061663-7	2018	The effect of novobiocin was specific to LRP1-expressing cells and could be recapitulated by an LRP1 blocking antibody and the allosteric C-terminal Hsp90 inhibitor SM253, but not the N-terminal inhibitor geldanamycin.	Novobiocin	14-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
30061663-7	2018	The effect of novobiocin was specific to LRP1-expressing cells and could be recapitulated by an LRP1 blocking antibody and the allosteric C-terminal Hsp90 inhibitor SM253, but not the N-terminal inhibitor geldanamycin.	SM253	165-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
30061663-8	2018	Together these data suggest that LRP1 is required for FN turnover in response to Hsp90 inhibition by novobiocin, which may have unintended physiological consequences in contexts where C-terminal Hsp90 inhibition is to be used therapeutically.	Novobiocin	101-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
29724897-0	2018	Targeting HSP90 dimerization via the C terminus is effective in imatinib-resistant CML and lacks the heat shock response.	Imatinib Mesylate	64-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
29724897-5	2018	We have developed a novel inhibitor (aminoxyrone [AX]) of HSP90 function by targeting HSP90 dimerization via the C-terminal domain.	aminoxyrone	37-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
29724897-5	2018	We have developed a novel inhibitor (aminoxyrone [AX]) of HSP90 function by targeting HSP90 dimerization via the C-terminal domain.	aminoxyrone	37-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
29677383-3	2018	Here we report on the effect of the most prominent drug candidates, namely, radicicol, geldanamycin, derivatives of purine, and novobiocin, on Hsp90"s characteristic conformational dynamics and the binding of three interaction partners.	monorden	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
29677383-3	2018	Here we report on the effect of the most prominent drug candidates, namely, radicicol, geldanamycin, derivatives of purine, and novobiocin, on Hsp90"s characteristic conformational dynamics and the binding of three interaction partners.	geldanamycin	87-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
29677383-3	2018	Here we report on the effect of the most prominent drug candidates, namely, radicicol, geldanamycin, derivatives of purine, and novobiocin, on Hsp90"s characteristic conformational dynamics and the binding of three interaction partners.	purine	116-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
29677383-3	2018	Here we report on the effect of the most prominent drug candidates, namely, radicicol, geldanamycin, derivatives of purine, and novobiocin, on Hsp90"s characteristic conformational dynamics and the binding of three interaction partners.	Novobiocin	128-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
29720349-2	2018	Novobiocin, the first Hsp90 C-terminal inhibitor identified, contains a synthetically complex noviose sugar that has limited the generation of structure-activity relationships for this region of the molecule.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
29720349-2	2018	Novobiocin, the first Hsp90 C-terminal inhibitor identified, contains a synthetically complex noviose sugar that has limited the generation of structure-activity relationships for this region of the molecule.	noviose sugar	94-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
29992450-3	2018	Dietary Se, VE and Se + VE significantly enhanced the activities and mRNA levels of catalase as well as superoxide dismutase (SOD) but decreased the mRNA levels of HSP70 and HSP90.	Selenium	8-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
29992450-3	2018	Dietary Se, VE and Se + VE significantly enhanced the activities and mRNA levels of catalase as well as superoxide dismutase (SOD) but decreased the mRNA levels of HSP70 and HSP90.	Selenium	19-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
29985945-9	2018	Decreased relaxation to NO donor spermine-NONOate reached the statistical significance in BCAs incubated with NMPP for 72 hours, concomitantly with downregulation of sGCbeta1 expression that was independent of heat shock protein 90 (HSP90), nor did it significantly affect BCA relaxation caused by BAY 58-2667 that activates sGC in the heme-deficiency.	alpha-bromocinnamaldehyde	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	233-238
30151087-2	2018	After the identification of novobiocin as a C-Hsp90 interacting ligand a diverse gamut of novologues emerged, from which KU-32 and KU-596 exhibited strong neuroprotective activity.	Novobiocin	28-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-51
30151087-6	2018	In addition, chemical shift perturbations obtained by methyl-TROSY reveal that novologues bind at the cryptic, C-Hsp90 ATP-binding pocket and produce global, long-range structural rearrangements to dimeric Hsp90.	Adenosine Triphosphate	119-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-118
30151087-6	2018	In addition, chemical shift perturbations obtained by methyl-TROSY reveal that novologues bind at the cryptic, C-Hsp90 ATP-binding pocket and produce global, long-range structural rearrangements to dimeric Hsp90.	Adenosine Triphosphate	119-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
29904758-0	2018	Correction: 2-Aroylquinoline-5,8-diones as potent anticancer agents displaying tubulin and heat shock protein 90 (HSP90) inhibition.	2-aroylquinoline-5,8-dione	12-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
29904758-1	2018	Correction for "2-Aroylquinoline-5,8-diones as potent anticancer agents displaying tubulin and heat shock protein 90 (HSP90) inhibition" by Kunal Nepali et al., Org.	2-aroylquinoline-5,8-dione	16-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-116
29904758-1	2018	Correction for "2-Aroylquinoline-5,8-diones as potent anticancer agents displaying tubulin and heat shock protein 90 (HSP90) inhibition" by Kunal Nepali et al., Org.	2-aroylquinoline-5,8-dione	16-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
30111035-1	2018	To evaluate the clinical efficacy and safety of tripterygium glycosides (TG) in the treatment of henoch-schonlein purpura nephritis(HSPN).	tripterygium glycosides	48-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-136
29561308-3	2018	1,4-Naphthoquinone (1,4-NQ) scaffold has been found in compounds able to inhibit important biological targets associated with cancer, which includes DNA topoisomerase, Hsp90 and monoamine oxidase.	1,4-naphthoquinone	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
29561308-3	2018	1,4-Naphthoquinone (1,4-NQ) scaffold has been found in compounds able to inhibit important biological targets associated with cancer, which includes DNA topoisomerase, Hsp90 and monoamine oxidase.	1,4-naphthoquinone	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
29469983-2	2018	In this study, which was conceived within an effort that culminated in the recent report of the first dual inhibitors of B-Raf and Hsp90, we describe the identification of four compounds based on 4-aryl-1H-pyrrole[2,3-b]pyridine scaffold as interesting starting points for the development of new B-Raf inhibitors.	4-aryl-1h-pyrrole[2,3-b]pyridine	196-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
30111035-1	2018	To evaluate the clinical efficacy and safety of tripterygium glycosides (TG) in the treatment of henoch-schonlein purpura nephritis(HSPN).	Thioguanine	73-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-136
29743242-6	2018	Arginine triad substitutions that disrupted CDK9/CycT1 assembly accumulated Thr-186-dephosphorylated CDK9 associated with the cytoplasmic Hsp90/Cdc37 chaperone.	Arginine	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
29743242-6	2018	Arginine triad substitutions that disrupted CDK9/CycT1 assembly accumulated Thr-186-dephosphorylated CDK9 associated with the cytoplasmic Hsp90/Cdc37 chaperone.	Threonine	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
29743242-8	2018	Hsp90 inhibition in primary T cells blocked P-TEFb assembly, disrupted Thr-186 phosphorylation, and suppressed proviral reactivation.	Threonine	71-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29743242-11	2018	We conclude that the transfer of CDK9 from the Hsp90/Cdc37 complex induced by Thr-186 phosphorylation is a key step in P-TEFb biogenesis.	Threonine	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
29573834-0	2018	Corrigendum to "Panaxynol, a natural Hsp90 inhibitor, effectively targets both lung cancer stem and non-stem cells" [Canc.	falcarinol	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
30035186-8	2018	In line with this, the specific HSP90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) was selected and it was found that the combination of Resminostat and 17-AAG may provide a "smart" clinical strategy for HCC patients by targeting cellular communication within the tumour microenvironment.	tanespimycin	48-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
30058412-0	2018	The in silico identification of potent anti-cancer agents by targeting the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
30058412-1	2018	To identify new HSP90 inhibitors, the ATP binding site of the N-domain of HSP90 was targeted by molecular docking of a library of 23,129,083 compounds (from the ZINC database) to the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
30058412-1	2018	To identify new HSP90 inhibitors, the ATP binding site of the N-domain of HSP90 was targeted by molecular docking of a library of 23,129,083 compounds (from the ZINC database) to the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
30058412-1	2018	To identify new HSP90 inhibitors, the ATP binding site of the N-domain of HSP90 was targeted by molecular docking of a library of 23,129,083 compounds (from the ZINC database) to the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
30058412-1	2018	To identify new HSP90 inhibitors, the ATP binding site of the N-domain of HSP90 was targeted by molecular docking of a library of 23,129,083 compounds (from the ZINC database) to the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	183-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
30058412-1	2018	To identify new HSP90 inhibitors, the ATP binding site of the N-domain of HSP90 was targeted by molecular docking of a library of 23,129,083 compounds (from the ZINC database) to the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	183-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
30058412-1	2018	To identify new HSP90 inhibitors, the ATP binding site of the N-domain of HSP90 was targeted by molecular docking of a library of 23,129,083 compounds (from the ZINC database) to the ATP binding site of the N-domain of HSP90.	Adenosine Triphosphate	183-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
30058412-8	2018	Finally, computing the toxicity of these compounds with the ProTox-II webserver shows that three compounds, namely ZINC89453765, ZINC23918431 and ZINC12414793, can be considered as good HSP90 inhibitors.	zinc89453765	115-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
30058412-8	2018	Finally, computing the toxicity of these compounds with the ProTox-II webserver shows that three compounds, namely ZINC89453765, ZINC23918431 and ZINC12414793, can be considered as good HSP90 inhibitors.	ZINC23918431	129-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
30058412-8	2018	Finally, computing the toxicity of these compounds with the ProTox-II webserver shows that three compounds, namely ZINC89453765, ZINC23918431 and ZINC12414793, can be considered as good HSP90 inhibitors.	2-(2,5-difluorophenyl)-4-((4-oxo-4H-pyrido[1,2-a]pyrimidin-2-yl)methyl)-2H-benzo[e][1,2,4]thiadiazin-3(4H)-one 1,1-dioxide	146-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-191
29553718-0	2018	Role of HSP90 in the Regulation of de Novo Purine Biosynthesis.	purine	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
29553718-4	2018	Here, we present a new-found biochemical mechanism for the regulation of de novo purine biosynthetic enzymes mediated through HSP90.	purine	81-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
29553718-5	2018	HSP90-client protein interaction assays were employed to identify two enzymes within the de novo purine biosynthetic pathway, PPAT and FGAMS, as client proteins of HSP90.	purine	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29553718-5	2018	HSP90-client protein interaction assays were employed to identify two enzymes within the de novo purine biosynthetic pathway, PPAT and FGAMS, as client proteins of HSP90.	purine	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
30035186-8	2018	In line with this, the specific HSP90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) was selected and it was found that the combination of Resminostat and 17-AAG may provide a "smart" clinical strategy for HCC patients by targeting cellular communication within the tumour microenvironment.	tanespimycin	90-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
30035186-8	2018	In line with this, the specific HSP90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) was selected and it was found that the combination of Resminostat and 17-AAG may provide a "smart" clinical strategy for HCC patients by targeting cellular communication within the tumour microenvironment.	tanespimycin	168-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
29698859-0	2018	Design, synthesis and pharmacological evaluation of ALK and Hsp90 dual inhibitors bearing resorcinol and 2,4-diaminopyrimidine motifs.	resorcinol	90-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
29930762-7	2018	The AXL inhibitor, R428, or HSP90 inhibitor, ganetespib, were effective in reversing ALK-TKI resistance and EMT changes in both ALK-TKI-resistant and TGF-beta1-exposed H2228 cells.	STA 9090	45-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
29890785-9	2018	Using molecular docking analysis, heteronemin exhibited more binding affinity to the N-terminal ATP-binding pocket of Hsp90 protein than 17-AAG, a standard Hsp90 inhibitor.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
29875144-7	2018	We have demonstrated that Hsp90 inhibitor 17-AAG (17-allylamino-geldenamycin) causes destabilization of Chl1 protein and enhances significant disruption of sister chromatid cohesion, which is comparable to that observed under the Deltachl1 condition.	tanespimycin	42-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
29875144-7	2018	We have demonstrated that Hsp90 inhibitor 17-AAG (17-allylamino-geldenamycin) causes destabilization of Chl1 protein and enhances significant disruption of sister chromatid cohesion, which is comparable to that observed under the Deltachl1 condition.	17-allylamino-geldenamycin	50-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
29559312-0	2018	Anti-tumour effects of beta-sitosterol are mediated by AMPK/PTEN/HSP90 axis in AGS human gastric adenocarcinoma cells and xenograft mouse models.	gamma-sitosterol	23-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
29602128-0	2018	Targeted cancer therapy through 17-DMAG as an Hsp90 inhibitor: Overview and current state of the art.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	32-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
29602128-6	2018	17-DMAG binds to the Hsp90, and inhibits its function which eventually results in the degradation of Hsp90 client proteins.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
29602128-6	2018	17-DMAG binds to the Hsp90, and inhibits its function which eventually results in the degradation of Hsp90 client proteins.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
29334122-9	2018	Inhibition of HSP90alpha in cultured neurons, using the specific inhibitor, geldanamycin (GA), and siRNA/shRNA of HSP90alpha, protected cultured neurons from necrosis.	geldanamycin	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-24
29334122-9	2018	Inhibition of HSP90alpha in cultured neurons, using the specific inhibitor, geldanamycin (GA), and siRNA/shRNA of HSP90alpha, protected cultured neurons from necrosis.	geldanamycin	90-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-24
29698859-0	2018	Design, synthesis and pharmacological evaluation of ALK and Hsp90 dual inhibitors bearing resorcinol and 2,4-diaminopyrimidine motifs.	2,4-diaminopyrimidine	105-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
29698859-3	2018	By using our previously developed ALK inhibitor 6 and the clinical Hsp90 inhibitors AUY922 or AT13387 as the templates, we developed several series of resorcinol tethered 2,4-diaminopyrimidines as ALK/Hsp90 dual inhibitors bearing various linkers at different linking sites.	resorcinol	151-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
29698859-3	2018	By using our previously developed ALK inhibitor 6 and the clinical Hsp90 inhibitors AUY922 or AT13387 as the templates, we developed several series of resorcinol tethered 2,4-diaminopyrimidines as ALK/Hsp90 dual inhibitors bearing various linkers at different linking sites.	resorcinol	151-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
29698859-3	2018	By using our previously developed ALK inhibitor 6 and the clinical Hsp90 inhibitors AUY922 or AT13387 as the templates, we developed several series of resorcinol tethered 2,4-diaminopyrimidines as ALK/Hsp90 dual inhibitors bearing various linkers at different linking sites.	2,4-diaminopyrimidine	171-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
29899847-7	2018	HSP90 inhibitors suppressed ubiquitination processes which were involved in p53 degradation, but a proteasome inhibitor, MG-132, prevented the HSP90 inhibitors-induced p53 down-regulation.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	121-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
29698859-3	2018	By using our previously developed ALK inhibitor 6 and the clinical Hsp90 inhibitors AUY922 or AT13387 as the templates, we developed several series of resorcinol tethered 2,4-diaminopyrimidines as ALK/Hsp90 dual inhibitors bearing various linkers at different linking sites.	2,4-diaminopyrimidine	171-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
29799521-8	2018	Importantly, lapatinib-resistant tumors and cells retained sensitivity to Hsp90 and HSF1 inhibitors, both in vitro and in vivo, thus providing a unifying and actionable therapeutic node.	Lapatinib	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
32231947-8	2018	Radicicol counteracted the effect of DON on cytokine secretion, indicating that Hsp90 plays a crucial role in DON-induced cytokine secretion in HL60 cells.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
32231947-8	2018	Radicicol counteracted the effect of DON on cytokine secretion, indicating that Hsp90 plays a crucial role in DON-induced cytokine secretion in HL60 cells.	deoxynivalenol	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
32231947-8	2018	Radicicol counteracted the effect of DON on cytokine secretion, indicating that Hsp90 plays a crucial role in DON-induced cytokine secretion in HL60 cells.	deoxynivalenol	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
29676157-6	2018	Among several validated hits, the Hsp90 inhibitor 17-allylaminogeldanamycin (17-AAG) robustly decreases the secretion of collagen-I by our model cell line and by human primary cells.	tanespimycin	50-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
29722782-0	2018	Chemo-enzymatic synthesis of (E)-2,3-diaryl-5-styryl-trans-2,3-dihydrobenzofuran-based scaffolds and their in vitro and in silico evaluation as a novel sub-family of potential allosteric modulators of the 90 kDa heat shock protein (Hsp90).	(e)-2,3-diaryl-5-styryl-trans-2,3-dihydrobenzofuran	29-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
29722782-2	2018	Thanks to this novel synthetic strategy, a library of benzofuran-based potential allosteric activators of the Heat shock protein 90 (Hsp90) was easily prepared.	benzofuran	54-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-131
29722782-2	2018	Thanks to this novel synthetic strategy, a library of benzofuran-based potential allosteric activators of the Heat shock protein 90 (Hsp90) was easily prepared.	benzofuran	54-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
29722782-4	2018	Combining experimental and computational results, we propose a mechanism of action for these compounds, and expand the structure-activity relationship (SAR) information available for benzofuran-based Hsp90 activators.	benzofuran	183-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
29760386-6	2018	Moreover, the unique reactivity of N-acyl-N-alkyl sulfonamide enables the rational design of a lysine-targeted covalent inhibitor that shows durable suppression of the activity of Hsp90 in cancer cells.	n-acyl-n-alkyl sulfonamide	35-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
29760386-6	2018	Moreover, the unique reactivity of N-acyl-N-alkyl sulfonamide enables the rational design of a lysine-targeted covalent inhibitor that shows durable suppression of the activity of Hsp90 in cancer cells.	Lysine	95-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
29627724-4	2018	Ganetespib is a heat shock protein 90 (Hsp90) inhibitor with preferential tumor selectivity and conjugated to ZnPc as a tumor-targeted ligand.	Zn(II)-phthalocyanine	110-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
29627724-4	2018	Ganetespib is a heat shock protein 90 (Hsp90) inhibitor with preferential tumor selectivity and conjugated to ZnPc as a tumor-targeted ligand.	Zn(II)-phthalocyanine	110-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
29627724-7	2018	Herein, with combination of the inhibition of Hsp90 and the generation of cytotoxic ROS, Gan-ZnPc implements tumor selectivity, concentrated PDT and chemotherapy in a synergistic manner, which results in highly effective anti-tumor activity in vitro and in vivo.	gan-znpc	89-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
29748445-7	2018	Importantly, leukemic stem cells are strongly dependent upon HSP90 for their survival, and the HSP90 inhibitor ganetespib causes leukemic stem cell exhaustion in patient-derived mouse xenograft models.	STA 9090	111-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
29433909-4	2018	OBJECTIVE: We evaluated apoptosis in a melanoma cell line treated with the Hsp90 inhibitor 17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), in hyperthermic conditions.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	91-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
29274099-5	2018	Meanwhile, both celastrol treatment and knockdown of HSP70 or HSF-1 in SH-SY5Y cells significantly inhibited the Tau hyperphosphorylation and HSP90 expression induced by Abeta1-42 .	celastrol	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
29627724-4	2018	Ganetespib is a heat shock protein 90 (Hsp90) inhibitor with preferential tumor selectivity and conjugated to ZnPc as a tumor-targeted ligand.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
29627724-4	2018	Ganetespib is a heat shock protein 90 (Hsp90) inhibitor with preferential tumor selectivity and conjugated to ZnPc as a tumor-targeted ligand.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
29706537-1	2018	Protein folding in the cell requires ATP-driven chaperone machines such as the conserved Hsp70 and Hsp90.	Adenosine Triphosphate	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
29664615-0	2018	The Noncompetitive Effect of Gambogic Acid Displaces Fluorescence-Labeled ATP but Requires ATP for Binding to Hsp90/HtpG.	gambogic acid	29-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
29664615-0	2018	The Noncompetitive Effect of Gambogic Acid Displaces Fluorescence-Labeled ATP but Requires ATP for Binding to Hsp90/HtpG.	Adenosine Triphosphate	91-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
29664615-3	2018	It was shown that gambogic acid (GBA) has the potential to inhibit human Hsp90.	gambogic acid	18-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
29486954-0	2018	Discovery of 18beta-glycyrrhetinic acid conjugated aminobenzothiazole derivatives as Hsp90-Cdc37 interaction disruptors that inhibit cell migration and reverse drug resistance.	18alpha-glycyrrhetinic acid	13-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
29486954-0	2018	Discovery of 18beta-glycyrrhetinic acid conjugated aminobenzothiazole derivatives as Hsp90-Cdc37 interaction disruptors that inhibit cell migration and reverse drug resistance.	VBA protocol	51-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
29486954-1	2018	A series of 18beta-glycyrrhetinic acid (GA) conjugated aminobenzothiazole derivatives were designed, synthesized and evaluated for disruption activity of Hsp90-Cdc37 as well as the effects of in vitro cell migration.	18alpha-glycyrrhetinic acid	12-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
29486954-1	2018	A series of 18beta-glycyrrhetinic acid (GA) conjugated aminobenzothiazole derivatives were designed, synthesized and evaluated for disruption activity of Hsp90-Cdc37 as well as the effects of in vitro cell migration.	VBA protocol	55-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
29486954-3	2018	A docking study of the most active compound 11g revealed key interactions between 11g and Hsp90-Cdc37 complex in which the benzothiazole moiety and the amine chain group were important for improving activity.	benzothiazole	123-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
29486954-3	2018	A docking study of the most active compound 11g revealed key interactions between 11g and Hsp90-Cdc37 complex in which the benzothiazole moiety and the amine chain group were important for improving activity.	Amines	152-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
29486954-8	2018	Thus, we conclude that GA aminobenzothiazole derivatives may be the potential Hsp90-Cdc37 disruptors with the ability to suppress cells migration and reversed drug-resistant.	ga aminobenzothiazole	23-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
29854279-0	2018	Triptolide, a HSP90 middle domain inhibitor, induces apoptosis in triple manner.	triptolide	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
29725069-4	2018	In this report, we show that HSP90 binding to HSF1 depends on HSP90 conformation and is only readily visualized for the ATP-dependent, N-domain dimerized chaperone, a conformation only rarely sampled by mammalian HSP90.	Adenosine Triphosphate	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
29725069-6	2018	Further, we show that ATP-competitive, N-domain targeted HSP90 inhibitors disrupt this interaction, resulting in the increased duration of HSF1 occupancy of the hsp70 promoter and significant prolongation of both the constitutive and heat-induced HSF1 transcriptional activity.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
29785917-6	2018	In conclusion, higher THI was associated with significant increase in RT, RR, BT, HSP70, HSP90 and cortisol levels, and the crossbred buffalo were more heat tolerant than Mediterranean buffalo.	2-acetyl-4(5)-tetrahydroxybutylimidazole	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
29717218-5	2018	In particular, ganetespib, a novel HSP90 inhibitor, is a promising agent for ErbB2+ cancers.	STA 9090	15-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
28482755-0	2018	3D-QSAR, molecular docking, and molecular dynamic simulations for prediction of new Hsp90 inhibitors based on isoxazole scaffold.	Isoxazoles	110-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
28482755-2	2018	Hsp90 inhibitors containing isoxazole scaffold are currently being used in the treatment of cancer as tumor suppressers.	Isoxazoles	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29712950-4	2018	In this study, we blocked Hsp90 with geldanamycin and studied the fate of NLRP3 in human retinal pigment epithelial (RPE) cells.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
29607642-1	2018	Obtaining a detailed description of how active site flap motion affects substrate or ligand binding will advance structure-based drug design (SBDD) efforts on systems including the kinases, HSP90, HIV protease, ureases, etc.	sbdd	142-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
29618179-2	2018	Geldanamycin (GA) was the first identified natural Hsp90 inhibitor, but hepatotoxicity has limited its clinical application.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
29618179-2	2018	Geldanamycin (GA) was the first identified natural Hsp90 inhibitor, but hepatotoxicity has limited its clinical application.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
29402077-7	2018	When applied to a blind, focused library of 17 Hsp90 inhibitors, our miniaturized single-read in vitro thioflavin T -based kinetics aggregation assay exclusively identified compounds that target the chaperone N-terminal nucleotide binding site.	thioflavin T	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
29662162-3	2018	Here we report on a tryptophan residue in Hsp90-M as a new type of switch point.	Tryptophan	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
29662162-4	2018	Our study shows that this conserved tryptophan senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-pi interaction with a neighboring lysine.	Tryptophan	36-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
29662162-4	2018	Our study shows that this conserved tryptophan senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-pi interaction with a neighboring lysine.	Lysine	189-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
29437790-4	2018	In addition, the radioconjugate was investigated as a tool to monitor the outcome of AUY922, an Hsp90 inhibitor, in an MCF-7 xenograft model.Results: We demonstrated that 89Zr-DFO-ZHER3:8698 can track changes in receptor expression in HER3-positive xenograft models and monitor the outcome of AUY922 treatment.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	85-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
29655319-4	2018	The groove for Hsp90 binding on the TPR domain includes residues Lys227 and Lys308, referred to as the carboxylate clamp, and is essential for Cyp40-Hsp90 binding.	carboxylate	103-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
29655319-4	2018	The groove for Hsp90 binding on the TPR domain includes residues Lys227 and Lys308, referred to as the carboxylate clamp, and is essential for Cyp40-Hsp90 binding.	carboxylate	103-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
29849874-0	2018	Oxidative Stress Induces HSP90 Upregulation on the Surface of Primary Human Endothelial Cells: Role of the Antioxidant 7,8-Dihydroxy-4-methylcoumarin in Preventing HSP90 Exposure to the Immune System.	7,8-dihydroxy-4-methylcoumarin	119-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
29849874-4	2018	Pretreatment of HUVEC with 7,8-DHMC prevented H2O2-induced alterations of HSP90 cellular distribution and secretion.	7,8-dihydroxy-4-methylcoumarin	27-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
29849874-4	2018	Pretreatment of HUVEC with 7,8-DHMC prevented H2O2-induced alterations of HSP90 cellular distribution and secretion.	Hydrogen Peroxide	46-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
29849874-6	2018	The antioxidant 7,8-DHMC, by preventing oxidative-stress-triggered HSP90 surface upregulation, may be useful to counteract possible autoreactive reactions to HSP90.	7,8-dihydroxy-4-methylcoumarin	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
29849874-6	2018	The antioxidant 7,8-DHMC, by preventing oxidative-stress-triggered HSP90 surface upregulation, may be useful to counteract possible autoreactive reactions to HSP90.	7,8-dihydroxy-4-methylcoumarin	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
29219946-0	2018	C1206, a novel curcumin derivative, potently inhibits Hsp90 and human chronic myeloid leukemia cells in vitro.	c1206	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
29528635-1	2018	Grp94 and Hsp90, the ER and cytoplasmic hsp90 paralogs, share a conserved ATP-binding pocket that has been targeted for therapeutics.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
29528635-1	2018	Grp94 and Hsp90, the ER and cytoplasmic hsp90 paralogs, share a conserved ATP-binding pocket that has been targeted for therapeutics.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
29528635-4	2018	The structures of 1 bound to Hsp90 and Grp94 reveal large conformational changes in Grp94 but not Hsp90 that expose site 2, a binding pocket adjacent to the central ATP cavity that is ordinarily blocked.	Adenosine Triphosphate	165-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
29331417-10	2018	Furthermore, via inhibition of the HSP90/CDC37 complex, ERK and FOSL1 reversed the cisplatin resistance phenotype.	Cisplatin	83-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
29421063-3	2018	The resulting product GO-CHI-HA was loaded with an anti-cancer drug SNX-2112, which is the Hsp90 inhibitor.	SNX 2112	68-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
29219946-0	2018	C1206, a novel curcumin derivative, potently inhibits Hsp90 and human chronic myeloid leukemia cells in vitro.	Curcumin	15-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	4-(4-pyridinyl methylene) curcumin	0-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	4-(4-pyridinyl methylene) curcumin	0-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	c1206	36-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	c1206	36-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	Curcumin	26-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	Curcumin	26-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	Curcumin	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
29219946-1	2018	4-(4-Pyridinyl methylene) curcumin (C1206) is a new derivative of curcumin that is more active than curcumin in inhibition of heat shock protein 90 (Hsp90) and antitumor action.	Curcumin	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
29219946-2	2018	In this study we investigated the relationship between C1206-induced inhibition of Hsp90 and its anti-leukemic effects.	c1206	55-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
29219946-9	2018	These results suggest that C1206 is a novel Hsp90 inhibitor and a promising therapeutic agent for chronic myeloid leukemia.	c1206	27-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
29247830-0	2018	Phase 2 Study of the HSP-90 Inhibitor AUY922 in Previously Treated and Molecularly Defined Patients with Advanced Non-Small Cell Lung Cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	38-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-27
28808818-2	2018	The purine-scaffold inhibitor PU-H71 (NSC 750424), selective for Hsp90 in epichaperome networks, has demonstrated antitumor activity in multiple preclinical cancer models.	purine	4-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
28808818-2	2018	The purine-scaffold inhibitor PU-H71 (NSC 750424), selective for Hsp90 in epichaperome networks, has demonstrated antitumor activity in multiple preclinical cancer models.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	30-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
29436674-0	2018	The targeted inhibition of Hsp90 by a synthetic small molecule, DPide offers an effective treatment strategy against TNBCs.	dpide	64-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
29317342-0	2018	Image-guided photo-therapeutic nanoporphyrin synergized HSP90 inhibitor in patient-derived xenograft bladder cancer model.	nanoporphyrin	31-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
29317342-3	2018	In this study, we evaluated a novel multifunctional nanoporphyrin platform loaded with an HSP90 inhibitor 17AAG (NP-AAG) for use as a multi-modality therapy against bladder cancer.	nanoporphyrin	52-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
29317342-3	2018	In this study, we evaluated a novel multifunctional nanoporphyrin platform loaded with an HSP90 inhibitor 17AAG (NP-AAG) for use as a multi-modality therapy against bladder cancer.	tanespimycin	106-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
29339390-5	2018	Additionally, the Hsp90 inhibitor SNX-0723 in combination with the phosphatidylinositol 3-kinase inhibitor PIK-75 synergistically reduces the liver-stage parasite load.	2-fluoro-6-(tetrahydrofuran-3-ylamino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indol-1-yl)benzamide	34-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
29588468-7	2018	In a sterol-deficient hyperfilamentous GPI mutant of C. albicans too, Ras1 hyperactivation results from Hsp90 downregulation and causes actin polymerization.	Sterols	5-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
29436674-6	2018	In the present study, we performed the design, synthesis, and biological evaluation of Hsp90 inhibitors and found that a synthetic small molecule, DPide exerted a potent anticancer activity against TNBC cell line, MDA-MB-231 and non-small cell lung cancer (NSCLC) cell line, H1975 with GI50 values of 0.478 and 1.67 microM, respectively.	dpide	147-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
29534015-2	2018	Here, we report the antitumor effect of celastrol, an anti-inflammatory compound and a recognized HSP90 inhibitor, in Hodgkin and Reed-Sternberg cell lines.	celastrol	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
29594044-3	2018	Ganetespib is a novel and potent non-geldanamycin heat shock protein 90 (Hsp90) inhibitor.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-71
29594044-3	2018	Ganetespib is a novel and potent non-geldanamycin heat shock protein 90 (Hsp90) inhibitor.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
29594044-3	2018	Ganetespib is a novel and potent non-geldanamycin heat shock protein 90 (Hsp90) inhibitor.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
29594044-16	2018	Conclusion: Ganetespib plus doxorubicin was a well-tolerated combination and there remains potential for the clinical development of Hsp90 inhibitors in SCLC.	STA 9090	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
32254419-3	2018	The specific binding of tanespimycin to the N-terminal of heat shock protein 90 (HSP90) endows the modified nanoprobes (NPs) with the ability to up-regulate HSP90 tumor cells and to display excellent X-ray attenuation intensity and T1 MR imaging performance in an orthotopic hepatocellular carcinoma tumor model.	tanespimycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-79
32254419-3	2018	The specific binding of tanespimycin to the N-terminal of heat shock protein 90 (HSP90) endows the modified nanoprobes (NPs) with the ability to up-regulate HSP90 tumor cells and to display excellent X-ray attenuation intensity and T1 MR imaging performance in an orthotopic hepatocellular carcinoma tumor model.	tanespimycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
32254419-3	2018	The specific binding of tanespimycin to the N-terminal of heat shock protein 90 (HSP90) endows the modified nanoprobes (NPs) with the ability to up-regulate HSP90 tumor cells and to display excellent X-ray attenuation intensity and T1 MR imaging performance in an orthotopic hepatocellular carcinoma tumor model.	tanespimycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
29507054-1	2018	Novel therapies are undergoing clinical trials, for example, the Hsp90 inhibitor, XL888, in combination with BRAF inhibitors for the treatment of therapy-resistant melanomas.	XL 888	82-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
29507054-7	2018	Notably, we found that MITF expression correlates with CDK2 upregulation in patients; thus, dinaciclib would warrant consideration for treatment of patients unresponsive to BRAF-MEK and/or Hsp90 inhibitors and/or harboring MITF amplification/overexpression.	dinaciclib	92-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-194
29248874-4	2018	Biochemical assays revealed that MC-LR exposure altered the protein levels of HSP70 and HSP90, generally inhibited superoxide dismutase and catalase, reduced glutathione content, and increased the cellular malondialdehyde level of HepG2 cells, suggesting that MC-LR may induce biochemical disturbance and oxidative stress in HepG2 cells.	cyanoginosin LR	33-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
29395478-7	2018	We observed pyrazole based scaffolds increased organellar protein folding capacity through upregulation of chaperones, mainly HSP90 and its co-chaperone HOP which coordinate refolding of misfolded/aggregated species.	pyrazole	12-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
29092071-10	2018	We found that not only the PAS domain but also the bHLH domain bound to HSP90.	Protactinium	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
29471019-5	2018	We discovered an increased interaction between PHD2 and the p23:Hsp90 chaperone complex in response to mitochondrial stress elicited by the mitochondrial neurotoxin 1-methyl-4-phenylpyridine (MPP+) within cultured DAergic cells.	1-Methyl-4-phenylpyridinium	165-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
29471019-5	2018	We discovered an increased interaction between PHD2 and the p23:Hsp90 chaperone complex in response to mitochondrial stress elicited by the mitochondrial neurotoxin 1-methyl-4-phenylpyridine (MPP+) within cultured DAergic cells.	mangion-purified polysaccharide (Candida albicans)	192-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
29334217-3	2018	Using a combination of nuclear magnetic resonance (NMR) titration, isothermal titration calorimetry, fluorescence anisotropy, and native agarose gel electrophoresis, we have identified a direct interaction between the p53 DBD and Hsp90 co-chaperone p23 that occurs in the absence of Hsp90.	Sepharose	137-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-235
29334217-3	2018	Using a combination of nuclear magnetic resonance (NMR) titration, isothermal titration calorimetry, fluorescence anisotropy, and native agarose gel electrophoresis, we have identified a direct interaction between the p53 DBD and Hsp90 co-chaperone p23 that occurs in the absence of Hsp90.	Sepharose	137-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	283-288
31458497-0	2018	[2 + 2 + 2] Cyclotrimerization with Propargyl Halides as Copartners: Formal Total Synthesis of the Antitumor Hsp90 Inhibitor AT13387.	propargyl halides	36-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
31458497-2	2018	The Hsp90 inhibitor AT13387 (onalespib) is under clinical trials for the treatment of refractory gastrointestinal stromal tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31458497-2	2018	The Hsp90 inhibitor AT13387 (onalespib) is under clinical trials for the treatment of refractory gastrointestinal stromal tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
31458497-5	2018	This strategy has been extended to synthesize the key precursor of the Hsp90 inhibitor, AT13387.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	88-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
29320629-2	2018	Hsp90 is a homodimer, whose conformational states and functions are regulated by ATP-binding and hydrolysis.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29416003-6	2018	While Tan IIA did not inhibit heat shock protein 90 (Hsp90), it synergistically enhanced the antitumor efficacy of the Hsp90 inhibitors 17-AAG and ganetespib in human breast cancer MCF-7 cells.	STA 9090	147-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
29339250-2	2018	According to our previous studies, we synthesized a series of coumarin pyrazoline compounds HCP1-HCP6 that might be HSP90 inhibitors.	coumarin	62-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
29339250-2	2018	According to our previous studies, we synthesized a series of coumarin pyrazoline compounds HCP1-HCP6 that might be HSP90 inhibitors.	pyrazoline	71-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
29339250-6	2018	Above all HCP1 exerted better HSP90 inhibitory and anticancer effects than our initially identified HSP90 inhibitor DPB.	1,4-diphenylbutadiene	116-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
29358373-4	2018	We found the following: (i) AHSP and hsp90 associate with distinct globin partners in their immature heme-free states (AHSP with apo-Hbalpha, and hsp90 with apo-Hbbeta or Hb-gamma) and that hsp90 does not associate with mature Hb.	Heme	101-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
29358373-5	2018	(ii) Hsp90 stabilizes the apo-globins and helps to drive their heme insertion reactions, as judged by pharmacologic hsp90 inhibition or by coexpression of an ATP-ase defective hsp90.	Heme	63-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
29358373-6	2018	(iii) In nonerythroid cells, heme insertion into all globins became hsp90-dependent, which may explain how mixed Hb tetramers can mature in cells that do not express AHSP.	Heme	29-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
29358373-7	2018	Together, our findings uncover a process in which hsp90 first binds to immature, heme-free Hb-gamma or Hb-beta, drives their heme insertion process, and then dissociates to allow their heterotetramer formation with Hb-alpha.	Heme	81-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
29358373-7	2018	Together, our findings uncover a process in which hsp90 first binds to immature, heme-free Hb-gamma or Hb-beta, drives their heme insertion process, and then dissociates to allow their heterotetramer formation with Hb-alpha.	Heme	125-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
29358373-8	2018	Thus, in driving heme insertion, hsp90 works in concert with AHSP to generate functional Hb tetramers during erythropoiesis.	Heme	17-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
29396434-4	2018	As shown, inhibition of Hsp90 with geldanamycin or radicicol is enhancing sensitivity of K562 erythroleukemia cells to CDC.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
29166573-0	2018	Interaction of Hsp90 with phospholipid model membranes.	Phospholipids	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
29166573-5	2018	Hsp90 had a preference to bind with more unsaturated phospholipid species and the affinity was higher with negatively charged lipids than zwitterionic lipids.	Phospholipids	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29166573-6	2018	Increasing the mole fraction of cholesterol in the phospholipid led to a decrease of binding affinity to Hsp90.	Cholesterol	32-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
29166573-6	2018	Increasing the mole fraction of cholesterol in the phospholipid led to a decrease of binding affinity to Hsp90.	Phospholipids	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
29186352-6	2018	Two different HSP90 inhibitors, 17-allylamino-17-demethoxygeldanamycin and BIIB021, reduced the PRL-mediated increase in cell viability of doxorubicin-treated cells and led to a decrease in JAK2, ATM, and phosphorylated ATM protein levels.	tanespimycin	32-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
29186352-6	2018	Two different HSP90 inhibitors, 17-allylamino-17-demethoxygeldanamycin and BIIB021, reduced the PRL-mediated increase in cell viability of doxorubicin-treated cells and led to a decrease in JAK2, ATM, and phosphorylated ATM protein levels.	Doxorubicin	139-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
29186352-8	2018	Drug synergism was detected between the ATM inhibitor (KU55933) and doxorubicin and between the HSP90 inhibitor (BIIB021) and doxorubicin.	Doxorubicin	126-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
29386501-11	2018	Emodin treatment recovered PPAR-gamma activity and phosphorylation, eNOS phosphorylation, and HSP90/eNOS coupling in HAECS in a concentration-dependent manner, which was reversed by the PPAR-gamma inhibitor GW9662, and the eNOS inhibitor, L-NAME.	2-chloro-5-nitrobenzanilide	207-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
29386501-12	2018	The recovery of HSP90/eNOS coupling by emodin was impaired by GW9662 treatment.	2-chloro-5-nitrobenzanilide	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
29721383-4	2018	Elevated serum HSP90alpha levels were detected before PDAC formation and an extracellular HSP90alpha (eHSP90alpha) inhibitor effectively prevented PDAC development.	pdac	147-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-100
29374167-1	2018	Heat shock protein 90 (Hsp90) is an ATP dependent molecular chaperone deeply involved in the complex network of cellular signaling governing some key functions, such as cell proliferation and survival, invasion and angiogenesis.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
29374167-1	2018	Heat shock protein 90 (Hsp90) is an ATP dependent molecular chaperone deeply involved in the complex network of cellular signaling governing some key functions, such as cell proliferation and survival, invasion and angiogenesis.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
29255172-4	2018	By investigating the cellular pathways that induce protection of mutant p53 from ubiquitin-mediated proteolysis, we found that HDAC6/Hsp90-dependent mutant p53 accumulation is sustained by RhoA geranylgeranylation downstream of the mevalonate pathway, as well as by RhoA- and actin-dependent transduction of mechanical inputs, such as the stiffness of the extracellular environment.	Mevalonic Acid	232-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
28681940-5	2018	Furthermore, we provided evidence that Runx2 was transcriptionally regulated by HSP90 when using MG132 and CHX chase assay.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	97-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
28641528-0	2018	Drug Design, Synthesis and In Vitro Evaluation of Substituted Benzofurans as Hsp90 Inhibitors.	Benzofurans	62-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
28641528-3	2018	Natural products like geldanamycin and radicicol are established Hsp90 inhibitors, but face limitations with toxicity and inactivity, by in vivo studies respectively.	geldanamycin	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
28641528-3	2018	Natural products like geldanamycin and radicicol are established Hsp90 inhibitors, but face limitations with toxicity and inactivity, by in vivo studies respectively.	monorden	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
28641528-5	2018	OBJECTIVE: In this article, the structure based drug design of substituted 2-aryl/heteroarylidene-6- hydroxybenzofuran-3(2H)-one analogues to optimize and mimic the pharmacophoric interactions of the valid Hsp90 inhibitor radicicolis focused.	2-aryl/heteroarylidene-6- hydroxybenzofuran-3(2h)-one	75-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
29658791-7	2018	Combining both models resulted in 22 new and confirmed HSP90-independent NR3C1 inhibitors, providing two scaffolds (i.e., pyrimidine and pyrazolo-pyrimidine), which could potentially be of interest in the treatment of depression (i.e., inhibiting the glucocorticoid receptor (i.e., NR3C1), while leaving its chaperone, HSP90, unaffected).	pyrimidine	122-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
29658791-7	2018	Combining both models resulted in 22 new and confirmed HSP90-independent NR3C1 inhibitors, providing two scaffolds (i.e., pyrimidine and pyrazolo-pyrimidine), which could potentially be of interest in the treatment of depression (i.e., inhibiting the glucocorticoid receptor (i.e., NR3C1), while leaving its chaperone, HSP90, unaffected).	pyrimidine	122-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	319-324
29658791-7	2018	Combining both models resulted in 22 new and confirmed HSP90-independent NR3C1 inhibitors, providing two scaffolds (i.e., pyrimidine and pyrazolo-pyrimidine), which could potentially be of interest in the treatment of depression (i.e., inhibiting the glucocorticoid receptor (i.e., NR3C1), while leaving its chaperone, HSP90, unaffected).	1H-pyrazolo[4,3-d]pyrimidine	137-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
29658791-7	2018	Combining both models resulted in 22 new and confirmed HSP90-independent NR3C1 inhibitors, providing two scaffolds (i.e., pyrimidine and pyrazolo-pyrimidine), which could potentially be of interest in the treatment of depression (i.e., inhibiting the glucocorticoid receptor (i.e., NR3C1), while leaving its chaperone, HSP90, unaffected).	1H-pyrazolo[4,3-d]pyrimidine	137-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	319-324
29387685-0	2017	The Stoichiometric Interaction of the Hsp90-Sgt1-Rar1 Complex by CD and SRCD Spectroscopy.	Cadmium	65-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
29387685-0	2017	The Stoichiometric Interaction of the Hsp90-Sgt1-Rar1 Complex by CD and SRCD Spectroscopy.	srcd	72-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
29387685-3	2017	The Hsp90-mediated activation of NLR receptors (Nucleotide-binding domain and Leucine-rich Repeat) in the innate immunity of both plants and animals is dependent on the co-chaperone Sgt1 and in plants on Rar1, a cysteine- and histidine-rich domain (CHORD)-containing protein.	Cysteine	212-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
29387685-3	2017	The Hsp90-mediated activation of NLR receptors (Nucleotide-binding domain and Leucine-rich Repeat) in the innate immunity of both plants and animals is dependent on the co-chaperone Sgt1 and in plants on Rar1, a cysteine- and histidine-rich domain (CHORD)-containing protein.	Histidine	226-235	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
29387685-5	2017	CD spectroscopy was successfully used to determine the stoichiometry of a ternary protein complex among Hsp90, Sgt1, and Rar1 in the presence of excess ADP.	Adenosine Diphosphate	152-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Celecoxib	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Celecoxib	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Celecoxib	42-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Celecoxib	42-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Ibuprofen	51-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Ibuprofen	51-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Ibuprofen	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
29541415-2	2018	We found that NSAIDs including celecoxib (CCB) and ibuprofen (IBU) significantly potentiated the cytotoxicity of Hsp90 inhibitors in human multidrug-resistant (MDR) cells expressing high levels of mutant p53 (mutp53) protein and P-glycoprotein (P-gp), and reversed Hsp90 inhibitor resistance caused by activation of heat shock factor 1 (HSF1) and by up-regulation of heat shock proteins (Hsps) and P-gp.	Ibuprofen	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
29541415-3	2018	Inhibition of Akt/mTOR and STAT3 pathways by CCB induced autophagy, which promoted the degradation of mutp53, one of Hsp90 client proteins, and subsequently down-regulated HSF1/Hsps and P-gp.	Celecoxib	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
29541415-5	2018	Furthermore, CCB and IBU suppressed Hsp90 inhibitor-induced HSF1/Hsp70/P-gp activity and mutp53 expression in MDR cells.	Celecoxib	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29541415-5	2018	Furthermore, CCB and IBU suppressed Hsp90 inhibitor-induced HSF1/Hsp70/P-gp activity and mutp53 expression in MDR cells.	Ibuprofen	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29321504-3	2018	In this study, we report new inhibitors that directly bind to N-terminal ATP-binding pocket of Hsp90.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
28842319-8	2018	This study provides a useful resource detailing the candidate signalling determinants of acquired TKI resistance; and reveals a therapeutic approach of inhibiting HSP90 function as a means of salvage therapy to overcome pazopanib and dasatinib resistance.	pazopanib	220-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
28842319-8	2018	This study provides a useful resource detailing the candidate signalling determinants of acquired TKI resistance; and reveals a therapeutic approach of inhibiting HSP90 function as a means of salvage therapy to overcome pazopanib and dasatinib resistance.	Dasatinib	234-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
29543923-3	2018	Since HSP90 was shown to participate in stabilization of the subunit of the key transcription factor HIF-1, which controls the hypoxic response, the aim of this study was to investigate the influence of a HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG), on MM cells cultured under low oxygenation conditions.	tanespimycin	221-259	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
29543923-3	2018	Since HSP90 was shown to participate in stabilization of the subunit of the key transcription factor HIF-1, which controls the hypoxic response, the aim of this study was to investigate the influence of a HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG), on MM cells cultured under low oxygenation conditions.	tanespimycin	221-259	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
29298657-4	2018	OBJECTIVE: Extensive exploration of Coumarin derivatives as a potent inhibitor of variety of proteins including EGFR, tyrosine kinase, ERK1/2, PI3K, HSP 90, Bax, STAT proteins, NF-kappaB and telomerase which have been associated with lung cancer.	coumarin	36-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-155
29491214-2	2018	In a previous study, we found that BPA induced hypoxia inducible factor-1alpha (HIF-1alpha) degradation by dissociation from heat shock protein 90 (Hsp90).	bisphenol A	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-146
29491214-2	2018	In a previous study, we found that BPA induced hypoxia inducible factor-1alpha (HIF-1alpha) degradation by dissociation from heat shock protein 90 (Hsp90).	bisphenol A	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
30463061-0	2018	Curcumin Protects an SH-SY5Y Cell Model of Parkinson"s Disease Against Toxic Injury by Regulating HSP90.	Curcumin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
29521219-5	2018	RESULTS: This review showed that HSP90 inhibitors i.e. Ganestespib have shown great potential in the treatment of non-small cell lung carcinoma (NSCLC).	ganestespib	55-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
29137866-2	2018	Neuroprotective Hsp90 C-terminal inhibitors derived from novobiocin (novologues) include KU-32 and KU-596.	Novobiocin	57-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
29172085-0	2018	Design, synthesis and pharmacological evaluation of N-(5-chloro-2,4-dihydroxybenzoyl)-(R)-N-arylmethyl-1,2,3,4-tetrahydro-3-isoquinolinecarboxamides as potent Hsp90 inhibitors.	n-(5-chloro-2,4-dihydroxybenzoyl)-(r)-n-arylmethyl-1,2,3,4-tetrahydro-3-isoquinolinecarboxamides	52-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
29172085-1	2018	Using diverse arylmethyl groups to replace the benzyl moiety of the lead Hsp90 inhibitor 1 (N-(5-chloro-2,4-dihydroxybenzoyl)-(R)-N-benzyl-1,2,3,4-tetrahydro-3-iso quinolinecarboxamide), thirty four derivatives (10-43) were developed, and exhibited improved Hsp90 inhibitory and antiproliferative activities.	n-(5-chloro-2,4-dihydroxybenzoyl)-(r)-n-benzyl-1,2,3,4-tetrahydro-3-iso quinolinecarboxamide	92-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
29172085-1	2018	Using diverse arylmethyl groups to replace the benzyl moiety of the lead Hsp90 inhibitor 1 (N-(5-chloro-2,4-dihydroxybenzoyl)-(R)-N-benzyl-1,2,3,4-tetrahydro-3-iso quinolinecarboxamide), thirty four derivatives (10-43) were developed, and exhibited improved Hsp90 inhibitory and antiproliferative activities.	n-(5-chloro-2,4-dihydroxybenzoyl)-(r)-n-benzyl-1,2,3,4-tetrahydro-3-iso quinolinecarboxamide	92-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	258-263
29172085-5	2018	Compared with the lead compound 1, docking and MD refinement of the Hsp90alpha-41 complex revealed a favorable H-bonding interaction between the side-chain of Tyr139 and the pyridine moiety of 41, which is the first time to be used for resorcinol-based Hsp90 inhibitors.	pyridine	174-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-78
29172085-5	2018	Compared with the lead compound 1, docking and MD refinement of the Hsp90alpha-41 complex revealed a favorable H-bonding interaction between the side-chain of Tyr139 and the pyridine moiety of 41, which is the first time to be used for resorcinol-based Hsp90 inhibitors.	pyridine	174-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
29172085-5	2018	Compared with the lead compound 1, docking and MD refinement of the Hsp90alpha-41 complex revealed a favorable H-bonding interaction between the side-chain of Tyr139 and the pyridine moiety of 41, which is the first time to be used for resorcinol-based Hsp90 inhibitors.	resorcinol	236-246	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-78
29172085-5	2018	Compared with the lead compound 1, docking and MD refinement of the Hsp90alpha-41 complex revealed a favorable H-bonding interaction between the side-chain of Tyr139 and the pyridine moiety of 41, which is the first time to be used for resorcinol-based Hsp90 inhibitors.	resorcinol	236-246	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
29177662-3	2018	The chaperone function of Hsp90 is linked to its ability to bind and hydrolyze ATP.	Adenosine Triphosphate	79-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
29177675-2	2018	There have been 18 Hsp90 inhibitors (Hsp90i) that have entered the clinic, all of which, though structurally distinct, target the ATP-binding Bergerat fold of the chaperone N-terminus.	Adenosine Triphosphate	130-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
28971773-2	2018	1,3,5-Triazine compounds explored for anticancer activities have been reported to act by various mechanisms on several molecular targets in human cells such as methyltransferase (DNMT), heat shock protein 90 (Hsp90) and phosphoinositide 3-kinase (PI3K).	1,3,5-TRIAZINE	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-207
28971773-2	2018	1,3,5-Triazine compounds explored for anticancer activities have been reported to act by various mechanisms on several molecular targets in human cells such as methyltransferase (DNMT), heat shock protein 90 (Hsp90) and phosphoinositide 3-kinase (PI3K).	1,3,5-TRIAZINE	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
29953987-4	2018	In this study, we report whether Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) enhanced etoposide-induced cytotoxicity in NSCLC cells through modulating the XPC expression.	tanespimycin	49-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
29953987-4	2018	In this study, we report whether Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) enhanced etoposide-induced cytotoxicity in NSCLC cells through modulating the XPC expression.	Etoposide	106-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
29953987-8	2018	Hsp90 inhibitor 17-AAG enhanced cytotoxicity and cell growth inhibition of etoposide in NSCLC cells, which were associated with the downregulation of XPC expression and inactivation of AKT.	Etoposide	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29953987-9	2018	Our findings suggested that the Hsp90 inhibition induced XPC downregulation involved in enhancing the etoposide-induced cytotoxicity in H1703 and H520 cells.	Etoposide	102-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
28987383-0	2017	HSP90 inhibitor (NVP-AUY922) enhances the anti-cancer effect of BCL-2 inhibitor (ABT-737) in small cell lung cancer expressing BCL-2.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28987383-0	2017	HSP90 inhibitor (NVP-AUY922) enhances the anti-cancer effect of BCL-2 inhibitor (ABT-737) in small cell lung cancer expressing BCL-2.	ABT-737	81-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29056443-6	2017	To overcome resistance against microtubule stabilizing agents such as taxanes, epothilone B (EpoB) has merit, especially in combination with molecular targeted agents that inhibit heat shock protein 90 (Hsp90) and/or mammalian target of rapamycin (mTOR).	epothilone B	79-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
29311797-1	2017	The ATP-dependent 90 kDa heat shock protein, Hsp90, is a major regulator of protein triage, from assisting in nascent protein folding to refolding or degrading aberrant proteins.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
31435315-1	2018	Objectives: This study was conducted to investigate the modulatory role of an ethanol extract of Theobroma cacao beans on heat shock protein 90 (HSP90) and asymmetric dimethylarginine (ADMA) levels of endothelial cells under the influence of plasma of pre-eclamptic patients.	Ethanol	78-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
29564982-0	2018	Towards the In-silico Design of New HSP90 Inhibitors: Molecular Docking and 3D-QSAR CoMFA Studies of Tetrahydropyrido [4, 3-d] Pyrimidine Derivatives as HSP90 Inhibitors.	tetrahydropyrido(4,3-d)pyrimidine	101-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29564982-0	2018	Towards the In-silico Design of New HSP90 Inhibitors: Molecular Docking and 3D-QSAR CoMFA Studies of Tetrahydropyrido [4, 3-d] Pyrimidine Derivatives as HSP90 Inhibitors.	tetrahydropyrido(4,3-d)pyrimidine	101-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
29564982-1	2018	BACKGROUND: HSP90 is necessary for the conformational maturation of proteins, proteins disaggregation, folding newly synthesized peptides and the refolding of denatured proteins.	Peptides	129-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
29564982-3	2018	METHODS: In this research, molecular docking and comparative molecular field analysis (CoMFA) were used to investigate the interactions of tetrahydropyrido[4,3-d]pyrimidine derivatives with the N-terminal domain binding site of the HSP90 and predicting their inhibitory activities.	tetrahydropyrido(4,3-d)pyrimidine	139-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
29564982-11	2018	The molecular docking analysis of compound m45 with the N-terminal domain binding site of the HSP90 show hydroxyl group on phenyl ring is necessary to form hydrogen bonding with hydrophilic residues in binding site and a conserved water molecule.	Hydrogen	156-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
29564982-11	2018	The molecular docking analysis of compound m45 with the N-terminal domain binding site of the HSP90 show hydroxyl group on phenyl ring is necessary to form hydrogen bonding with hydrophilic residues in binding site and a conserved water molecule.	Water	231-236	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
29058824-0	2017	Synthesis and Biological Evaluation of Stilbene Analogues as Hsp90 C-Terminal Inhibitors.	Stilbenes	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	N-methylpiperidine	59-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	N-methylpiperidine	59-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	acyclic tertiary amines	96-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	acyclic tertiary amines	96-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	Stilbenes	127-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	Stilbenes	127-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	Triazoles	166-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
29058824-3	2017	Heat shock protein 90 (Hsp90) inhibition was observed when N-methylpiperidine was replaced with acyclic tertiary amines on the stilbene analogues that also contain a triazole-derived side chain.	Triazoles	166-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
28841232-2	2017	This study combined for the first time the HSP90 inhibitor ganetespib (Gan) and the proteasome inhibitor carfilzomib (Carf) to target key mechanisms of homeostasis in pancreatic cancer.	STA 9090	59-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
29247221-3	2017	Where inhibition of Hsp90 with a C-terminal inhibitor, novobiocin, reduced the fibronectin matrix, treatment with an N-terminal inhibitor, geldanamycin, increased fibronectin levels.	Novobiocin	55-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
30555625-3	2018	Exchanging specific residues for lysine improves binding affinity for Hsp90, indicating some residues are not critical for interacting with the target, whereas others are essential.	Lysine	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
29348817-0	2017	A Mitochondrial-targeted purine-based HSP90 antagonist for leukemia therapy.	purine	25-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
29348817-2	2017	Here, we targeted the protein folding environment in mitochondria by coupling a purine-based inhibitor of the molecular chaperone Heat Shock Protein-90 (Hsp90), PU-H71 to the mitochondrial-targeting moiety, triphenylphosphonium (TPP).	purine	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-151
29348817-2	2017	Here, we targeted the protein folding environment in mitochondria by coupling a purine-based inhibitor of the molecular chaperone Heat Shock Protein-90 (Hsp90), PU-H71 to the mitochondrial-targeting moiety, triphenylphosphonium (TPP).	purine	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	Plutonium	11-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	Plutonium	11-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	Plutonium	11-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	tpp	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	tpp	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	tpp	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
29348817-3	2017	Binding of PU-H71-TPP to ADP-Hsp90, Hsp90 co-chaperone complex or mitochondrial Hsp90 homolog, TRAP1 involved hydrogen bonds, pi-pi stacking, cation-pi contacts and hydrophobic interactions with the surrounding amino acids in the active site.	Adenosine Diphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
28580714-5	2017	The ATP-binding site of this bacterial protein has high structural similarity to the ATP-binding site of heat-shock protein 90 (Hsp90), a host cell chaperone universally required for viral replication, which led us to examine inhibition of Hsp90 as the compounds" potential mechanism of action.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-126
28580714-5	2017	The ATP-binding site of this bacterial protein has high structural similarity to the ATP-binding site of heat-shock protein 90 (Hsp90), a host cell chaperone universally required for viral replication, which led us to examine inhibition of Hsp90 as the compounds" potential mechanism of action.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
28580714-5	2017	The ATP-binding site of this bacterial protein has high structural similarity to the ATP-binding site of heat-shock protein 90 (Hsp90), a host cell chaperone universally required for viral replication, which led us to examine inhibition of Hsp90 as the compounds" potential mechanism of action.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
28580714-5	2017	The ATP-binding site of this bacterial protein has high structural similarity to the ATP-binding site of heat-shock protein 90 (Hsp90), a host cell chaperone universally required for viral replication, which led us to examine inhibition of Hsp90 as the compounds" potential mechanism of action.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-126
28580714-5	2017	The ATP-binding site of this bacterial protein has high structural similarity to the ATP-binding site of heat-shock protein 90 (Hsp90), a host cell chaperone universally required for viral replication, which led us to examine inhibition of Hsp90 as the compounds" potential mechanism of action.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
28580714-7	2017	The presented novel structural class of small molecules that target the Hsp90 ATP-binding site has excellent potential for further antiviral drug development because of the compounds" low toxicity and synthetic accessibility.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
29028527-0	2017	Identification and optimization of novel 6-acylamino-2-aminoquinolines as potent Hsp90 C-terminal inhibitors.	6-acylamino-2-aminoquinolines	41-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
29051117-0	2017	Melatonin reduces oxidative damage and upregulates heat shock protein 90 expression in cryopreserved human semen.	Melatonin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
29051117-8	2017	Moreover, 0.1mM melatonin upregulated the expression of heat shock protein 90 (HSP90), which confers resistance to stressors in frozen-thawed sperm.	Melatonin	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-77
29051117-8	2017	Moreover, 0.1mM melatonin upregulated the expression of heat shock protein 90 (HSP90), which confers resistance to stressors in frozen-thawed sperm.	Melatonin	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
29051117-9	2017	Results obtained upon addition of inhibitors of melatonin receptors (luzindole and 4-P-PDOT) and an HSP90 inhibitor (geldanamycin) in the cryoprotectant demonstrated that melatonin promoted HSP90 translation via the melatonin receptor MT1 and increased adenosine triphosphate levels, thus increasing the viability of thawed sperm.	geldanamycin	117-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
29051117-9	2017	Results obtained upon addition of inhibitors of melatonin receptors (luzindole and 4-P-PDOT) and an HSP90 inhibitor (geldanamycin) in the cryoprotectant demonstrated that melatonin promoted HSP90 translation via the melatonin receptor MT1 and increased adenosine triphosphate levels, thus increasing the viability of thawed sperm.	Adenosine Triphosphate	253-275	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
27879375-12	2017	In addition, results clearly showed that koenimbine encouraged cells to express Hsp 70 and Hsp 90 in a concentration-dependent manner up to a concentration of 100 microM and a time-dependent manner at 24-hour incubation both at transcriptional and translational levels.	koenimbin	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-97
28913790-0	2017	Delivery of HSP90 Inhibitor Using Water Soluble Polymeric Conjugates with High Drug Payload.	Water	34-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
28913790-4	2017	METHODS: We developed a simplified synthetic strategy to prepare polyethylene glycol based water-soluble polymeric system for model HSP90 inhibitor geldanamycin (GDM).	Polyethylene Glycols	65-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
28913790-4	2017	METHODS: We developed a simplified synthetic strategy to prepare polyethylene glycol based water-soluble polymeric system for model HSP90 inhibitor geldanamycin (GDM).	Water	91-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
28913790-4	2017	METHODS: We developed a simplified synthetic strategy to prepare polyethylene glycol based water-soluble polymeric system for model HSP90 inhibitor geldanamycin (GDM).	geldanamycin	148-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
28913790-4	2017	METHODS: We developed a simplified synthetic strategy to prepare polyethylene glycol based water-soluble polymeric system for model HSP90 inhibitor geldanamycin (GDM).	geldanamycin	162-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
28913790-10	2017	CONCLUSION: Water-soluble polymeric conjugate with high drug content was synthesized that exhibited in-vitro growth inhibitory activity similar to small molecular weight HSP90 inhibitor.	Water	12-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
29028527-1	2017	In order to discover novel Hsp90 inhibitors targeting the C-terminal ATP binding pocket, a novobiocin derivative based ROCS model was constructed for virtual screening.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
29028527-1	2017	In order to discover novel Hsp90 inhibitors targeting the C-terminal ATP binding pocket, a novobiocin derivative based ROCS model was constructed for virtual screening.	Novobiocin	91-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
28940589-0	2017	Development of Phenyl Cyclohexylcarboxamides as a Novel Class of Hsp90 C-terminal Inhibitors.	phenyl cyclohexylcarboxamides	15-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
28270068-0	2017	Improving the Hsp90 Inhibitors Containing 4-(2,4-Dihydroxyphenyl)-1,2,3-thiadiazole Scaffold: Synthesis, Affinity and Effect on Cancer Cells.	Oprea1_064698	42-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
28270068-3	2017	OBJECTIVE: To improve the compounds containing 4-(2,4-dihydroxyphenyl)-1,2,3-thiadiazole scaffold as human Hsp90 inhibitors.	Oprea1_064698	47-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
28270068-5	2017	RESULTS: A series of compounds containing the 4-(2,4-dihydroxyphenyl)-1,2,3-thiadiazole scaffold were synthesized as Hsp90 inhibitors.	Oprea1_064698	46-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
28940589-2	2017	Novobiocin, a coumarin antibiotic, was the first Hsp90 C-terminal inhibitor identified, however, it manifested poor anti-proliferative activity (SKBr3, IC50  700 mum).	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
28973376-2	2017	AIPL1 functions as a photoreceptor-specific co-chaperone that interacts with the molecular chaperone HSP90 to facilitate the stable assembly of the retinal cyclic GMP (cGMP) phosphodiesterase (PDE6) holoenzyme.	Cyclic GMP	156-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
28973376-2	2017	AIPL1 functions as a photoreceptor-specific co-chaperone that interacts with the molecular chaperone HSP90 to facilitate the stable assembly of the retinal cyclic GMP (cGMP) phosphodiesterase (PDE6) holoenzyme.	Cyclic GMP	168-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
29158891-5	2017	Oxygen-dependent (through pVHL, PHDs, calcium-mediated) and independent (through growth factor signaling pathway, mdm2 pathway, HSP90) regulation of HIF-1alpha leads to angiogenesis, metastasis, and cell survival.	Oxygen	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
29019670-1	2017	Previously, vibsanin B (ViB) was found to preferentially target HSP90beta compared to HSP90alpha.	vibsanin B	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-96
29290944-0	2017	Mitochondrial targeted HSP90 inhibitor Gamitrinib-TPP (G-TPP) induces PINK1/Parkin-dependent mitophagy.	Gamitrinib-TPP	39-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
29290944-0	2017	Mitochondrial targeted HSP90 inhibitor Gamitrinib-TPP (G-TPP) induces PINK1/Parkin-dependent mitophagy.	UNII-M6LC47TUG3	55-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
29290944-7	2017	Here, we used the mitochondrial targeted HSP90 inhibitor Gamitrinib-triphenylphosphonium (G-TPP), an anti-cancer agent, to chemically interfere with mitochondrial protein folding.	gamitrinib-triphenylphosphonium	57-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
29290944-7	2017	Here, we used the mitochondrial targeted HSP90 inhibitor Gamitrinib-triphenylphosphonium (G-TPP), an anti-cancer agent, to chemically interfere with mitochondrial protein folding.	UNII-M6LC47TUG3	90-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
29290944-8	2017	G-TPP treatment induced PINK1 accumulation, ubiquitin phosphorylation at Ser65, Parkin activation and its recruitment to mitochondria was specific for mitochondrial HSP90 inhibition and largely independent of mitochondrial membrane depolarization.	UNII-M6LC47TUG3	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
29061812-0	2017	Tumor Suppression Efficacy of Heat Shock Protein 90 Inhibitor 17AAG in a Liposarcoma Mouse Model.	tanespimycin	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-51
29061812-5	2017	On these, we performed cell viability assays and migration assays under treatment with the HSP90 inhibitor, 17AAG.	tanespimycin	108-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
29061812-10	2017	Also, the HSP90 inhibitor 17AAG effectively inhibited the activity of protein kinase B (AKT) and blocked extracellular signal-regulated kinase (ERK) activity.	tanespimycin	26-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
28739485-8	2017	Inhibition of this chaperone with the novel drug Onalespib (AT13387) demonstrates that HSP90 is an upstream regulator of the ACK1-dependent phosphorylation of STAT1 and STAT3.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	49-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
28757353-4	2017	MLK3 and MLK4beta protein levels declined under conditions of prolonged osmotic stress, heat stress or exposure to the Hsp90 inhibitor geldanamycin (GA); and MLK3 protein declined faster than MLK4beta.	geldanamycin	135-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
28543094-6	2017	Specific inhibitors for HO-1, HSP90, caspase-3, DNase I and EndoG almost completely blocked the DNA fragmentation induced by graphene exposure.	Graphite	125-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
28715732-0	2017	Proteasome inhibitor-induced cleavage of HSP90 is mediated by ROS generation and caspase 10-activation in human leukemic cells.	ros	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
28873084-1	2017	BACKGROUND: KW-2478 is a novel non-ansamycin Hsp90 inhibitor with modest single-agent activity in relapsed/refractory myeloma but which shows synergistic antimyeloma activity with bortezomib (BTZ) in preclinical studies.	KW-2478	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
28873084-2	2017	This study determined the safety, preliminary clinical activity, and pharmacokinetics of KW-2478, an Hsp90 inhibitor, in combination with BTZ in patients with relapsed/refractory multiple myeloma (MM).	KW-2478	89-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
28779264-7	2017	We tested the effect of HSP90 inhibition by three structurally unrelated compounds (alvespimycin, luminespib, radicicol) and asserted its specificity in cells depleted of cytosolic HSP90 (by RNA interference).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
28779264-7	2017	We tested the effect of HSP90 inhibition by three structurally unrelated compounds (alvespimycin, luminespib, radicicol) and asserted its specificity in cells depleted of cytosolic HSP90 (by RNA interference).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	98-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
28779264-7	2017	We tested the effect of HSP90 inhibition by three structurally unrelated compounds (alvespimycin, luminespib, radicicol) and asserted its specificity in cells depleted of cytosolic HSP90 (by RNA interference).	monorden	110-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
28779264-12	2017	Upregulated V2-receptors were fully functional; hence, in culture treated with an HSP90 inhibitor, addition of vasopressin resulted in higher levels of cAMP than in controls.	Cyclic AMP	152-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
28779264-13	2017	CONCLUSION: Since formation of cAMP is the first signalling step in raising water permeability of the collecting duct epithelia, we suggest that V2-receptor upregulation generates hypersensitivity to vasopressin linking HSP90 inhibition to the development of hyponatremia.	Cyclic AMP	31-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
29190920-6	2017	Furthermore, we showed that 3-ANE blocked VEGF-mediated endothelial nitric oxide synthase (eNOS) phosphorylation, vascular permeability and NO production in HUVECs, via disrupting the VEGF-induced association of eNOS and heat-shock protein 90 (HSP90).	3-ane	28-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	221-242
29190920-6	2017	Furthermore, we showed that 3-ANE blocked VEGF-mediated endothelial nitric oxide synthase (eNOS) phosphorylation, vascular permeability and NO production in HUVECs, via disrupting the VEGF-induced association of eNOS and heat-shock protein 90 (HSP90).	3-ane	28-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	244-249
29262861-0	2017	HSP90 promotes cell glycolysis, proliferation and inhibits apoptosis by regulating PKM2 abundance via Thr-328 phosphorylation in hepatocellular carcinoma.	Threonine	102-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
29262861-8	2017	Mechanistically, HSP90 was found to increase the phosphorylation of PKM2 at Thr-328.	Threonine	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
29262861-9	2017	Protein kinase glycogen synthase kinase-3beta (GSK-3beta) formed a protein complex with HSP90 and PKM2, and directly mediated Thr-328 phosphorylation of PKM2 induced by HSP90.	Threonine	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
29093475-4	2017	Our results showed that HSP90 binds to the N-terminal extreme of Htt-N in a sequence just ahead of the polyQ tract.	polyglutamine	103-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
29091774-3	2017	Like other Hsp90 kinase clients, binding of CDK4/6 to Cdc37 is blocked by ATP-competitive inhibitors.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
29285257-5	2017	In this study, a chromene compound, J2 that exhibited better cross-linking activity of HSP27 than xanthone compound, SW15 which was previously identified, was yielding sensitization to NSCLC cells with high expression of HSP27 when combined with HSP90 inhibitor and standard anticancer modalities such as taxol and cisplatin.	Benzopyrans	17-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
29079741-1	2017	FK506 binding protein of 51 kDa (FKBP51) is a heat shock protein 90 (Hsp90) co-chaperone involved in the regulation of steroid hormone receptors activity.	Tacrolimus	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
29079741-1	2017	FK506 binding protein of 51 kDa (FKBP51) is a heat shock protein 90 (Hsp90) co-chaperone involved in the regulation of steroid hormone receptors activity.	Tacrolimus	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
29079741-5	2017	The results demonstrated that the Hsp90 C-terminal peptide binds to the TPR domain of FKBP51 with the help of di-carboxylate clamp involving Lys272, Glu273, Lys352, Asn322, and Lys329 which are conserved throughout several di-carboxylate clamp TPR proteins.	malonic acid	110-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
29079741-5	2017	The results demonstrated that the Hsp90 C-terminal peptide binds to the TPR domain of FKBP51 with the help of di-carboxylate clamp involving Lys272, Glu273, Lys352, Asn322, and Lys329 which are conserved throughout several di-carboxylate clamp TPR proteins.	malonic acid	223-237	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
29228626-5	2017	Here we show that a single, short treatment with a relatively low dose of HSP90 inhibitor Ganetespib potentiates cytotoxic as well as radio- and chemosensitizing effects of hyperthermia and reduces thermotolerance in cervix cancer cell lines.	STA 9090	90-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
29262632-0	2017	Inhibition of HSP90 sensitizes a novel Raf/ERK dual inhibitor CY-9d in triple-negative breast cancer cells.	Cysteine	62-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
28873084-0	2017	A phase I/II study of KW-2478, an Hsp90 inhibitor, in combination with bortezomib in patients with relapsed/refractory multiple myeloma.	KW-2478	22-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
29045407-8	2017	We find that the SAXS data of the apo state of Hsp90 is compatible with a single wide-open conformation, whereas the SAXS data of Hsp90 bound to ATP or to an ATP-analogue strongly suggest heterogenous ensembles of a closed and a wide-open state.	Adenosine Triphosphate	145-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
29045865-1	2017	The function of the molecular chaperone Hsp90 depends on large conformational changes, the rearrangement of local motifs, and the binding and hydrolysis of ATP.	Adenosine Triphosphate	156-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
28679777-3	2017	We examined the efficacy of onalespib, a potent, long-acting novel HSP90 inhibitor as a single agent and in combination with temozolomide (TMZ) against gliomas in vitro and in vivoExperimental Design: The effect of onalespib on HSP90, its client proteins, and on the biology of glioma cell lines and patient-derived glioma-initiating cells (GSC) was determined.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
28851842-8	2017	NMR spectroscopy revealed that this inhibitory compound binds the N-terminal domain of Hsp90 close to its ATP-binding site and overlapping with a transient Aha1-interaction site.	Adenosine Triphosphate	106-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
28933546-9	2017	The selectivity of these inhibitors was tested against heat shock protein 90 (HSP90), which possesses a similar ATP-binding fold.	Adenosine Triphosphate	112-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-76
28933546-9	2017	The selectivity of these inhibitors was tested against heat shock protein 90 (HSP90), which possesses a similar ATP-binding fold.	Adenosine Triphosphate	112-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
28774796-5	2017	The combination of the HSP90 inhibitor 17AAG with the PI3K/mTOR inhibitor NVP-BEZ235 showed a synergistic activity decreasing melanoma cell growth, inducing apoptosis and targeting simultaneously the MAPK and PI3K/AKT/mTOR pathways.	tanespimycin	39-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
28774796-5	2017	The combination of the HSP90 inhibitor 17AAG with the PI3K/mTOR inhibitor NVP-BEZ235 showed a synergistic activity decreasing melanoma cell growth, inducing apoptosis and targeting simultaneously the MAPK and PI3K/AKT/mTOR pathways.	dactolisib	74-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
28797845-0	2017	The HSP90 inhibitor, NVP-AUY922, attenuates intrinsic PI3K inhibitor resistance in KRAS-mutant non-small cell lung cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	25-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
28797845-5	2017	The HSP90 inhibitor AUY922 suppressed both PI3K/AKT/mTOR and RAF/MEK/ERK signaling, rendering cells sensitive to a PI3K inhibitor (omipalisib, GSK458).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
28797845-5	2017	The HSP90 inhibitor AUY922 suppressed both PI3K/AKT/mTOR and RAF/MEK/ERK signaling, rendering cells sensitive to a PI3K inhibitor (omipalisib, GSK458).	omipalisib	131-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
28797845-5	2017	The HSP90 inhibitor AUY922 suppressed both PI3K/AKT/mTOR and RAF/MEK/ERK signaling, rendering cells sensitive to a PI3K inhibitor (omipalisib, GSK458).	omipalisib	143-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
28504248-0	2017	The flavonoid TL-2-8 induces cell death and immature mitophagy in breast cancer cells via abrogating the function of the AHA1/Hsp90 complex.	Flavonoids	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Manganese(2+)	24-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-241
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Manganese(2+)	24-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Indocyanine Green	29-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-241
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Indocyanine Green	29-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Indocyanine Green	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-241
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Indocyanine Green	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	mn-icg	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-241
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	mn-icg	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Polyethylene Glycols	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-241
28833643-4	2017	With NCPs consisting of Mn2+/indocyanine green (ICG) as the example, Mn-ICG@pHis-PEG display efficient pH-responsive tumor retention after systemic administration and then load Gambogic acid (GA), a natural inhibitor of heat-shock protein 90 (Hsp90) that plays an essential role for cells to resist heating-induced damage.	Polyethylene Glycols	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
28910138-9	2017	Increases in cellular plasticity were found to occur upon exposure to geldanamycin to inhibit HSP90, when subjected to various forms of cellular stress, or inhibition of histone acetylation.	geldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
28736082-8	2017	Among these proteins, expression levels of PEPCK-M, catalase, tubulin alpha chain, alpha-enolase, and endoplasmic reticulum resident protein 29 were significantly altered by DHT and the levels of HSP 90 and EF-Tu were changed by FSK.	fsk	229-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-202
28751373-10	2017	We also show that the HSP90 contribution is due to NOS-dependent mechanisms.NEW &amp; NOTEWORTHY We show that heat shock protein 90 functionally contributes to the heat loss response of cutaneous vasodilation during exercise in the heat, and this response is mediated through the activation of nitric oxide synthase.	Adenosine Monophosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
28751373-10	2017	We also show that the HSP90 contribution is due to NOS-dependent mechanisms.NEW &amp; NOTEWORTHY We show that heat shock protein 90 functionally contributes to the heat loss response of cutaneous vasodilation during exercise in the heat, and this response is mediated through the activation of nitric oxide synthase.	Adenosine Monophosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-131
28849241-0	2017	A novel chalcone-based molecule, BDP inhibits MDA-MB-231 triple-negative breast cancer cell growth by suppressing Hsp90 function.	Chalcone	8-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
28849241-0	2017	A novel chalcone-based molecule, BDP inhibits MDA-MB-231 triple-negative breast cancer cell growth by suppressing Hsp90 function.	(E)-3-(2-bromo-3,4,5-trimethoxyphenyl)-1-(2,4-dihydroxyphenyl)prop-2-en-1-one	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
28849241-5	2017	In the present study, we evaluated the in vitro effect of a small molecule Hsp90 inhibitor, (E)-3-(2-bromo-3,4,5-trimethoxyphenyl)-1-(2,4-dihydroxyphenyl)prop-2-en-1-one (BDP) on TNBC cell line, MDA-MB-231.	(E)-3-(2-bromo-3,4,5-trimethoxyphenyl)-1-(2,4-dihydroxyphenyl)prop-2-en-1-one	92-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
28849241-5	2017	In the present study, we evaluated the in vitro effect of a small molecule Hsp90 inhibitor, (E)-3-(2-bromo-3,4,5-trimethoxyphenyl)-1-(2,4-dihydroxyphenyl)prop-2-en-1-one (BDP) on TNBC cell line, MDA-MB-231.	(E)-3-(2-bromo-3,4,5-trimethoxyphenyl)-1-(2,4-dihydroxyphenyl)prop-2-en-1-one	171-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
28715732-3	2017	In this study, we found that HSP90 was cleaved to a 55kDa protein after treatment with proteasome inhibitors including MG132 in leukemia cells but was not cleaved in other tissue-derived cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	119-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
28715732-4	2017	HSP90 has two major isoforms (HSP90alpha and HSP90beta), and both were cleaved by MG132 treatment.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	82-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28715732-4	2017	HSP90 has two major isoforms (HSP90alpha and HSP90beta), and both were cleaved by MG132 treatment.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	82-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-40
28715732-5	2017	MG132 treatment also induced a decrease in HSP90 client proteins.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
28715732-6	2017	MG132 treatment generated ROS, and the cleavage of HSP90 was blocked by a ROS scavenger, N-acetylcysteine (NAC).	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28715732-6	2017	MG132 treatment generated ROS, and the cleavage of HSP90 was blocked by a ROS scavenger, N-acetylcysteine (NAC).	ros	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28715732-6	2017	MG132 treatment generated ROS, and the cleavage of HSP90 was blocked by a ROS scavenger, N-acetylcysteine (NAC).	Acetylcysteine	89-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28715732-6	2017	MG132 treatment generated ROS, and the cleavage of HSP90 was blocked by a ROS scavenger, N-acetylcysteine (NAC).	Acetylcysteine	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28930677-1	2017	Hsp90 chaperones undergo ATP-driven conformational changes during the maturation of client proteins, populating a closed state upon ATP binding in which the N-terminal domains of the homodimer form a second inter-protomer dimer interface.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28930677-1	2017	Hsp90 chaperones undergo ATP-driven conformational changes during the maturation of client proteins, populating a closed state upon ATP binding in which the N-terminal domains of the homodimer form a second inter-protomer dimer interface.	Adenosine Triphosphate	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28844386-2	2017	Neuroprotective Hsp90 C-terminal inhibitors (novologues) contain a biaryl ring system, and include KU-596, which was modified and investigated for potential anti-cancer activity.	KU-596	99-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
28715732-8	2017	Based on an inhibitor study, the cleavage of HSP90 induced by MG132 was dependent on caspase 10 activation.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
28715732-11	2017	Taken all together, our results suggest that the cleavage of HSP90 by MG132 treatment is mediated by ROS generation and caspase 10 activation.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	70-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
28715732-11	2017	Taken all together, our results suggest that the cleavage of HSP90 by MG132 treatment is mediated by ROS generation and caspase 10 activation.	ros	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
28822683-0	2017	Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.	Adenosine Diphosphate	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28915917-7	2017	Correlative immunofluorescence and immunoelectron microscopy showed that two small HSPs (HSP27 and alphaB-crystallin) and the ATP-dependent chaperone HSP90 translocated to the titin springs in myopathy.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
28914785-5	2017	In the present study, we further demonstrated that 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), an inhibitor of Hsp90, could suppress the self-renewal of BCSCs by downregulating B lymphoma Mo-MLV insertion region 1 homolog (BMI1), a polycomb family member with oncogenic activity in breast cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	51-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
28914785-5	2017	In the present study, we further demonstrated that 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), an inhibitor of Hsp90, could suppress the self-renewal of BCSCs by downregulating B lymphoma Mo-MLV insertion region 1 homolog (BMI1), a polycomb family member with oncogenic activity in breast cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	104-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
28878208-4	2017	We show that inhibition of HSP90 with ganetespib enhances T-cell-mediated killing of patient-derived human melanoma cells by their autologous T cells in vitro and potentiates responses to anti-CTLA4 and anti-PD1 therapy in vivo.	STA 9090	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
28871086-7	2017	Treatment of Ercc1 -/  mice, a mouse model of a human progeroid syndrome, with the HSP90 inhibitor 17-DMAG extended healthspan, delayed the onset of several age-related symptoms and reduced p16INK4a expression.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	99-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
28717943-0	2017	A pyrrole-based natural small molecule mitigates HSP90 expression in MDA-MB-231 cells and inhibits tumor angiogenesis in mice by inactivating HSF-1.	Pyrroles	2-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
28816449-4	2017	After analyzing X-ray cocrystal structures, the purine ring of the Hsp90 inhibitor 2 (BIIB021) was modified to pyrazolopyrimidine scaffolds.	purine	48-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
28816449-4	2017	After analyzing X-ray cocrystal structures, the purine ring of the Hsp90 inhibitor 2 (BIIB021) was modified to pyrazolopyrimidine scaffolds.	1H-pyrazolo[4,3-d]pyrimidine	111-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
28816449-5	2017	One pyrazolopyrimidine, 12b (DN401), bound better to TRAP1 than to Hsp90, inactivated the mitochondrial TRAP1 in vivo, and it exhibited potent anticancer activity.	1H-pyrazolo[4,3-d]pyrimidine	4-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
28822683-2	2017	Extensive analysis has focused on ATP-driven conformational changes of Hsp90; however, little is known about how Hsp90 operates under physiological nucleotide conditions in which both ATP and ADP are present.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
28822683-2	2017	Extensive analysis has focused on ATP-driven conformational changes of Hsp90; however, little is known about how Hsp90 operates under physiological nucleotide conditions in which both ATP and ADP are present.	Adenosine Triphosphate	184-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
28822683-2	2017	Extensive analysis has focused on ATP-driven conformational changes of Hsp90; however, little is known about how Hsp90 operates under physiological nucleotide conditions in which both ATP and ADP are present.	Adenosine Diphosphate	192-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
28822683-3	2017	By quantifying Hsp90 activity under mixed nucleotide conditions, we find dramatic differences in ADP sensitivity among Hsp90 homologs.	Adenosine Diphosphate	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28822683-3	2017	By quantifying Hsp90 activity under mixed nucleotide conditions, we find dramatic differences in ADP sensitivity among Hsp90 homologs.	Adenosine Diphosphate	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
28822683-4	2017	ADP acts as a strong ATPase inhibitor of cytosol-specific Hsp90 homologs, whereas organellular Hsp90 homologs (Grp94 and TRAP1) are relatively insensitive to the presence of ADP.	Adenosine Diphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
28822683-5	2017	These results imply that an ATP/ADP heterodimer of cytosolic Hsp90 is the predominant active state under physiological nucleotide conditions.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
28822683-5	2017	These results imply that an ATP/ADP heterodimer of cytosolic Hsp90 is the predominant active state under physiological nucleotide conditions.	Adenosine Diphosphate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
28822683-7	2017	ADP inhibition of bacterial Hsp90 can be relieved by bacterial Hsp70 and an activating client protein.	Adenosine Diphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
28822683-8	2017	These results suggest that altering ADP inhibition may be a mechanism of Hsp90 regulation.	Adenosine Diphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
28822683-11	2017	An accounting of ADP is critically important for designing and interpreting experiments with Hsp90.	Adenosine Diphosphate	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
28822683-12	2017	For example, contaminating ADP is a confounding factor in fluorescence resonance energy transfer experiments measuring arm closure rates of Hsp90.	Adenosine Diphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
28822683-13	2017	Our observations suggest that ADP at physiological levels is important to Hsp90 structure, activity, and regulation.	Adenosine Diphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
28619753-2	2017	PU-H71 is a next-generation Hsp90 inhibitor that preferentially targets the functionally distinct pool of Hsp90 present in tumor cells.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
28550115-4	2017	In this report, we provide the first evidence, to our knowledge, of the geldanamycin (Ge)-inhibitable HSP90 on the surface of live monocyte-derived Mphis (hMDMs).	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
28550115-4	2017	In this report, we provide the first evidence, to our knowledge, of the geldanamycin (Ge)-inhibitable HSP90 on the surface of live monocyte-derived Mphis (hMDMs).	geldanamycin	86-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
28713903-2	2017	The present study investigated the effect of Hsp90 inhibition on human acute myeloid leukemia (AML) cells using the novel small-molecule inhibitor SNX-2112.	SNX 2112	147-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
28713903-3	2017	We found that SNX-2112 more potently inhibited KG-1a cell growth than the classical Hsp90 inhibitor 17-(2-dimethylaminoethyl)amino-17-demethoxygeldanamycin as determined by CCK-8 assay.	17-(2-dimethylaminoethyl)amino-17-demethoxygeldanamycin	100-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
28619753-2	2017	PU-H71 is a next-generation Hsp90 inhibitor that preferentially targets the functionally distinct pool of Hsp90 present in tumor cells.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
28619753-9	2017	Finally, we found that the anti-lymphoma activity of PU-H71 is synergistic with dual PI3K/mTOR inhibition in vitro and in vivo Overall, this work provides support for Hsp90 as a therapeutic target in BL and suggests the potential for combination therapy with PU-H71 and inhibitors of PI3K/mTOR.	Plutonium	53-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
28619753-9	2017	Finally, we found that the anti-lymphoma activity of PU-H71 is synergistic with dual PI3K/mTOR inhibition in vitro and in vivo Overall, this work provides support for Hsp90 as a therapeutic target in BL and suggests the potential for combination therapy with PU-H71 and inhibitors of PI3K/mTOR.	Plutonium	259-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
28711525-0	2017	Novel Hsp90 inhibitor platycodin D disrupts Hsp90/Cdc37 complex and enhances the anticancer effect of mTOR inhibitor.	platycodin D	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
28859673-13	2017	CONCLUSION: Finally, we conclude on eNOS-metformin-HSp90 signaling and its remedial effect for controlling the EPC to improve the diabetic condition for delaying diabetes-related complication.	Metformin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28711525-0	2017	Novel Hsp90 inhibitor platycodin D disrupts Hsp90/Cdc37 complex and enhances the anticancer effect of mTOR inhibitor.	platycodin D	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
28711525-2	2017	In this study, platycodin D (PD), a saponin isolated from traditional Chinese herb Platycodonis Radix, was identified as a novel Hsp90 inhibitor.	platycodin D	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28711525-2	2017	In this study, platycodin D (PD), a saponin isolated from traditional Chinese herb Platycodonis Radix, was identified as a novel Hsp90 inhibitor.	Saponins	36-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28583846-8	2017	This work demonstrates the effectiveness of ganetespib, an HSP90 inhibitor in modulating DNA methylation through downregulation of DNMT expression.	STA 9090	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
29100402-7	2017	In addition, our study reveals a putative cooperation between STK33 and other HSP90 client protein kinases involved in molecular and cellular events through which cancer cells ensure their survival by securing the oxygen and nutrient supply.	Oxygen	214-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
28624441-0	2017	Hsp90 inhibitor geldanamycin attenuates the cytotoxicity of sunitinib in cardiomyocytes via inhibition of the autophagy pathway.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28624441-0	2017	Hsp90 inhibitor geldanamycin attenuates the cytotoxicity of sunitinib in cardiomyocytes via inhibition of the autophagy pathway.	Sunitinib	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28624441-3	2017	Here, we examined the effect of geldanamycin, an inhibitor of heat shock protein (Hsp) 90, on sunitinib-induced cytotoxicity in cardiomyocytes.	Sunitinib	94-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-89
28624441-10	2017	Thus, the further investigation of combination or sequential treatment with an Hsp90 inhibitor and sunitinib is warranted as a potential strategy of attenuating the cardiotoxicity associated with sunitinib administration in the clinical setting.	Sunitinib	196-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
28673683-0	2017	Single-walled carbon nanotubes (SWCNTs) inhibit heat shock protein 90 (HSP90) signaling in human lung fibroblasts and keratinocytes.	Carbon	14-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
28673683-0	2017	Single-walled carbon nanotubes (SWCNTs) inhibit heat shock protein 90 (HSP90) signaling in human lung fibroblasts and keratinocytes.	Carbon	14-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
28673683-12	2017	Finally, we showed that ectopic expression of HSP90, but not HSP40 or HSP70, completely abrogated the cytotoxic effects of SWCNTs, suggesting that SWCNT-induced cellular toxicity is HSP90 dependent.	swcnts	123-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
28673683-12	2017	Finally, we showed that ectopic expression of HSP90, but not HSP40 or HSP70, completely abrogated the cytotoxic effects of SWCNTs, suggesting that SWCNT-induced cellular toxicity is HSP90 dependent.	swcnts	123-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
28673683-12	2017	Finally, we showed that ectopic expression of HSP90, but not HSP40 or HSP70, completely abrogated the cytotoxic effects of SWCNTs, suggesting that SWCNT-induced cellular toxicity is HSP90 dependent.	Carbon	123-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
28673683-12	2017	Finally, we showed that ectopic expression of HSP90, but not HSP40 or HSP70, completely abrogated the cytotoxic effects of SWCNTs, suggesting that SWCNT-induced cellular toxicity is HSP90 dependent.	Carbon	123-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
28673683-13	2017	In summary, our findings suggest that the toxic effects of SWCNTs are mediated through inhibition of HSP90 in human lung fibroblasts and keratinocytes.	swcnts	59-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
28811486-3	2017	In this study we assessed the potential of non-invasive imaging approaches (photoacoustic imaging (PAI) and magnetic resonance imaging (MRI)) to detect melanin induction in SKMEL28 human melanoma cells, following inhibition of Hsp90 and BRAF signaling using 17-AAG and vemurafenib, respectively.	Melanins	152-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	227-232
28811486-4	2017	We confirmed, using western blot and spectrophotometry, that Hsp90 or BRAF inhibitor-induced melanoma cell differentiation resulted in an upregulation of tyrosinase and melanin expression levels, in comparison to control cells.	Melanins	169-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
28078663-11	2017	Ganetespib, an HSP90 inhibitor, with or without taxanes, inhibited the proliferation of angiosarcoma cells via apoptosis in a dose-dependent manner.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28713919-4	2017	To this end, we evaluated ganetespib (STA-9090), a novel and potent HSP90 inhibitor, for its activity in gastric cancer cell lines.	STA 9090	26-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
28713919-4	2017	To this end, we evaluated ganetespib (STA-9090), a novel and potent HSP90 inhibitor, for its activity in gastric cancer cell lines.	STA 9090	38-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
28637869-10	2017	Furthermore, the Hsp90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin dose dependently inhibited A3G and A3B mutational activity on HBV viral DNA.	tanespimycin	33-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
28764748-3	2017	Preclinical data suggest that HSP90 inhibition is synergistic with taxanes with the potential for significant clinical activity.	Taxoids	67-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
28764748-4	2017	We therefore tested ganetespib, a HSP90 inhibitor, in combination with paclitaxel and trastuzumab in patients with trastuzumab-refractory HER2-positive metastatic breast cancer.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
28478401-9	2017	Treatment with combined JAK1/JAK2 inhibitors or with JAK2 inhibitors in combination with HSP90 inhibitors was more effective than monotherapy with JAK2 inhibitors in bleomycin-induced pulmonary fibrosis and in adTBR-induced dermal fibrosis.	Bleomycin	166-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
28478401-9	2017	Treatment with combined JAK1/JAK2 inhibitors or with JAK2 inhibitors in combination with HSP90 inhibitors was more effective than monotherapy with JAK2 inhibitors in bleomycin-induced pulmonary fibrosis and in adTBR-induced dermal fibrosis.	adtbr	210-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
28495207-12	2017	CONCLUSIONS: A set of symmetrical scaffold molecules with bisphenol A cores induced allosteric inhibition of Hsp90.	bisphenol A	58-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
28631426-8	2017	The inhibition of Hsp90alpha affects nuclear localization of MRE11 and RAD50, impairs DDR signaling (e.g., BRCA1 and CHK2 phosphorylation), and slows down DSBs repair.	dsbs	155-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-28
28763460-9	2017	Besides, DHB remarkably reduced heat shock protein 90 (Hsp90) expression and its interaction with hERG, indicating that DHB disrupted hERG trafficking by impairing channel folding.	dihydroberberine	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
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
28789442-1	2017	The present study investigated the effects of HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) on apoptosis and the cell cycle of the HCT-116 human colon carcinoma cell line, with the aim of elucidating their underlying mechanisms.	tanespimycin	62-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
28823258-0	2017	[Proliferation and Apoptosis of Leukemia Cell Line K562 Treated with HSP90 Inhibitor 17-DMAG].	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	85-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
28823258-1	2017	OBJECTIVE: To investigate the role of HSP90 in proliferation and apoptosis of leukemia cells K562 through detecting the effect of HSP90 inhibitors 17-[2-(Dimethylamino) ethyl] amino-17-desmethoxygeldanamycin(17-DMAG) on leukemia K562 cell lines.	17-[2-(dimethylamino) ethyl] amino-17-desmethoxygeldanamycin	147-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
28823258-1	2017	OBJECTIVE: To investigate the role of HSP90 in proliferation and apoptosis of leukemia cells K562 through detecting the effect of HSP90 inhibitors 17-[2-(Dimethylamino) ethyl] amino-17-desmethoxygeldanamycin(17-DMAG) on leukemia K562 cell lines.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	208-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
28823258-4	2017	17-DAMG down-regulated the HSP90 mRNA expression in dosage-dependent mauner as well(r=0.9227) (P&lt;0.01).	17-damg	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
28823258-5	2017	CONCLUSION: HSP90 inhibitor 17-DMAG can inhibit the proliferation of K562 cells and induce their apoptosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	28-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
28823260-1	2017	OBJECTIVE: To explore the effect of heat shock protein 90(HSP90) inhibitor 17-DMAG, an inhibitor specific for heat shock protein 90, on the proliferation and apoptosis of acute lymphocytic leukemia cell lines Jurkat.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
28823260-4	2017	RESULTS: After Jurkat cells were treated with different concentrations of 17-DMAG for 48 hours, the HSP90 mRNA expression decreased significantly in dose dependent manner (r=0.9530, P&lt;0.01).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	74-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
28763460-9	2017	Besides, DHB remarkably reduced heat shock protein 90 (Hsp90) expression and its interaction with hERG, indicating that DHB disrupted hERG trafficking by impairing channel folding.	dihydroberberine	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
28763460-9	2017	Besides, DHB remarkably reduced heat shock protein 90 (Hsp90) expression and its interaction with hERG, indicating that DHB disrupted hERG trafficking by impairing channel folding.	dihydroberberine	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
28763460-9	2017	Besides, DHB remarkably reduced heat shock protein 90 (Hsp90) expression and its interaction with hERG, indicating that DHB disrupted hERG trafficking by impairing channel folding.	dihydroberberine	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
28301080-0	2017	HSP90 inhibitor AUY922 can reverse Fulvestrant induced feedback reaction in human breast cancer cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28742020-0	2017	Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.	Adenosine Triphosphate	40-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
28742020-1	2017	Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate "client" proteins, facilitating their folding and activating them for biological function.	Adenosine Triphosphate	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28743892-6	2017	The mutant DYRK1B variants were more vulnerable to the HSP90 inhibitor ganetespib and showed enhanced binding to the co-chaperone CDC37 as compared to wild type DYRK1B.	STA 9090	71-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
28664723-6	2017	The stability of mono- and disubstituted disulfides was determined to be sufficient during transit through the cytosol while still allowing for release of the cargo within 24 h. This linker system successfully released the compound Luminespib, an HSP90 inhibitor, which was deactivated by direct MPP conjugation.	mono- and disubstituted disulfides	17-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	247-252
28664723-6	2017	The stability of mono- and disubstituted disulfides was determined to be sufficient during transit through the cytosol while still allowing for release of the cargo within 24 h. This linker system successfully released the compound Luminespib, an HSP90 inhibitor, which was deactivated by direct MPP conjugation.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	232-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	247-252
28288818-0	2017	3-O-(Z)-coumaroyloleanolic acid overcomes Cks1b-induced chemoresistance in lung cancer by inhibiting Hsp90 and MEK pathways.	3-o-(z)-coumaroyloleanolic acid	0-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
28288818-5	2017	Interestingly, inhibition of either Hsp90 or MEK1/2 rendered a similar magnitude of antitumor activity by resensitization of the chemoresistant Cks1b-OE cells to CDDP and DOX, suggesting that both Hsp90 and MEK1/2 are essential to Cks1b for induction of chemoresistance.	Cisplatin	162-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
28288818-5	2017	Interestingly, inhibition of either Hsp90 or MEK1/2 rendered a similar magnitude of antitumor activity by resensitization of the chemoresistant Cks1b-OE cells to CDDP and DOX, suggesting that both Hsp90 and MEK1/2 are essential to Cks1b for induction of chemoresistance.	Doxorubicin	171-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
27826093-7	2017	RESULTS: Hsp90 release was stimulated with optimal doses of estradiol, IL-1, and TNF-alpha (10 ng/mL) from 15 minutes to 120 minutes.	Estradiol	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
27890930-0	2017	Histone deacetylase inhibitors interrupt HSP90 RASGRP1 and HSP90 CRAF interactions to upregulate BIM and circumvent drug resistance in lymphoma cells.	bim	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
27890930-0	2017	Histone deacetylase inhibitors interrupt HSP90 RASGRP1 and HSP90 CRAF interactions to upregulate BIM and circumvent drug resistance in lymphoma cells.	bim	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
28426997-0	2017	Design and synthesis of neolamellarin a derivatives targeting heat shock protein 90.	neolamellarin A	24-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
28426997-1	2017	In this study, we designed and synthesized a novel family of neolamellarin A derivatives that showed high inhibitory activity toward heat shock protein 90 (Hsp90), a kinase associated with cell proliferation.	neolamellarin A	61-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-154
28426997-1	2017	In this study, we designed and synthesized a novel family of neolamellarin A derivatives that showed high inhibitory activity toward heat shock protein 90 (Hsp90), a kinase associated with cell proliferation.	neolamellarin A	61-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
28426997-2	2017	The 3,4-bis(catechol)pyrrole scaffold and the benzyl group with methoxy modification at N position of pyrrole are essential to the Hsp90 inhibitory activity and cytotoxicity of these compounds.	3,4-bis(catechol)pyrrole	4-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
28426997-2	2017	The 3,4-bis(catechol)pyrrole scaffold and the benzyl group with methoxy modification at N position of pyrrole are essential to the Hsp90 inhibitory activity and cytotoxicity of these compounds.	Pyrroles	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
28426997-5	2017	Further molecular dynamics simulation indicated that the hydrophobic interactions as well as the hydrogen bonds contributed to the high affinity of 9p to Hsp90.	Hydrogen	97-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
28512265-3	2017	In this study, we show that the dying myeloma cells treated with chaetocin resulted in the induction of heat shock protein (HSP) 90, which was inhibited by antioxidant N-acetyl cysteine, and showed an increase in the expression of MAGE-A3 and MAGE-C1/CT7.	chaetocin	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-131
28512265-3	2017	In this study, we show that the dying myeloma cells treated with chaetocin resulted in the induction of heat shock protein (HSP) 90, which was inhibited by antioxidant N-acetyl cysteine, and showed an increase in the expression of MAGE-A3 and MAGE-C1/CT7.	Acetylcysteine	168-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-131
28512265-6	2017	These results suggest that the pretreatment of myeloma cells with chaetocin can enhance DC function through the up-regulation of HSP90 and cancer testis antigens in dying myeloma cells and can potently induce the Th1 polarization of DCs and myeloma-specific cytotoxic T lymphocytes.	chaetocin	66-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28410515-1	2017	When exposed to cancer cells, cytotoxic drugs such as doxorubicin (DOX) can lead to the induction of heat shock protein 90 (Hsp90), a molecular chaperone associated with a number of cancer-related client proteins, and result in cell survival.	Doxorubicin	54-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-122
28410515-1	2017	When exposed to cancer cells, cytotoxic drugs such as doxorubicin (DOX) can lead to the induction of heat shock protein 90 (Hsp90), a molecular chaperone associated with a number of cancer-related client proteins, and result in cell survival.	Doxorubicin	54-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
28410515-1	2017	When exposed to cancer cells, cytotoxic drugs such as doxorubicin (DOX) can lead to the induction of heat shock protein 90 (Hsp90), a molecular chaperone associated with a number of cancer-related client proteins, and result in cell survival.	Doxorubicin	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-122
28410515-1	2017	When exposed to cancer cells, cytotoxic drugs such as doxorubicin (DOX) can lead to the induction of heat shock protein 90 (Hsp90), a molecular chaperone associated with a number of cancer-related client proteins, and result in cell survival.	Doxorubicin	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
28410515-2	2017	Co-administration of DOX with tanespimycin (TNP), an Hsp90 inhibitor, can sensitize the cancer cells to the cytotoxic effects of DOX.	Doxorubicin	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
28410515-2	2017	Co-administration of DOX with tanespimycin (TNP), an Hsp90 inhibitor, can sensitize the cancer cells to the cytotoxic effects of DOX.	tanespimycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
28410515-2	2017	Co-administration of DOX with tanespimycin (TNP), an Hsp90 inhibitor, can sensitize the cancer cells to the cytotoxic effects of DOX.	Doxorubicin	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
28819369-0	2017	In vitro Cytotoxic Activities of the Oral Platinum(IV) Prodrug Oxoplatin and HSP90 Inhibitor Ganetespib against a Panel of Gastric Cancer Cell Lines.	STA 9090	93-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
28819369-17	2017	In conclusion, the HSP90 inhibitor ganetespib synergizes with platinum anticancer drugs and modulates intracellular signal transduction in direction of a less proliferative and aggressive phenotype.	STA 9090	35-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
28336809-2	2017	17-N-Allylamino-17-demethoxygeldanamycin (17-AAG), an HSP90 inhibitor, was tested in phase II/III clinical trials, but due to lack of efficacy, clinical evaluation of 17-AAG has achieved limited success, which led to resistance to 17-AAG.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
28556958-0	2017	Downregulation of androgen receptors by NaAsO2 via inhibition of AKT-NF-kappaB and HSP90 in castration resistant prostate cancer.	sodium arsenite	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
28556958-14	2017	NaAsO2 promoted HSP90 acetylation by down-regulating HDAC6, which reduces the stability of AR in prostate cancer cells.	sodium arsenite	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
28666484-0	2017	Prediction of new Hsp90 inhibitors based on 3,4-isoxazolediamide scaffold using QSAR study, molecular docking and molecular dynamic simulation.	3,4-isoxazolediamide	44-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
28666484-2	2017	METHODS: In the current study, 3,4-isoxazolediamide derivatives were suggested as an Hsp90 inhibitor for anti-cancer therapy.	3,4-isoxazolediamide	31-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
28666484-13	2017	CONCLUSION: The QSAR and docking analyses shown to be beneficial tools in the proposal of anti-cancer activities and a leader to the synthesis of new Hsp90 inhibitors based 3,4-isoxazolediamide.	3,4-isoxazolediamide	173-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
28476040-0	2017	Efficacy of an HSP90 inhibitor, ganetespib, in preclinical thyroid cancer models.	STA 9090	32-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28114285-0	2017	HSP90 stabilizes B-cell receptor kinases in a multi-client interactome: PU-H71 induces CLL apoptosis in a cytoprotective microenvironment.	Plutonium	72-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28615625-4	2017	Importantly, the hybrids composed of Az and geldanamycin, which have high inhibitory activities towards both Hsp70 and Hsp90, exhibit enhanced anti-leukemia activity relative to the individual inhibitors.	apoptozole	37-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
28615625-4	2017	Importantly, the hybrids composed of Az and geldanamycin, which have high inhibitory activities towards both Hsp70 and Hsp90, exhibit enhanced anti-leukemia activity relative to the individual inhibitors.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
28642708-0	2017	Myricitrin Protects Cardiomyocytes from Hypoxia/Reoxygenation Injury: Involvement of Heat Shock Protein 90.	myricitrin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
28642708-6	2017	Moreover, the potential targets of myricitrin was predicted using Discovery Studio software, and heat shock protein 90 (Hsp90) was identified as the main disease-related target.	myricitrin	35-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-118
28642708-6	2017	Moreover, the potential targets of myricitrin was predicted using Discovery Studio software, and heat shock protein 90 (Hsp90) was identified as the main disease-related target.	myricitrin	35-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
28642708-7	2017	Further mechanistic investigation revealed that 17-AAG, a pharmacologic inhibitor of Hsp90, significantly blocked the myricitrin-induced cardioprotective effect demonstrated by increased apoptosis and ROS generation.	myricitrin	118-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
28642708-7	2017	Further mechanistic investigation revealed that 17-AAG, a pharmacologic inhibitor of Hsp90, significantly blocked the myricitrin-induced cardioprotective effect demonstrated by increased apoptosis and ROS generation.	ros	201-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
28642708-8	2017	These results suggested that myricitrin provides protection to H9c2 cardiomyocytes against H/R-induced oxidative stress and apoptosis, most likely via increased expression of Hsp90.	myricitrin	29-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
28301080-0	2017	HSP90 inhibitor AUY922 can reverse Fulvestrant induced feedback reaction in human breast cancer cells.	Fulvestrant	35-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28190264-6	2017	Cytokine-induced beta cell hsp90alpha release and JNK activation were significantly reduced by pre-treating cells with the endoplasmic reticulum stress-mitigating chemical chaperone tauroursodeoxycholic acid.	ursodoxicoltaurine	182-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-37
28383119-1	2017	Hsp90 is a dimeric molecular chaperone that undergoes an essential and highly regulated open-to-closed-to-open conformational cycle upon ATP binding and hydrolysis.	Adenosine Triphosphate	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28383119-2	2017	Although it has been established that a large energy barrier to closure is responsible for Hsp90"s low ATP hydrolysis rate, the specific molecular contacts that create this energy barrier are not known.	Adenosine Triphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
28915577-4	2017	Through an in-vitro and in-vivo approach utilizing cell lines for hepatocellular carcinoma (HCC), osteosarcoma (OS), and glioblastoma (GBM), we demonstrate that SAHA potently inhibits HIF-a nuclear translocation via direct acetylation of its associated chaperone, heat shock protein 90 (Hsp90).	Vorinostat	161-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	264-285
28591051-4	2017	Binary logistic regression identified that HSPN was independently associated with age, RDW, platelet, and total cholesterol (odds ratio = 1.409, 1.353, 0.996, and 2.019, respectively).	Cholesterol	112-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-47
28537252-4	2017	Phosphorylation of human Hsp90alpha at the highly conserved tyrosine 627 has previously been reported to reduce client interaction and Aha1 binding.	Tyrosine	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-35
28915577-4	2017	Through an in-vitro and in-vivo approach utilizing cell lines for hepatocellular carcinoma (HCC), osteosarcoma (OS), and glioblastoma (GBM), we demonstrate that SAHA potently inhibits HIF-a nuclear translocation via direct acetylation of its associated chaperone, heat shock protein 90 (Hsp90).	Vorinostat	161-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	287-292
28915577-5	2017	In the presence of SAHA we found elevated levels of acetyl-Hsp90, decreased interaction between acetyl-Hsp90 and HIF-a, decreased nuclear/cytoplasmic HIF-alpha expression, absent HIF-alpha association with its nuclear karyopharyin Importin, and markedly decreased HIF-a transcriptional activity.	Vorinostat	19-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
28915577-5	2017	In the presence of SAHA we found elevated levels of acetyl-Hsp90, decreased interaction between acetyl-Hsp90 and HIF-a, decreased nuclear/cytoplasmic HIF-alpha expression, absent HIF-alpha association with its nuclear karyopharyin Importin, and markedly decreased HIF-a transcriptional activity.	Vorinostat	19-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
28542269-4	2017	Exposure of cancer cells to HSP90 inhibitors, including 17-AAG, has been shown to cause resistance to chemotherapeutic treatment mostly attributable to induction of the heat shock response and increased cellular levels of pro-survival chaperones.	tanespimycin	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
28542269-5	2017	In this study, we show that treatment of glioblastoma cells with 17-AAG leads to HSP90 inhibition indicated by loss of stability of the EGFR client protein, and significant increase in HSP70 expression.	tanespimycin	65-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
28380438-11	2017	The signal was also reduced when cells were treated with 17-N-allylamino-17-demethoxygeldanamycin, an HSP90 inhibitor that inhibits HIF-1alpha.	tanespimycin	57-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
28412368-0	2017	HSP90 inhibitor NVP-AUY922 induces cell apoptosis by disruption of the survivin in papillary thyroid carcinoma cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28167505-0	2017	Acquired Resistance to the Hsp90 Inhibitor, Ganetespib, in KRAS-Mutant NSCLC Is Mediated via Reactivation of the ERK-p90RSK-mTOR Signaling Network.	STA 9090	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
28167505-3	2017	Here, we examined the mechanism(s) of acquired resistance to the Hsp90 inhibitor, ganetespib, and identified novel and rationally devised Hsp90 inhibitor combinations, which may prevent and overcome resistance to Hsp90 inhibitors.	STA 9090	82-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
28167505-3	2017	Here, we examined the mechanism(s) of acquired resistance to the Hsp90 inhibitor, ganetespib, and identified novel and rationally devised Hsp90 inhibitor combinations, which may prevent and overcome resistance to Hsp90 inhibitors.	STA 9090	82-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
28412732-5	2017	We also evaluated the expression of HSP90 by immunohistochemistry in human GBC tumors.In vitro assays showed that 17-AAG and GA significantly reduced the expression of HSP90 target proteins, including EGFR, AKT, phospho-AKT, Cyclin B1, phospho-ERK and Cyclin D1.	geldanamycin	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
28306192-4	2017	To investigate mechanisms of resistance, we generated resistant cell lines through gradual dose escalation of the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	130-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
28306192-4	2017	To investigate mechanisms of resistance, we generated resistant cell lines through gradual dose escalation of the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	170-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
28306192-8	2017	Most significantly, resistant cells were also identified as cross-resistant towards structurally distinct HSP90 inhibitors such as radicicol and the second-generation HSP90 inhibitors CCT018159, VER50589 and AUY922.	monorden	131-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
28306192-10	2017	In conclusion, we report that prolonged 17-AAG treatment results in acquired resistance of cancer cells towards not just 17-AAG but also to a spectrum of structurally distinct HSP90 inhibitors.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
28412732-5	2017	We also evaluated the expression of HSP90 by immunohistochemistry in human GBC tumors.In vitro assays showed that 17-AAG and GA significantly reduced the expression of HSP90 target proteins, including EGFR, AKT, phospho-AKT, Cyclin B1, phospho-ERK and Cyclin D1.	geldanamycin	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
28153791-3	2017	In this study, we show that an HDAC6-selective inhibitor, A452, increased wild-type p53 levels by destabilizing MDM2, but decreased mutant p53 by inducing MDM2 and inhibiting Hsp90-mutant p53 complex formation.	Tetramethylammonium azide	58-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
28377614-3	2017	Here we investigated the role of Hsp90 and its co-chaperones during the uptake of native diphtheria toxin into human cells and identified the components of the Hsp90 machinery including Hsp90, Hsp70, Cyp40 and the FK506 binding proteins FKBP51 and FKBP52 as DTA binding partners.	deoxythymidylyl-3'-5'-deoxyadenylate	258-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
28377614-3	2017	Here we investigated the role of Hsp90 and its co-chaperones during the uptake of native diphtheria toxin into human cells and identified the components of the Hsp90 machinery including Hsp90, Hsp70, Cyp40 and the FK506 binding proteins FKBP51 and FKBP52 as DTA binding partners.	deoxythymidylyl-3'-5'-deoxyadenylate	258-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
28529458-5	2017	Mechanically, 17-DMAG treatment inhibited a complex network consists at least ERK, AKT, and Hippo pathway in TNBC cells, and higher expression of HDAC6 inhibited HSP90 activity via deacetylating HSP90.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	14-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
28915605-2	2017	In this study, we determined the therapeutic effects and mechanisms of action of a specific HSP90 inhibitor, 17-dimethylamino-ethylamino-17-demethoxygeldanamycin (17-DMAG), in gastric cancer cell lines (AGS, SNU-1, and KATO-III), patient-derived tissues, and a mouse xenograft model.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	109-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
28915605-2	2017	In this study, we determined the therapeutic effects and mechanisms of action of a specific HSP90 inhibitor, 17-dimethylamino-ethylamino-17-demethoxygeldanamycin (17-DMAG), in gastric cancer cell lines (AGS, SNU-1, and KATO-III), patient-derived tissues, and a mouse xenograft model.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	163-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
28153791-8	2017	Furthermore, it chemosensitized cancer cells to the Hsp90 inhibitor 17-AAG.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
28278223-6	2017	The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90.	carboxylate	4-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
28236106-8	2017	Inhibition of HSP90 by geldanamycin or 17-AAG did not affect basal motility, but suppressed progesterone-mediated forward progressive motility, hyperactivation and acrosome reaction.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
28236106-8	2017	Inhibition of HSP90 by geldanamycin or 17-AAG did not affect basal motility, but suppressed progesterone-mediated forward progressive motility, hyperactivation and acrosome reaction.	Progesterone	92-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
28236106-9	2017	Progesterone treatment dephosphorylated both HSP90alpha and HSP90beta at Ser/Thr-Pro residues, but not Tyr residues.	Progesterone	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
28236106-9	2017	Progesterone treatment dephosphorylated both HSP90alpha and HSP90beta at Ser/Thr-Pro residues, but not Tyr residues.	Serine	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
28471204-11	2017	CONCLUSIONS: Our analysis has shown that import of HSP90 inhibitors is likely dependent on membrane level of HSP90 as well as its total expression, and therefore can potentially reflect HSP90 addiction of cancer cells.Key words: breast neoplasms - HSP90 - heat shock proteins - geldanamycin This work was supported by MEYS - NPS I - LO1413.	geldanamycin	278-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28471204-11	2017	CONCLUSIONS: Our analysis has shown that import of HSP90 inhibitors is likely dependent on membrane level of HSP90 as well as its total expression, and therefore can potentially reflect HSP90 addiction of cancer cells.Key words: breast neoplasms - HSP90 - heat shock proteins - geldanamycin This work was supported by MEYS - NPS I - LO1413.	geldanamycin	278-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
28471204-11	2017	CONCLUSIONS: Our analysis has shown that import of HSP90 inhibitors is likely dependent on membrane level of HSP90 as well as its total expression, and therefore can potentially reflect HSP90 addiction of cancer cells.Key words: breast neoplasms - HSP90 - heat shock proteins - geldanamycin This work was supported by MEYS - NPS I - LO1413.	geldanamycin	278-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
28471204-11	2017	CONCLUSIONS: Our analysis has shown that import of HSP90 inhibitors is likely dependent on membrane level of HSP90 as well as its total expression, and therefore can potentially reflect HSP90 addiction of cancer cells.Key words: breast neoplasms - HSP90 - heat shock proteins - geldanamycin This work was supported by MEYS - NPS I - LO1413.	geldanamycin	278-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
28454472-0	2017	Hsp90 inhibitor SY-016 induces G2/M arrest and apoptosis in paclitaxel-resistant human ovarian cancer cells.	sy-016	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28454472-0	2017	Hsp90 inhibitor SY-016 induces G2/M arrest and apoptosis in paclitaxel-resistant human ovarian cancer cells.	Paclitaxel	60-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28454472-1	2017	The aim of the present study was to evaluate the in vitro effect of a heat shock protein (Hsp)90 inhibitor, SY-016, on the paclitaxel (PTX)-resistant human ovarian cancer cell line OVCAR-3PTX, and explore its mechanism of apoptosis.	sy-016	108-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-96
28454472-1	2017	The aim of the present study was to evaluate the in vitro effect of a heat shock protein (Hsp)90 inhibitor, SY-016, on the paclitaxel (PTX)-resistant human ovarian cancer cell line OVCAR-3PTX, and explore its mechanism of apoptosis.	Paclitaxel	123-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-96
28454472-1	2017	The aim of the present study was to evaluate the in vitro effect of a heat shock protein (Hsp)90 inhibitor, SY-016, on the paclitaxel (PTX)-resistant human ovarian cancer cell line OVCAR-3PTX, and explore its mechanism of apoptosis.	Paclitaxel	135-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-96
28109840-7	2017	Replacement of the phosphorylation site by glutamate affects the conformational dynamics of Hsp90 and interaction with the kinase-specific cochaperone Cdc37.	Glutamic Acid	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	105-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	105-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	105-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	105-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	113-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	113-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	113-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28139075-2	2017	By evaluating and comparing the impact of a clinical N-terminal heat shock protein 90 (Hsp90) inhibitor, AUY922 (luminespib), on Hsp90 inhibition-associated cellular events in cancer cells versus normal cells, we found that it produces similar phenotype characteristics in both cell types, indicating that AUY922 is not selective for targeting Hsp90 in tumor cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	113-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
28139075-3	2017	By comparison, the C-terminal Hsp90 modulator SM258 suppresses cell proliferation, triggers apoptosis, regulates the expression of Hsp90-associated heat shock proteins, and enhances the degradation of Hsp90"s client proteins preferentially in cancer cells over normal cells.	sm258	46-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
28139075-3	2017	By comparison, the C-terminal Hsp90 modulator SM258 suppresses cell proliferation, triggers apoptosis, regulates the expression of Hsp90-associated heat shock proteins, and enhances the degradation of Hsp90"s client proteins preferentially in cancer cells over normal cells.	sm258	46-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
28139075-3	2017	By comparison, the C-terminal Hsp90 modulator SM258 suppresses cell proliferation, triggers apoptosis, regulates the expression of Hsp90-associated heat shock proteins, and enhances the degradation of Hsp90"s client proteins preferentially in cancer cells over normal cells.	sm258	46-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
28139075-4	2017	Our findings support a new paradigm that AUY922 is not tumor selective, whereas SM258 is more selective and likely acts through an Hsp90-dependent mechanism.	sm258	80-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
28146421-4	2017	AR42 did not alter basal chaperone activity but increased the ability of pazopanib to inhibit HSP90, HSP70 and GRP78.	pazopanib	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
28146421-5	2017	AR42 and pazopanib caused HSP90/HSP70 dissociation from RAF-1 and B-RAF that resulted in reduced "RAF" expression.	pazopanib	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
28081601-3	2017	Herein, we report a novel, multifunctional nanoceria platform loaded with a unique combination of two therapeutic drugs, doxorubicin (Doxo) and Hsp90 inhibitor ganetespib (GT), for the diagnosis and effective treatment of NSCLC.	STA 9090	160-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
27878398-0	2017	HSP90 is a promising target in gemcitabine and 5-fluorouracil resistant pancreatic cancer.	gemcitabine	31-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27878398-0	2017	HSP90 is a promising target in gemcitabine and 5-fluorouracil resistant pancreatic cancer.	Fluorouracil	47-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27878398-4	2017	The aim of this study was to evaluate the efficacy of different HSP90 inhibitors in gemcitabine and 5-FU resistant PC.	gemcitabine	84-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
27878398-4	2017	The aim of this study was to evaluate the efficacy of different HSP90 inhibitors in gemcitabine and 5-FU resistant PC.	Fluorouracil	100-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
27878398-16	2017	HSP90 inhibition disrupts multiple signaling cascades in gemcitabine and 5-FU resistant PC simultaneously and promotes cancer cell apoptosis.	gemcitabine	57-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27878398-16	2017	HSP90 inhibition disrupts multiple signaling cascades in gemcitabine and 5-FU resistant PC simultaneously and promotes cancer cell apoptosis.	Fluorouracil	73-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28255900-9	2017	The differences between HSPC1 inhibitors were also reflected in combination treatment-17-DMAG was more effective compared with NVP-AUY922 in potentiating the cytotoxic effects of 5-fluorouracil, oxaliplatin and irinotecan.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	86-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
28255900-9	2017	The differences between HSPC1 inhibitors were also reflected in combination treatment-17-DMAG was more effective compared with NVP-AUY922 in potentiating the cytotoxic effects of 5-fluorouracil, oxaliplatin and irinotecan.	Fluorouracil	179-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
28255900-9	2017	The differences between HSPC1 inhibitors were also reflected in combination treatment-17-DMAG was more effective compared with NVP-AUY922 in potentiating the cytotoxic effects of 5-fluorouracil, oxaliplatin and irinotecan.	Irinotecan	211-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
28049024-0	2017	1,4-Naphthoquinone activates the HSP90/HSF1 pathway through the S-arylation of HSP90 in A431 cells: Negative regulation of the redox signal transduction pathway by persulfides/polysulfides.	1,4-naphthoquinone	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
28049024-0	2017	1,4-Naphthoquinone activates the HSP90/HSF1 pathway through the S-arylation of HSP90 in A431 cells: Negative regulation of the redox signal transduction pathway by persulfides/polysulfides.	1,4-naphthoquinone	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
28049024-0	2017	1,4-Naphthoquinone activates the HSP90/HSF1 pathway through the S-arylation of HSP90 in A431 cells: Negative regulation of the redox signal transduction pathway by persulfides/polysulfides.	persulfides	164-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
28049024-0	2017	1,4-Naphthoquinone activates the HSP90/HSF1 pathway through the S-arylation of HSP90 in A431 cells: Negative regulation of the redox signal transduction pathway by persulfides/polysulfides.	persulfides	164-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
28049024-0	2017	1,4-Naphthoquinone activates the HSP90/HSF1 pathway through the S-arylation of HSP90 in A431 cells: Negative regulation of the redox signal transduction pathway by persulfides/polysulfides.	polysulfide	176-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
28049024-2	2017	We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ.	1,4-naphthoquinone	81-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-145
28049024-2	2017	We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ.	1,4-naphthoquinone	81-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
28049024-2	2017	We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ.	1,4-naphthoquinone	101-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-145
28049024-2	2017	We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ.	1,4-naphthoquinone	101-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
28049024-2	2017	We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ.	1,4-naphthoquinone	223-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-145
28049024-2	2017	We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ.	1,4-naphthoquinone	223-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
28049024-5	2017	Exposure of A431 cells to 1,4-NQ covalently modified cellular HSP90, resulting in repression of the association between HSF1 with HSP90, thereby enhancing HSF1 translocation into the nuclei.	1,4-naphthoquinone	26-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
28049024-5	2017	Exposure of A431 cells to 1,4-NQ covalently modified cellular HSP90, resulting in repression of the association between HSF1 with HSP90, thereby enhancing HSF1 translocation into the nuclei.	1,4-naphthoquinone	26-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
28049024-11	2017	The results suggest that activation of the HSP90-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.	1,4-naphthoquinone	94-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
28049024-11	2017	The results suggest that activation of the HSP90-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.	1,4-naphthoquinone	124-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
28049024-11	2017	The results suggest that activation of the HSP90-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.	polysulfide	144-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
28049024-11	2017	The results suggest that activation of the HSP90-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.	1,4-naphthoquinone	124-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
28049024-11	2017	The results suggest that activation of the HSP90-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.	Sulfur	206-212	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
28108310-8	2017	We have presented mechanisms by which DOX compromises lysosomal acidification, integrity and chaperone-mediated autophagy through its effect on lysosome-associated and resident proteins such as LAMP, vATPase, Hsp90, Hsc70 and cathepsins.	Doxorubicin	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
28302199-6	2017	RESULTS: The 25-(OH)D3 level in the HSP and HSPN groups was significantly lower than that in the healthy control group (P&lt;0.05), and the 25-(OH)D3 level in the HSPN group was significantly lower than that in the HSP group (P&lt;0.05).	Calcifediol	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-48
28302199-6	2017	RESULTS: The 25-(OH)D3 level in the HSP and HSPN groups was significantly lower than that in the healthy control group (P&lt;0.05), and the 25-(OH)D3 level in the HSPN group was significantly lower than that in the HSP group (P&lt;0.05).	Calcifediol	140-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-167
28236106-9	2017	Progesterone treatment dephosphorylated both HSP90alpha and HSP90beta at Ser/Thr-Pro residues, but not Tyr residues.	Threonine	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
28236106-9	2017	Progesterone treatment dephosphorylated both HSP90alpha and HSP90beta at Ser/Thr-Pro residues, but not Tyr residues.	Proline	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
28236106-10	2017	CONCLUSION: HSP90 levels are downregulated in oligoasthenozoospermia, and its functional inhibition attenuates progesterone-mediated sperm motility and acrosome reaction.	Progesterone	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
28213093-3	2017	Geldanamycin (GDM), a potent inhibitor of Hsp90 was withdrawn from clinical trials due to its undesirable hepatotoxicity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
28213093-3	2017	Geldanamycin (GDM), a potent inhibitor of Hsp90 was withdrawn from clinical trials due to its undesirable hepatotoxicity.	geldanamycin	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
28199108-2	2017	Parallel off-rate measurements against HSP90 and application of structure-based drug design enabled rapid hit to lead progression in a program to identify pan-isoform ATP-competitive inhibitors of PDHK.	Adenosine Triphosphate	167-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
28298630-5	2017	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28298630-5	2017	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.	STA 9090	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28298630-5	2017	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.	SNX 2112	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28298630-5	2017	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28298630-5	2017	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.	CUDC 305	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
28291803-7	2017	Combination of the Hsp70-inducing inhibitors of Hsp90 with known inhibitors of the Hsp induction such as quercetin, triptolide, KNK437, NZ28 prevented up-regulation of Hsp70 in the cancer cells thereby increasing their post-radiation apoptotic/necrotic death and decreasing their post-radiation viability/clonogenicity.	Quercetin	105-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
28291803-7	2017	Combination of the Hsp70-inducing inhibitors of Hsp90 with known inhibitors of the Hsp induction such as quercetin, triptolide, KNK437, NZ28 prevented up-regulation of Hsp70 in the cancer cells thereby increasing their post-radiation apoptotic/necrotic death and decreasing their post-radiation viability/clonogenicity.	triptolide	116-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
28278223-6	2017	The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90.	Lysine	121-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
28278223-6	2017	The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90.	carboxylate	146-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
28278223-6	2017	The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90.	carboxylate	146-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
28278223-6	2017	The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90.	carboxylate	4-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
28278223-6	2017	The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90.	Lysine	121-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
28073608-0	2017	Design, synthesis and biological evaluation of 7-(aryl)-2,3-dihydro-[1,4]dioxino[2,3-g]quinoline derivatives as potential Hsp90 inhibitors and anticancer agents.	7-(aryl)-2,3-dihydro-[1,4]dioxino[2,3-g]quinoline	47-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
28053100-5	2017	The Hsp90 activity was required for L-protein stability and activity because an Hsp90-specific inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), destabilized the MuV L protein and suppressed viral RNA synthesis.	tanespimycin	106-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
28053100-5	2017	The Hsp90 activity was required for L-protein stability and activity because an Hsp90-specific inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), destabilized the MuV L protein and suppressed viral RNA synthesis.	tanespimycin	106-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
28053100-5	2017	The Hsp90 activity was required for L-protein stability and activity because an Hsp90-specific inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), destabilized the MuV L protein and suppressed viral RNA synthesis.	tanespimycin	146-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
28053100-5	2017	The Hsp90 activity was required for L-protein stability and activity because an Hsp90-specific inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), destabilized the MuV L protein and suppressed viral RNA synthesis.	tanespimycin	146-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
27942688-1	2017	Glucosyl-novobiocin-based diazirine photoaffinity labelling reagents (PALs) were designed and synthesized to probe the Hsp90 C-terminal domain unknown binding pocket and the structure-activity relationship.	glucosyl-novobiocin	0-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
27942688-1	2017	Glucosyl-novobiocin-based diazirine photoaffinity labelling reagents (PALs) were designed and synthesized to probe the Hsp90 C-terminal domain unknown binding pocket and the structure-activity relationship.	Diazomethane	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
28003358-5	2017	In HepG2 cells, HSP90 inhibition led to proteasome-dependent degradation of SCAP-SREBP, which resulted in the down-regulation of SREBP target genes and the reduction in intracellular triglyceride and cholesterol levels.	Triglycerides	183-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
28003358-5	2017	In HepG2 cells, HSP90 inhibition led to proteasome-dependent degradation of SCAP-SREBP, which resulted in the down-regulation of SREBP target genes and the reduction in intracellular triglyceride and cholesterol levels.	Cholesterol	200-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
28073914-4	2017	Ulk1-mediated phosphorylation of Ser-339 in Cdc37 compromised the recruitment of client kinases to a complex comprising Cdc37 and heat shock protein 90 (Hsp90) but only modestly affected Cdc37 binding to Hsp90.	Serine	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-151
28073914-4	2017	Ulk1-mediated phosphorylation of Ser-339 in Cdc37 compromised the recruitment of client kinases to a complex comprising Cdc37 and heat shock protein 90 (Hsp90) but only modestly affected Cdc37 binding to Hsp90.	Serine	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
28073914-4	2017	Ulk1-mediated phosphorylation of Ser-339 in Cdc37 compromised the recruitment of client kinases to a complex comprising Cdc37 and heat shock protein 90 (Hsp90) but only modestly affected Cdc37 binding to Hsp90.	Serine	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
28073914-5	2017	Because the recruitment of protein kinase clients to the Hsp90 complex is essential for their stability and functions, Ser-339 phosphorylation of Cdc37 disrupts its ability as a co-chaperone to coordinate Hsp90.	Serine	119-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
27862436-1	2017	The phenotypes produced when cells are treated with the heat shock protein 90 (Hsp90) inhibitors AUY922 or 17-AAG (classical inhibitors) are different to those produced when cells are knocked down with Hsp90alpha.	tanespimycin	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-77
27862436-1	2017	The phenotypes produced when cells are treated with the heat shock protein 90 (Hsp90) inhibitors AUY922 or 17-AAG (classical inhibitors) are different to those produced when cells are knocked down with Hsp90alpha.	tanespimycin	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
27862436-1	2017	The phenotypes produced when cells are treated with the heat shock protein 90 (Hsp90) inhibitors AUY922 or 17-AAG (classical inhibitors) are different to those produced when cells are knocked down with Hsp90alpha.	tanespimycin	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	202-212
28036294-0	2017	Hsp90 N- and C-terminal double inhibition synergistically suppresses Bcr-Abl-positive human leukemia cells.	lauric acid	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28036294-4	2017	Present studies demonstrate that double inhibition of the N- and C-terminal termini can disrupt Hsp90 chaperone function synergistically, but not antagonistically, in Bcr-Abl-positive human leukemia cells.	lauric acid	171-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
28073608-1	2017	A new series of quinoline analogues was designed and synthesized as Hsp90 inhibitors.	quinoline	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
28073608-6	2017	Molecular modeling studies displayed possible mode of interaction between this compound and N-terminal ATP-binding site of Hsp90.	Adenosine Triphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
27834954-2	2017	The HSP90 inhibitor ganetespib is currently being assessed in advanced clinical oncology trials.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26983679-2	2017	Recent Advances: The chaperone heat shock protein 90 (hsp90) associates with signaling proteins in cells, including sGC, where it helps to drive heme insertion into the sGC-beta1 subunit.	Heme	145-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-52
26983679-2	2017	Recent Advances: The chaperone heat shock protein 90 (hsp90) associates with signaling proteins in cells, including sGC, where it helps to drive heme insertion into the sGC-beta1 subunit.	Heme	145-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
26983679-4	2017	CRITICAL ISSUES: In this article, we review evidence to date regarding the mechanisms that modulate sGC activity by a pathway where binding of hsp90 or sGC agonist to heme-free sGC dictates the assembly and fate of an active sGC heterodimer, both by NO and heme-dependent or heme-independent pathways.	Heme	167-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
26983679-4	2017	CRITICAL ISSUES: In this article, we review evidence to date regarding the mechanisms that modulate sGC activity by a pathway where binding of hsp90 or sGC agonist to heme-free sGC dictates the assembly and fate of an active sGC heterodimer, both by NO and heme-dependent or heme-independent pathways.	Heme	257-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
26983679-4	2017	CRITICAL ISSUES: In this article, we review evidence to date regarding the mechanisms that modulate sGC activity by a pathway where binding of hsp90 or sGC agonist to heme-free sGC dictates the assembly and fate of an active sGC heterodimer, both by NO and heme-dependent or heme-independent pathways.	Heme	257-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
27834954-7	2017	HSP90 inhibition caused the rapid decay of key components of the Fanconi anemia pathway required for repair of carboplatin-induced interstrand crosslinks (ICLs), as well as of cell cycle checkpoint mediators.	Carboplatin	111-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27600766-5	2017	RESULTS: Inhibitors of the PARP DNA repair pathway, olaparib and rucaparib, and the HSP90 inhibitor 17-DMAG, enhanced the clonogenic cell kill and spheroid growth delay induced by X-radiation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	100-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
27557816-4	2017	Inhibition of Hsp90 by treatment of porcine monocytic line 3D4/31 with geldanamycin (GA), a specific inhibitor of Hsp90, caused a 70 % decrease in viral Cap protein expression.	geldanamycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
27557816-4	2017	Inhibition of Hsp90 by treatment of porcine monocytic line 3D4/31 with geldanamycin (GA), a specific inhibitor of Hsp90, caused a 70 % decrease in viral Cap protein expression.	geldanamycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
27557816-4	2017	Inhibition of Hsp90 by treatment of porcine monocytic line 3D4/31 with geldanamycin (GA), a specific inhibitor of Hsp90, caused a 70 % decrease in viral Cap protein expression.	geldanamycin	85-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
27557816-4	2017	Inhibition of Hsp90 by treatment of porcine monocytic line 3D4/31 with geldanamycin (GA), a specific inhibitor of Hsp90, caused a 70 % decrease in viral Cap protein expression.	geldanamycin	85-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
28143445-0	2017	HSP90 inhibition sensitizes head and neck cancer to platin-based chemoradiotherapy by modulation of the DNA damage response resulting in chromosomal fragmentation.	Platinum	52-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
28143445-4	2017	Here, we evaluated the HSP90 inhibitor, AUY922, combined with CCRT.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
28032595-3	2017	To prospectively identify mechanisms through which HSP90-dependent cancer cells evade pharmacologic HSP90 blockade, we generated multiple mutant KRAS-driven cancer cell lines with acquired resistance to the purine-scaffold HSP90 inhibitor PU-H71.	purine	207-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
28032595-6	2017	Finally, comparison with structurally distinct HSP90 inhibitors currently in clinical development revealed that PU-H71 resistance could be overcome, in part, by ganetespib (also known as STA9090) but not tanespimycin (also known as 17-AAG).	STA 9090	161-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
27791982-6	2017	We found that ErbB2 inhibition by lapatinib inhibits transcription factor HSF1, and its target Hsp90, followed by mutant p53 degradation in MDM2 dependent manner.	Lapatinib	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
28088573-3	2017	Many potential inhibitors of hsp90 have been tested for cancer therapy but their usefulness is limited by their poor solubility in water and their ability to reach the target cells and the correct intracellular compartment.	Water	131-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
28758577-10	2017	We have further on structure-function relationship of HSP90 to understand its efficacy as a new target in AD and PD by utilizing new generation of HSP90 inhibitors such as geldanamycin and its derivatives, 17-AAG, 17-DMAG, IPI-504, radicicol and its derivatives.	tanespimycin	206-212	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
27959508-4	2017	In the current study, a structure-based approach has been applied to a Grp94 nonselective compound, SNX 2112, which led to the development of 8j (ACO1), a Grp94-selective inhibitor that manifests ~440 nM affinity and &gt;200-fold selectivity against cytosolic Hsp90 isoforms.	SNX 2112	100-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	260-265
27959508-4	2017	In the current study, a structure-based approach has been applied to a Grp94 nonselective compound, SNX 2112, which led to the development of 8j (ACO1), a Grp94-selective inhibitor that manifests ~440 nM affinity and &gt;200-fold selectivity against cytosolic Hsp90 isoforms.	8j	142-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	260-265
27688186-0	2017	Design, synthesis and pharmacological evaluation of 4,5-diarylisoxazols bearing amino acid residues within the 3-amido motif as potent heat shock protein 90 (Hsp90) inhibitors.	4,5-diarylisoxazols	52-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-156
27688186-0	2017	Design, synthesis and pharmacological evaluation of 4,5-diarylisoxazols bearing amino acid residues within the 3-amido motif as potent heat shock protein 90 (Hsp90) inhibitors.	4,5-diarylisoxazols	52-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
27688186-0	2017	Design, synthesis and pharmacological evaluation of 4,5-diarylisoxazols bearing amino acid residues within the 3-amido motif as potent heat shock protein 90 (Hsp90) inhibitors.	3-amido	111-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-156
27688186-0	2017	Design, synthesis and pharmacological evaluation of 4,5-diarylisoxazols bearing amino acid residues within the 3-amido motif as potent heat shock protein 90 (Hsp90) inhibitors.	3-amido	111-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
27688186-1	2017	A structure-based medicinal chemistry optimization was conducted on the clinical Hsp90 inhibitor diarylisoxazole 3.	diarylisoxazole	97-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
27903966-4	2017	[Pemetrexed + sildenafil] reduced the expression of c-FLIP-s, MCL-1 and BCL-XL that was blocked in a cell-type -dependent fashion by either over-expression of HSP90 / GRP78 / HSP70 / HSP27 or by blockade of eIF2alpha-CHOP signaling.	Pemetrexed	1-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
27903966-4	2017	[Pemetrexed + sildenafil] reduced the expression of c-FLIP-s, MCL-1 and BCL-XL that was blocked in a cell-type -dependent fashion by either over-expression of HSP90 / GRP78 / HSP70 / HSP27 or by blockade of eIF2alpha-CHOP signaling.	Sildenafil Citrate	14-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
27903966-6	2017	Pemetrexed reduced the ATPase activities of HSP90 and HSP70 in an ATM-AMPK-dependent fashion that was enhanced by sildenafil signaling via PKGI/II.	Pemetrexed	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
27903966-6	2017	Pemetrexed reduced the ATPase activities of HSP90 and HSP70 in an ATM-AMPK-dependent fashion that was enhanced by sildenafil signaling via PKGI/II.	Sildenafil Citrate	114-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
27770383-0	2017	Chalcone-templated Hsp90 inhibitors and their effects on gefitinib resistance in non-small cell lung cancer (NSCLC).	Chalcone	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
27770383-0	2017	Chalcone-templated Hsp90 inhibitors and their effects on gefitinib resistance in non-small cell lung cancer (NSCLC).	Gefitinib	57-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
27770383-2	2017	In this study, we designed and synthesized a series of Hsp90 inhibitors that hybridized NVP-AUY992 (2) and PU3 (3) in the chalcone scaffold using a structure-based approach.	pu3 (3)	107-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27770383-2	2017	In this study, we designed and synthesized a series of Hsp90 inhibitors that hybridized NVP-AUY992 (2) and PU3 (3) in the chalcone scaffold using a structure-based approach.	Chalcone	122-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27770383-4	2017	The compound 1g represents a new class of Hsp90 inhibitors with a chalcone structure.	Chalcone	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
27959508-0	2017	Transformation of the Non-Selective Aminocyclohexanol-Based Hsp90 Inhibitor into a Grp94-Seletive Scaffold.	aminocyclohexanol	36-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
27959508-3	2017	Although, the N-terminal ATP binding site is highly conserved among all four Hsp90 isoforms, recent cocrystal structures of Grp94 have revealed subtle differences between Grp94 and other Hsp90 isoforms that has been exploited for the development of Grp94-selective inhibitors.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
27779106-5	2017	STA-12-8666 selectively binds activated HSP90 and releases its cytotoxic payload resulting in drug accumulation in pancreatic cancer cells in vivo.	sta-12	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
27863422-5	2017	Two drugs, auranofin, a thioredoxin reductase inhibitor, and ganetespib, an HSP90 inhibitor, were predicted to have anti-cancer activities in silico and were confirmed active across a panel of genetically diverse EWS cells.	STA 9090	61-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
27793846-6	2017	Notably, non-small cell lung cancer cells (NSCLC) positive for p14ARF were sensitive to treatment with the HSP90 inhibitor geldanamycin.	geldanamycin	123-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
27913182-2	2017	The chaperone activity of HSP90 is regulated by the hydrolysis of ATP at the protein"s N-terminal domain.	Adenosine Triphosphate	66-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
27913182-4	2017	This paper describes an application of virtual screening, thermal shift assaying and protein NMR spectroscopy leading to the discovery of HSP90 inhibitors that contain the resorcinol structure.	resorcinol	172-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
27913182-5	2017	The resorcinol scaffold can be found in a class of HSP90 inhibitors that are currently undergoing clinical trials.	resorcinol	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
27913182-6	2017	The proved success of the resorcinol moiety in HSP90 inhibitors validates this combined virtual screen and biophysical technique approach, which may be applied for future inhibitor discovery work for HSP90 as well as other targets.	resorcinol	26-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
27913182-6	2017	The proved success of the resorcinol moiety in HSP90 inhibitors validates this combined virtual screen and biophysical technique approach, which may be applied for future inhibitor discovery work for HSP90 as well as other targets.	resorcinol	26-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
27914802-0	2017	Synthesis and in vitro antiproliferative activity of C5-benzyl substituted 2-amino-pyrrolo[2,3-d]pyrimidines as potent Hsp90 inhibitors.	c5-benzyl substituted 2-amino-pyrrolo[2,3-d]pyrimidines	53-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
27914802-1	2017	A novel series of heat shock protein 90 (Hsp90) inhibitors was identified by X-ray crystal analysis of complex structures at solvent-exposed exit pocket C. The 2-amino-pyrrolo[2,3-d]pyrimidine derivatives, 7-deazapurines substituted with a benzyl moiety at C5, showed potent Hsp90 inhibition and broad-spectrum antiproliferative activity against NCI-60 cancer cell lines.	7H-Pyrrolo[2,3-d]pyrimidin-2-amine	160-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
27914802-1	2017	A novel series of heat shock protein 90 (Hsp90) inhibitors was identified by X-ray crystal analysis of complex structures at solvent-exposed exit pocket C. The 2-amino-pyrrolo[2,3-d]pyrimidine derivatives, 7-deazapurines substituted with a benzyl moiety at C5, showed potent Hsp90 inhibition and broad-spectrum antiproliferative activity against NCI-60 cancer cell lines.	7H-Pyrrolo[2,3-d]pyrimidin-2-amine	160-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
27914802-1	2017	A novel series of heat shock protein 90 (Hsp90) inhibitors was identified by X-ray crystal analysis of complex structures at solvent-exposed exit pocket C. The 2-amino-pyrrolo[2,3-d]pyrimidine derivatives, 7-deazapurines substituted with a benzyl moiety at C5, showed potent Hsp90 inhibition and broad-spectrum antiproliferative activity against NCI-60 cancer cell lines.	7H-Pyrrolo[2,3-d]pyrimidin-2-amine	160-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	275-280
27914802-1	2017	A novel series of heat shock protein 90 (Hsp90) inhibitors was identified by X-ray crystal analysis of complex structures at solvent-exposed exit pocket C. The 2-amino-pyrrolo[2,3-d]pyrimidine derivatives, 7-deazapurines substituted with a benzyl moiety at C5, showed potent Hsp90 inhibition and broad-spectrum antiproliferative activity against NCI-60 cancer cell lines.	7-deazapurine	206-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
27914802-1	2017	A novel series of heat shock protein 90 (Hsp90) inhibitors was identified by X-ray crystal analysis of complex structures at solvent-exposed exit pocket C. The 2-amino-pyrrolo[2,3-d]pyrimidine derivatives, 7-deazapurines substituted with a benzyl moiety at C5, showed potent Hsp90 inhibition and broad-spectrum antiproliferative activity against NCI-60 cancer cell lines.	7-deazapurine	206-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
27914802-3	2017	The interaction of 6a at the ATP-binding pocket of Hsp90 was confirmed by X-ray crystallography and Western blot analysis.	Adenosine Triphosphate	29-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
27914946-0	2017	Design, synthesis and biological evaluation of alkylamino biphenylamides as Hsp90 C-terminal inhibitors.	alkylamino biphenylamides	47-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
27914946-2	2017	Novobiocin, a coumarin antibiotic, was the first natural product identified that targeted the Hsp90 C-terminal domain and manifested anti-proliferative activity (SKBr3 IC50~700muM).	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
27887849-4	2017	A2780cis cells revealed the same fold of resistance to Hsp90 inhibitor 17-DMAG as it is declared for cisplatin (18 times), but only 3.2 times for thiazine[6,5-b]indole.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27887849-4	2017	A2780cis cells revealed the same fold of resistance to Hsp90 inhibitor 17-DMAG as it is declared for cisplatin (18 times), but only 3.2 times for thiazine[6,5-b]indole.	Cisplatin	101-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27887849-10	2017	Our results signify antiproliferative and pro-apoptotic effects of novel thiazine[6,5-b]indole potentiated by Hsp90 inhibitor 17-DMAG in ovarian adenocarcinoma cells resistant to cisplatin and therefore represents new strategy in cancer treatment.	thiazine[6,5-b]indole	73-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
27887849-10	2017	Our results signify antiproliferative and pro-apoptotic effects of novel thiazine[6,5-b]indole potentiated by Hsp90 inhibitor 17-DMAG in ovarian adenocarcinoma cells resistant to cisplatin and therefore represents new strategy in cancer treatment.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	126-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
27818030-0	2017	Optimization and bioevaluation of Cdc37-derived peptides: An insight into Hsp90-Cdc37 protein-protein interaction modulators.	Peptides	48-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
29035890-8	2017	RESULTS: Correspondingly, the clinical data showed APAP-administered patients resulted in increased Hsp90 levels in serum when compared to other clinical parameters of liver injury.	Acetaminophen	51-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
28758577-10	2017	We have further on structure-function relationship of HSP90 to understand its efficacy as a new target in AD and PD by utilizing new generation of HSP90 inhibitors such as geldanamycin and its derivatives, 17-AAG, 17-DMAG, IPI-504, radicicol and its derivatives.	tanespimycin	223-230	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
28758577-10	2017	We have further on structure-function relationship of HSP90 to understand its efficacy as a new target in AD and PD by utilizing new generation of HSP90 inhibitors such as geldanamycin and its derivatives, 17-AAG, 17-DMAG, IPI-504, radicicol and its derivatives.	monorden	232-241	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
27573064-3	2017	These quadruplex structures can be formed by sequences containing repetitive guanine-rich tracks and the analysis of Non-B-DNA database indicated an enrichment of these sequences in genomic regions controlling cellular proliferation, such as for example in the promoter regions of c- MYC, k-RAS, c-KIT, HSP90 and VEGF among others.	Guanine	77-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	303-308
28758577-10	2017	We have further on structure-function relationship of HSP90 to understand its efficacy as a new target in AD and PD by utilizing new generation of HSP90 inhibitors such as geldanamycin and its derivatives, 17-AAG, 17-DMAG, IPI-504, radicicol and its derivatives.	geldanamycin	172-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
27231111-1	2017	BACKGROUND &amp; OBJECTIVE: The Hsp90 chaperone protein regulates the folding, maturation and stability of a wide variety of oncoproteins.	Adenosine Monophosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
28670440-4	2017	Using this approach, we find that 75% of melanoma cell lines can be treated with either the MEK inhibitor AZD6244 or the HSP90 inhibitor 17AAG.	tanespimycin	137-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
28019639-2	2017	METHOD: More recently, novobiocin was found to act also on eukaryotic cells by blocking the 90 kDa heat shock protein (Hsp90).	Novobiocin	23-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
28019639-4	2017	As opposed to the geldanamycin and radicicol, the known inhibitors of Hsp90 that bind to the N-terminal region, the binding domain of novobiocin is localized in the C-terminal part of this protein.	Novobiocin	134-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
28062703-0	2017	TAS-116, a Novel Hsp90 Inhibitor, Selectively Enhances Radiosensitivity of Human Cancer Cells to X-rays and Carbon Ion Radiation.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
28062703-0	2017	TAS-116, a Novel Hsp90 Inhibitor, Selectively Enhances Radiosensitivity of Human Cancer Cells to X-rays and Carbon Ion Radiation.	Carbon	108-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
28062703-2	2017	TAS-116 is a novel Hsp90 inhibitor with lower adverse effects than other Hsp90 inhibitors, and here, we investigated the radiosensitizing effects of TAS-116 in low linear energy transfer (LET) X-ray and high LET carbon ion-irradiated human cancer cells and mouse tumor xenografts.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
27863425-2	2016	Therapeutic HSP90 inhibitors, i.e. Geldanamycin (GA), target ERBB2 to degradation.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
27863425-2	2016	Therapeutic HSP90 inhibitors, i.e. Geldanamycin (GA), target ERBB2 to degradation.	geldanamycin	49-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
27859703-4	2016	Classical inhibitors that block the binding of adenine triphosphate (ATP) to the N-terminus of Hsp90 are highly toxic to cells and trigger a resistance mechanism within cells.	adenine triphosphate	47-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
27859703-4	2016	Classical inhibitors that block the binding of adenine triphosphate (ATP) to the N-terminus of Hsp90 are highly toxic to cells and trigger a resistance mechanism within cells.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
27738310-2	2016	An Hsp90 isoform (Hsp90alpha) has been shown to be selectively phosphorylated on two N-terminal threonine residues (threonine 5 and 7) and is involved in the DNA damage response and apoptosis.	Threonine	96-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-28
27738310-2	2016	An Hsp90 isoform (Hsp90alpha) has been shown to be selectively phosphorylated on two N-terminal threonine residues (threonine 5 and 7) and is involved in the DNA damage response and apoptosis.	Threonine	116-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-28
27738310-10	2016	Thus, this study provides evidence that Hsp90alpha is a component of the signal transduction events mediated by ATM following IR, and that Hsp90alpha loss decreases gammaH2AX levels.	gammah2ax	165-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-149
27616574-0	2016	Targeting Hsp90 with FS-108 circumvents gefitinib resistance in EGFR mutant non-small cell lung cancer cells.	Gefitinib	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
27616574-11	2016	CONCLUSION: FS-108 is a powerful agent that impacts the survival of gefitinib-resistant cells in vitro and in vivo through targeting Hsp90.	Gefitinib	68-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
27354472-0	2016	Hsp90 Inhibitor Ganetespib Sensitizes Non-Small Cell Lung Cancer to Radiation but Has Variable Effects with Chemoradiation.	STA 9090	16-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27880046-0	2017	Docosahexaenoic Acid-mediated Inhibition of Heat Shock Protein 90-p23 Chaperone Complex and Downstream Client Proteins in Lung and Breast Cancer.	Docosahexaenoic Acids	0-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-65
27880046-2	2017	Specific Hsp90 inhibitors have been designed to target the ATP-binding site in order to prevent Hsp90 chaperone maturation.	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
27880046-2	2017	Specific Hsp90 inhibitors have been designed to target the ATP-binding site in order to prevent Hsp90 chaperone maturation.	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
27880046-3	2017	The current study investigated the effects of docosahexaenoic acid (DHA; C22:6 n-3) on Hsp90 function and downstream client protein expression.	Docosahexaenoic Acids	46-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
27880046-3	2017	The current study investigated the effects of docosahexaenoic acid (DHA; C22:6 n-3) on Hsp90 function and downstream client protein expression.	Docosahexaenoic Acids	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
27880046-4	2017	In vitro analyses of BT-474 human breast carcinoma and A549 human lung adenocarcinoma cell lines revealed dose-dependent decreases in intracellular ATP levels by DHA treatment, resulting in a significant reduction of Hsp90 and p23 association in both cell lines.	Adenosine Triphosphate	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	217-222
27880046-4	2017	In vitro analyses of BT-474 human breast carcinoma and A549 human lung adenocarcinoma cell lines revealed dose-dependent decreases in intracellular ATP levels by DHA treatment, resulting in a significant reduction of Hsp90 and p23 association in both cell lines.	Docosahexaenoic Acids	162-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	217-222
27880046-6	2017	Similar results were observed when employing 2-deoxyglucose (2-DG), confirming that DHA and 2-DG, both independently and combined, can disturb Hsp90 molecular chaperone function.	Deoxyglucose	45-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
27880046-6	2017	Similar results were observed when employing 2-deoxyglucose (2-DG), confirming that DHA and 2-DG, both independently and combined, can disturb Hsp90 molecular chaperone function.	Deoxyglucose	61-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
27880046-6	2017	Similar results were observed when employing 2-deoxyglucose (2-DG), confirming that DHA and 2-DG, both independently and combined, can disturb Hsp90 molecular chaperone function.	Docosahexaenoic Acids	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
27880046-6	2017	Similar results were observed when employing 2-deoxyglucose (2-DG), confirming that DHA and 2-DG, both independently and combined, can disturb Hsp90 molecular chaperone function.	Deoxyglucose	92-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
27818141-5	2016	Both Hsp90 and p23 triggered the release of RSC from DNA or a nucleosome.	rsc	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
27526951-1	2016	BACKGROUND: While there is compelling rationale to use heat shock protein 90 (Hsp90) inhibitors for treatment of advanced prostate cancer, agents that target the N-terminal ATP-binding site of Hsp90 have shown little clinical benefit.	Adenosine Triphosphate	173-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
27783977-0	2016	Targeting the entry region of Hsp90"s ATP binding pocket with a novel 6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl amide.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
27783977-0	2016	Targeting the entry region of Hsp90"s ATP binding pocket with a novel 6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl amide.	6,7-dihydrothieno(3,2-c)pyridin-5(4H)-yl amide	70-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
27783977-4	2016	Among the synthetic compounds, 6,7-dihydrothieno [3,2-c]pyridin-5(4H)-yl amide 19 exhibits a remarkable binding affinity to the N-terminus of Hsp90 in a fluorescence polarization (FP) binding assay (IC50 = 50.3 nM).	6,7-dihydrothieno(3,2-c)pyridin-5(4H)-yl amide	31-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
27783977-10	2016	Overall, compound 19 represents a new class of Hsp90 inhibitor with its 6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl-amide structure, and it has the therapeutic potential to overcome drug resistance in cancer chemotherapy.	6,7-dihydrothieno(3,2-c)pyridin-5(4H)-yl amide	72-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
27354472-3	2016	We used the potent HSP90 inhibitor ganetespib to determine whether it can enhance CRT effects in NSCLC.	STA 9090	35-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
27742706-0	2016	HSP90 inhibition overcomes ibrutinib resistance in mantle cell lymphoma.	ibrutinib	27-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27742706-4	2016	We reasoned that newer heat shock protein 90 (HSP90) inhibitors could overcome ibrutinib resistance by targeting multiple oncogenic pathways in MCL.	ibrutinib	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-44
27742706-4	2016	We reasoned that newer heat shock protein 90 (HSP90) inhibitors could overcome ibrutinib resistance by targeting multiple oncogenic pathways in MCL.	ibrutinib	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
27663270-1	2016	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone responsible for the activation, maturation, and trafficking of several hundred client proteins in the cell.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
27803431-7	2016	Carbachol activated PKC, augmented phosphorylation of heat shock factor 1 (HSF1) and enhanced expression of heat shock proteins (hsps), hsp70 and hsp90.	Carbachol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
27703006-5	2016	Hsp90 facilitates Ser-621 phosphorylation of CRAF and prevents the kinase from degradation.	Serine	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27745993-5	2016	The docking study of 5 showed a similar binding mode as L-80: it occupied the C-terminal ATP-binding pocket of HSP90, indicating that the anticancer and antiangiogenic activities of 5 were derived from HIF-1alpha destabilization by inhibiting the C-terminal ATP-binding site of hHSP90.	l-80	56-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
27745993-5	2016	The docking study of 5 showed a similar binding mode as L-80: it occupied the C-terminal ATP-binding pocket of HSP90, indicating that the anticancer and antiangiogenic activities of 5 were derived from HIF-1alpha destabilization by inhibiting the C-terminal ATP-binding site of hHSP90.	l-80	56-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	278-284
27745993-5	2016	The docking study of 5 showed a similar binding mode as L-80: it occupied the C-terminal ATP-binding pocket of HSP90, indicating that the anticancer and antiangiogenic activities of 5 were derived from HIF-1alpha destabilization by inhibiting the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
27745993-5	2016	The docking study of 5 showed a similar binding mode as L-80: it occupied the C-terminal ATP-binding pocket of HSP90, indicating that the anticancer and antiangiogenic activities of 5 were derived from HIF-1alpha destabilization by inhibiting the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	278-284
27745993-5	2016	The docking study of 5 showed a similar binding mode as L-80: it occupied the C-terminal ATP-binding pocket of HSP90, indicating that the anticancer and antiangiogenic activities of 5 were derived from HIF-1alpha destabilization by inhibiting the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	258-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
27745993-5	2016	The docking study of 5 showed a similar binding mode as L-80: it occupied the C-terminal ATP-binding pocket of HSP90, indicating that the anticancer and antiangiogenic activities of 5 were derived from HIF-1alpha destabilization by inhibiting the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	258-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	278-284
27452798-7	2016	It was noted that melatonin treatment retained GR into cytoplasm by inhibiting the dissociation of HSP90 from GR-HSP90 complex and enhanced expression of Nrf2/HO-1 and Bcl-2 expression.	Melatonin	18-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
27452798-7	2016	It was noted that melatonin treatment retained GR into cytoplasm by inhibiting the dissociation of HSP90 from GR-HSP90 complex and enhanced expression of Nrf2/HO-1 and Bcl-2 expression.	Melatonin	18-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
27663270-1	2016	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone responsible for the activation, maturation, and trafficking of several hundred client proteins in the cell.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
27647369-0	2016	Optimization and biological evaluation of celastrol derivatives as Hsp90-Cdc37 interaction disruptors with improved druglike properties.	celastrol	42-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
27647369-5	2016	Celastrol, as a natural product, can disrupt the Hsp90-Cdc37 interaction and induce degradation of kinase clients.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
27647369-6	2016	The study conducted here attempted to elucidate the structure-activity relationship of celastrol derivatives as Hsp90-Cdc37 disruptors and to improve the druglike properties.	celastrol	87-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
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
28164660-7	2016	CONCLUSIONS: High serum uric acid may be independently correlated with the development of tubulointerstitial lesions as well as glomerulosclerosis in HSPN.	Uric Acid	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-154
27739328-0	2016	MC1568 inhibits HDAC6/8 activity and influenza A virus replication in lung epithelial cells: role of Hsp90 acetylation.	MC1568	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
27686098-4	2016	We found that REV-ERBalpha binds to the C-terminal portion and GR to the N-terminal portion of HSP90alpha and HSP90beta, a chaperone responsible for the activation of proteins to ensure survival of a cell.	rev-erbalpha	14-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-105
27723736-1	2016	Hsp90 couples ATP hydrolysis to large conformational changes essential for activation of client proteins.	Adenosine Triphosphate	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27543462-5	2016	Attenuation of these effects by molecules targeting p38 and Hsp90 indicated Hsp90 as a possible target for H2S-induced activation of p38.	Hydrogen Sulfide	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
27543462-5	2016	Attenuation of these effects by molecules targeting p38 and Hsp90 indicated Hsp90 as a possible target for H2S-induced activation of p38.	Hydrogen Sulfide	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
27894402-0	2016	HSP90 inhibitor enhances anti-proliferative and apoptotic effects of celecoxib on HT-29 colorectal cancer cells via increasing BAX/BCL-2 ratio.	Celecoxib	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27894402-5	2016	17-Demethoxy-17-allylamino geldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor, shows anti-inflammatory effects via down-regulation of the key mediators of inflammation such as Nuclear Factor kappaB (NF-kB), JAK/Signal Transducer and Activator of Transcription (JAK/STAT).	tanespimycin	0-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-73
27894402-5	2016	17-Demethoxy-17-allylamino geldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor, shows anti-inflammatory effects via down-regulation of the key mediators of inflammation such as Nuclear Factor kappaB (NF-kB), JAK/Signal Transducer and Activator of Transcription (JAK/STAT).	tanespimycin	0-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
27796344-0	2016	Antileukemic Scalarane Sesterterpenoids and Meroditerpenoid from Carteriospongia (Phyllospongia) sp., Induce Apoptosis via Dual Inhibitory Effects on Topoisomerase II and Hsp90.	sesterterpenoids	23-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
27796344-0	2016	Antileukemic Scalarane Sesterterpenoids and Meroditerpenoid from Carteriospongia (Phyllospongia) sp., Induce Apoptosis via Dual Inhibitory Effects on Topoisomerase II and Hsp90.	meroditerpenoid	44-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
27796344-6	2016	Using the molecular docking analysis, 1 exhibited more binding affinity to N-terminal ATP-binding pocket of Hsp90 protein than 17-AAG, a standard Hsp90 inhibitor.	Adenosine Triphosphate	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27796344-6	2016	Using the molecular docking analysis, 1 exhibited more binding affinity to N-terminal ATP-binding pocket of Hsp90 protein than 17-AAG, a standard Hsp90 inhibitor.	Adenosine Triphosphate	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
27796344-6	2016	Using the molecular docking analysis, 1 exhibited more binding affinity to N-terminal ATP-binding pocket of Hsp90 protein than 17-AAG, a standard Hsp90 inhibitor.	tanespimycin	127-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27796344-6	2016	Using the molecular docking analysis, 1 exhibited more binding affinity to N-terminal ATP-binding pocket of Hsp90 protein than 17-AAG, a standard Hsp90 inhibitor.	tanespimycin	127-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
27759563-7	2016	MG treatment affected Hsp90 chaperone activity and decreased its binding to LATS1, a key kinase of the Hippo pathway.	Pyruvaldehyde	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
27805204-0	2016	Correction: Identification of the key structural elements of a dihydropyrimidinone core driving toward more potent Hsp90 C-terminal inhibitors.	thiazolo(2,3-b)dihydropyrimidinone	63-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
27805204-1	2016	Correction for "Identification of the key structural elements of a dihydropyrimidinone core driving toward more potent Hsp90 C-terminal inhibitors" by S. Teracciano et al., Chem.	thiazolo(2,3-b)dihydropyrimidinone	67-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
27673365-0	2016	Emergence of resistance to tyrosine kinase inhibitors in non-small-cell lung cancer can be delayed by an upfront combination with the HSP90 inhibitor onalespib.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	150-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27673365-3	2016	METHODS: The HSP90 inhibitor, onalespib, was combined with either crizotinib or erlotinib in ALK- or EGFR-activated xenograft models respectively (H2228, HCC827).	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
27673365-6	2016	Analysis of H2228 tumours, which had relapsed on crizotinib monotherapy, identified a number of clinically relevant crizotinib resistance mechanisms, suggesting that HSP90 inhibitor treatment was capable of suppressing multiple mechanisms of resistance.	Crizotinib	116-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
27731433-0	2016	Identification of the key structural elements of a dihydropyrimidinone core driving toward more potent Hsp90 C-terminal inhibitors.	thiazolo(2,3-b)dihydropyrimidinone	51-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
27376491-0	2016	Design and synthesis of pyrimidinyl acyl thioureas as novel Hsp90 inhibitors in invasive ductal breast cancer and its bone metastasis.	pyrimidinyl acyl thioureas	24-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
27376491-4	2016	Hsp90 perform these processes through its ATP binding and subsequent hydrolysis energy.	Adenosine Triphosphate	42-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27376491-7	2016	Thus, we designed and synthesized novel pyrimidinyl acyl thiourea derivatives to selectively inhibit Hsp90 alpha in human invasive ductal breast (MCF-7) and human bone osteosarcoma (Saos-2) cell lines.	pyrimidinyl acyl thiourea	40-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-112
27376491-11	2016	Molecular docking studies were also performed to determine interaction between Hsp90 ATPase domain and pyrimidinyl acyl thiourea derivatives.	Thiourea	120-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
27376491-12	2016	The results indicated that the compounds are able to interact with Hsp90 ATP binding pocket and inhibit ATPase function.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
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
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
27769261-9	2016	Up-regulation of Hsp90 and associated decrease in pro-inflammatory cytokine production was found in CD28nullCD8+ T and NKT-like cells in the presence of 10 muM prednisolone and 2.5 ng/mL cyclosporine A.	cd28nullcd8	100-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
27769261-9	2016	Up-regulation of Hsp90 and associated decrease in pro-inflammatory cytokine production was found in CD28nullCD8+ T and NKT-like cells in the presence of 10 muM prednisolone and 2.5 ng/mL cyclosporine A.	Prednisolone	160-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
27769261-9	2016	Up-regulation of Hsp90 and associated decrease in pro-inflammatory cytokine production was found in CD28nullCD8+ T and NKT-like cells in the presence of 10 muM prednisolone and 2.5 ng/mL cyclosporine A.	Cyclosporine	187-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
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
27266997-0	2016	Design and synthesis of N-(5-chloro-2,4-dihydroxybenzoyl)-(R)-1,2,3,4-tetrahydroisoquinoline-3-carboxamides as novel Hsp90 inhibitors.	n-(5-chloro-2,4-dihydroxybenzoyl)-(r)-1,2,3,4-tetrahydroisoquinoline-3-carboxamides	24-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27266997-2	2016	Herein, we reported the design and synthesis of two series of novel N-(5-chloro-2,4-dihydroxybenzoyl)-1,2,3,4-tetrahydroisoquinoline-3- carboxamides as Hsp90 inhibitors using (S)-Tic (1,2,3,4-tetrahydroisoquinoline-3- carboxylic acid) (A1-13) and (R)-Tic (B1-13) as scaffold, respectively.	n-(5-chloro-2,4-dihydroxybenzoyl)-1,2,3,4-tetrahydroisoquinoline-3- carboxamides	68-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
27266997-8	2016	In addition, docking and Molecular dynamics (MD) refinement of the B7-Hsp90 complex showed that the binding model of B7 to Hsp90 was similar with that of 8-benzyladenines.	8-benzyladenines	154-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
27266997-8	2016	In addition, docking and Molecular dynamics (MD) refinement of the B7-Hsp90 complex showed that the binding model of B7 to Hsp90 was similar with that of 8-benzyladenines.	8-benzyladenines	154-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
28090422-4	2016	Importantly, we noted that expression of eL36 and eL42 is elevated in a panel of human rhabdomyosarcomas where it drives high expression of Hsp90 and modulates sensitivity of these cells to an Hsp90 inhibitor 17-AAG.	tanespimycin	209-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
28090422-4	2016	Importantly, we noted that expression of eL36 and eL42 is elevated in a panel of human rhabdomyosarcomas where it drives high expression of Hsp90 and modulates sensitivity of these cells to an Hsp90 inhibitor 17-AAG.	tanespimycin	209-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
27527413-0	2016	Structure-activity relationship of Garcinia xanthones analogues: Potent Hsp90 inhibitors with cytotoxicity and antiangiogenesis activity.	garcinia xanthones	35-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
27527413-2	2016	Gambogic acid (GA), the main active compound of Gamboge hanburyi, has been reported as a natural inhibitor of Hsp90.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
27527413-2	2016	Gambogic acid (GA), the main active compound of Gamboge hanburyi, has been reported as a natural inhibitor of Hsp90.	gambogic acid	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
27527413-3	2016	Here, we present the structure-activity relationship of Garcinia xanthones analogues as Hsp90 inhibitors and identify that compound 25, with a simplified skeleton, had an improved inhibitory effect toward Hsp90.	garcinia xanthones	56-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
27527413-3	2016	Here, we present the structure-activity relationship of Garcinia xanthones analogues as Hsp90 inhibitors and identify that compound 25, with a simplified skeleton, had an improved inhibitory effect toward Hsp90.	garcinia xanthones	56-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
27435264-8	2016	Of interest, under MDD, the bone development effects of 1,25-dihydroxyvitamin D3 were ineffectual and these could be rescued by the addition of S-adenosylmethionine, which restored expression of arginine methyltransferase 1, PGC1alpha, adiponectin, and HSP90.	S-Adenosylmethionine	144-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	253-258
27435264-9	2016	In conclusion, MDD inactivates vitamin D signaling via both disruption of VDR-PGC1alpha interaction and sequestration of nuclear VDR attributable to HSP90 overexpression.	Vitamin D	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
27187154-1	2016	We have recently demonstrated that AR-12 (OSU-03012) reduces the function and ATPase activities of multiple HSP90 and HSP70 family chaperones.	Argon	35-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27187154-1	2016	We have recently demonstrated that AR-12 (OSU-03012) reduces the function and ATPase activities of multiple HSP90 and HSP70 family chaperones.	osu	42-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27187154-6	2016	AR-12-stimulated the co-localization of Influenza, EBV and HIV virus proteins with LC3 in autophagosomes and reduced viral protein association with the chaperones HSP90, HSP70, and GRP78.	OSU 03012	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
27597738-6	2016	At the mechanistic level, neratinib treatment leads to HSP90 release from ErbB2 and its subsequent ubiquitylation and endocytic degradation.	neratinib	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27759563-0	2016	Methylglyoxal, a glycolysis side-product, induces Hsp90 glycation and YAP-mediated tumor growth and metastasis.	Pyruvaldehyde	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
27620500-10	2016	Nematode Cdc37, which does not require the N-terminal Hsp90 domain for binding, can form a ternary complex with the MC construct of Hsp90, which lacks the aggregation propensity of sB-Raf.	Methylcholanthrene	116-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
27620500-12	2016	We thus find that the interaction between sB-Raf and the Hsp90 chaperone system is based on contacts with the M domain of Hsp90, which contributes in forming the ternary complex with CeCdc37 as long as the kinase is not stabilized by nucleotide.	cecdc37	183-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
27620500-12	2016	We thus find that the interaction between sB-Raf and the Hsp90 chaperone system is based on contacts with the M domain of Hsp90, which contributes in forming the ternary complex with CeCdc37 as long as the kinase is not stabilized by nucleotide.	cecdc37	183-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
27498942-0	2016	In vitro study comparing the efficacy of the water-soluble HSP90 inhibitors, 17-AEPGA and 17-DMAG, with that of the non-water-soluble HSP90 inhibitor, 17-AAG, in breast cancer cell lines.	Water	45-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
27530778-0	2016	Thermodynamic Analysis of the Geldanamycin-Hsp90 Interaction in a Whole Cell Lysate Using a Mass Spectrometry-Based Proteomics Approach.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
27530778-2	2016	Heat shock protein 90 (Hsp90) is the known target of geldanamycin, which directly binds to Hsp90"s N-terminal ATP binding domain and inhibits Hsp90"s ATPase activity.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
27530778-3	2016	The affinity of geldanamycin for Hsp90 has been measured in multiple studies.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
27530778-5	2016	Here the stability of proteins from rates of oxidation (SPROX) technique was used in combination with an isobaric mass tagging strategy to measure the binding affinity of geldanamycin to unpurified Hsp90 in an MCF-7 cell lysate.	geldanamycin	171-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	69-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	69-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	390-395
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	390-395
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	390-395
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
27530778-8	2016	These Kd values, which are similar to those previously reported in a geldanamycin-Hsp90 binding study that involved the use of a fluorescently labeled geldanamycin analogue, establish that the slow-tight binding behavior previously observed for the fluorescently labeled geldanamycin analogue is not an artifact of the fluorescent label, but rather an inherent property of the geldanamycin-Hsp90 binding interaction.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	390-395
27530778-9	2016	The slow-tight binding property of this complex may be related to time-dependent conformational changes in Hsp90 and/or to time-dependent chemical changes in geldanamycin, both of which have been previously proposed to explain the slow-tight binding behavior of the geldanamycin-Hsp90 complex.	geldanamycin	158-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	279-284
27530778-9	2016	The slow-tight binding property of this complex may be related to time-dependent conformational changes in Hsp90 and/or to time-dependent chemical changes in geldanamycin, both of which have been previously proposed to explain the slow-tight binding behavior of the geldanamycin-Hsp90 complex.	geldanamycin	266-278	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
27530778-9	2016	The slow-tight binding property of this complex may be related to time-dependent conformational changes in Hsp90 and/or to time-dependent chemical changes in geldanamycin, both of which have been previously proposed to explain the slow-tight binding behavior of the geldanamycin-Hsp90 complex.	geldanamycin	266-278	heat shock protein 90 alpha family class A member 1	Homo sapiens	279-284
27476419-1	2016	Benzoquinone ansamycins are important leads for the discovery of novel inhibitors of heat shock protein 90 (Hsp90), a promising target of cancer chemotherapeutics.	benzoquinone ansamycins	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
27631127-5	2016	In most cases with AR, serum HSP90 decreased to baseline after the treatment.	Argon	19-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
27469073-2	2016	17- N-allylamino- 17-demethoxygeldanamycin (17AAG) was the first Hsp90 inhibitor to enter clinical trials for cancer therapy.	tanespimycin	0-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
27469073-2	2016	17- N-allylamino- 17-demethoxygeldanamycin (17AAG) was the first Hsp90 inhibitor to enter clinical trials for cancer therapy.	tanespimycin	44-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
27492719-0	2016	Identification of Limonol Derivatives as Heat Shock Protein 90 (Hsp90) Inhibitors through a Multidisciplinary Approach.	LIMONOL	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
27492719-0	2016	Identification of Limonol Derivatives as Heat Shock Protein 90 (Hsp90) Inhibitors through a Multidisciplinary Approach.	LIMONOL	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
27492719-2	2016	In an attempt to identify new small molecules modulating the activity of Hsp90, we screened a small library of tetranortriterpenes.	tetranortriterpenes	111-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
27492719-7	2016	Taken together, these results point to limonol-derivatives as promising scaffolds for the design of novel Hsp90alpha inhibitors.	LIMONOL	39-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
27582553-4	2016	The topo II and Hsp90 inhibitors, known to bind to their ATP binding site, were searched.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
27422303-0	2016	A phase II study of the HSP90 inhibitor AUY922 in chemotherapy refractory advanced pancreatic cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
27376828-0	2016	Mechanism of Inhibition of Hsp90 Dimerization by Gyrase B Inhibitor Coumermycin A1 (C-A1) Revealed by Molecular Dynamics Simulations and Thermodynamic Calculations.	coumermycin	68-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
27476419-1	2016	Benzoquinone ansamycins are important leads for the discovery of novel inhibitors of heat shock protein 90 (Hsp90), a promising target of cancer chemotherapeutics.	benzoquinone ansamycins	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27476419-5	2016	In vitro antiproliferative activity and Hsp90 binding affinity of the compounds were determined, suggesting the C18-oxygen of herbimycin A is removable and bulky lipophilic groups can be accommodated at C15 without loss of activity.	herbimycin	126-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
27231263-2	2016	SNX-2112, a novel inhibitor of Hsp90, is a promising drug candidate for treating various types of cancers; however, the insolubility greatly limits its clinical application.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
27549813-1	2016	Here is reported the development of a novel scoring function that performs remarkably well at identifying the native binding pose of a subset of HSP90 inhibitors containing aminopyrimidine or resorcinol based scaffolds.	2-aminopyrimidine	173-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
27549813-1	2016	Here is reported the development of a novel scoring function that performs remarkably well at identifying the native binding pose of a subset of HSP90 inhibitors containing aminopyrimidine or resorcinol based scaffolds.	resorcinol	192-202	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
27549813-5	2016	These results indicate that the specific residues considered by PocketScore are determinant to properly model the interaction between HSP90 and its subset of inhibitors containing aminopyrimidine or resorcinol based scaffolds.	2-aminopyrimidine	180-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27549813-5	2016	These results indicate that the specific residues considered by PocketScore are determinant to properly model the interaction between HSP90 and its subset of inhibitors containing aminopyrimidine or resorcinol based scaffolds.	resorcinol	199-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27562018-2	2016	The present D3R challenge was built around experimental datasets involving Heat shock protein (Hsp) 90, an ATP-dependent molecular chaperone which is an important anticancer drug target.	Adenosine Triphosphate	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-102
27562018-3	2016	The Hsp90 ATP binding site is known to be a challenging target for accurate calculations of ligand binding affinities because of the ligand-dependent conformational changes in the binding site, the presence of ordered waters and the broad chemical diversity of ligands that can bind at this site.	Adenosine Triphosphate	10-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
27448590-4	2016	Remarkably, ELISAs involving selected citrullinated HSP90beta/alpha peptides identified a key epitope corresponding to an internal Arg residue (R502 [HSP90beta]/R510 [HSP90alpha]) that is normally buried within the crystal structure of native/unmodified HSP90.	Arginine	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-177
27448590-4	2016	Remarkably, ELISAs involving selected citrullinated HSP90beta/alpha peptides identified a key epitope corresponding to an internal Arg residue (R502 [HSP90beta]/R510 [HSP90alpha]) that is normally buried within the crystal structure of native/unmodified HSP90.	Arginine	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
27448590-6	2016	Conventional as well as scaled molecular dynamics simulations further demonstrate that citrullination of selected Arg residues leads to progressive disruption of HSP90 tertiary structure, promoting exposure of R502/R510 to PAD modification and subsequent autoantibody binding.	Arginine	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
26764527-0	2016	A phase I trial of the intravenous Hsp90 inhibitor alvespimycin (17-DMAG) in patients with relapsed chronic lymphocytic leukemia/small lymphocytic lymphoma.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
27580824-9	2016	The protein stability of CLC-1 is notably increased by FKBP8 and the Hsp90beta inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) that substantially suppresses cullin 4 expression.	tanespimycin	89-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-78
27580824-9	2016	The protein stability of CLC-1 is notably increased by FKBP8 and the Hsp90beta inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) that substantially suppresses cullin 4 expression.	tanespimycin	129-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-78
27354066-3	2016	We show here that the dietary agent phenethyl isothiocyanate (PEITC) inhibits heat shock protein 90 (Hsp90), the main negative regulator of HSF1; activates p38 mitogen-activated protein kinase (MAPK); and increases S326 phosphorylation, trimerization, and nuclear translocation of HSF1, and the transcription of a luciferase reporter, as well as the endogenous prototypic HSF1 target Hsp70.	phenethyl isothiocyanate	36-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
27354066-3	2016	We show here that the dietary agent phenethyl isothiocyanate (PEITC) inhibits heat shock protein 90 (Hsp90), the main negative regulator of HSF1; activates p38 mitogen-activated protein kinase (MAPK); and increases S326 phosphorylation, trimerization, and nuclear translocation of HSF1, and the transcription of a luciferase reporter, as well as the endogenous prototypic HSF1 target Hsp70.	phenethyl isothiocyanate	36-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
27354066-3	2016	We show here that the dietary agent phenethyl isothiocyanate (PEITC) inhibits heat shock protein 90 (Hsp90), the main negative regulator of HSF1; activates p38 mitogen-activated protein kinase (MAPK); and increases S326 phosphorylation, trimerization, and nuclear translocation of HSF1, and the transcription of a luciferase reporter, as well as the endogenous prototypic HSF1 target Hsp70.	phenethyl isothiocyanate	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
27354066-3	2016	We show here that the dietary agent phenethyl isothiocyanate (PEITC) inhibits heat shock protein 90 (Hsp90), the main negative regulator of HSF1; activates p38 mitogen-activated protein kinase (MAPK); and increases S326 phosphorylation, trimerization, and nuclear translocation of HSF1, and the transcription of a luciferase reporter, as well as the endogenous prototypic HSF1 target Hsp70.	phenethyl isothiocyanate	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
27153346-0	2016	Novel 1,6-naphthyridin-2(1H)-ones as potential anticancer agents targeting Hsp90.	1,6-naphthyridin-2(1h)-ones	6-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
27153346-1	2016	Hsp90 is an ATP-dependent chaperone known to be overexpressed in many cancers.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27153346-3	2016	Novobiocin, an aminocoumarin antibiotic, was reported to inhibit Hsp90 targeting C-terminal domain, and showed anti-proliferative properties, leading to the development of new and more active compounds.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
27563925-3	2016	Additionally, CAF contractility was measured in a 3D collagen contraction assay and migration was measured by scratch assay; RESULTS: HSP90 inhibitors dipalmitoyl-radicicol and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) reduced tumour size and proliferation in CAF/BPH1 reconstituted tumours in vivo.	dipalmitoyl-radicicol	151-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27563925-3	2016	Additionally, CAF contractility was measured in a 3D collagen contraction assay and migration was measured by scratch assay; RESULTS: HSP90 inhibitors dipalmitoyl-radicicol and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) reduced tumour size and proliferation in CAF/BPH1 reconstituted tumours in vivo.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	177-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27563925-3	2016	Additionally, CAF contractility was measured in a 3D collagen contraction assay and migration was measured by scratch assay; RESULTS: HSP90 inhibitors dipalmitoyl-radicicol and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) reduced tumour size and proliferation in CAF/BPH1 reconstituted tumours in vivo.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	230-237	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27563925-3	2016	Additionally, CAF contractility was measured in a 3D collagen contraction assay and migration was measured by scratch assay; RESULTS: HSP90 inhibitors dipalmitoyl-radicicol and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) reduced tumour size and proliferation in CAF/BPH1 reconstituted tumours in vivo.	bph1	284-288	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
27563925-5	2016	HSP90 inhibitors radicicol and 17-DMAG inhibited contractility and reduced the migration of CAF in scratch assays.	monorden	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27563925-5	2016	HSP90 inhibitors radicicol and 17-DMAG inhibited contractility and reduced the migration of CAF in scratch assays.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	31-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27472464-9	2016	In conclusion, HSP90 inhibitor 17-AAG could improve pulmonary arteriole remodeling via inhibiting the excessive proliferation of PASMCs, and inhibition of HSP90 may represent a therapeutic avenue for the treatment of PAH.	pasmcs	129-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
27494878-9	2016	17-AAG, a specific Hsp90, could abrogate the CD24 induce- HUVEC migration, invasion and tubule formation in vitro and in vivo.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
27489107-2	2016	In a high throughput screening for small molecules that induce UHRF1 protein degradation, we have identified the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	129-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
27489107-2	2016	In a high throughput screening for small molecules that induce UHRF1 protein degradation, we have identified the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	169-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
27489107-4	2016	Pharmacological inhibition of HSP90 with 17-AAG or 17-dimethylaminoethylamino-17-demethoxygeldanamycin results in UHRF1 ubiquitination and proteasome-dependent degradation.	tanespimycin	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
27489107-4	2016	Pharmacological inhibition of HSP90 with 17-AAG or 17-dimethylaminoethylamino-17-demethoxygeldanamycin results in UHRF1 ubiquitination and proteasome-dependent degradation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	51-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
27382012-0	2016	Hybrid Enzalutamide Derivatives with Histone Deacetylase Inhibitor Activity Decrease Heat Shock Protein 90 and Androgen Receptor Levels and Inhibit Viability in Enzalutamide-Resistant C4-2 Prostate Cancer Cells.	enzalutamide	7-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
27382012-3	2016	We designed hybrid molecules containing partial chemical scaffolds of enzalutamide and suberoylanilide hydroxamic acid (SAHA), with weakened intrinsic pan-HDACI activities, to target HSP90 and AR in enzalutamide-resistant PCa cells.	enzalutamide	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
27382012-3	2016	We designed hybrid molecules containing partial chemical scaffolds of enzalutamide and suberoylanilide hydroxamic acid (SAHA), with weakened intrinsic pan-HDACI activities, to target HSP90 and AR in enzalutamide-resistant PCa cells.	Vorinostat	87-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
27382012-3	2016	We designed hybrid molecules containing partial chemical scaffolds of enzalutamide and suberoylanilide hydroxamic acid (SAHA), with weakened intrinsic pan-HDACI activities, to target HSP90 and AR in enzalutamide-resistant PCa cells.	Vorinostat	120-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
27382012-3	2016	We designed hybrid molecules containing partial chemical scaffolds of enzalutamide and suberoylanilide hydroxamic acid (SAHA), with weakened intrinsic pan-HDACI activities, to target HSP90 and AR in enzalutamide-resistant PCa cells.	enzalutamide	199-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
27382012-11	2016	The results suggest the potential of the new compounds as prototype antitumor drugs that would downregulate HSP90 and AR in enzalutamide-resistant PCa cells with weakened effects on nuclear HDACI targets.	enzalutamide	124-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27449291-6	2016	In this study, we identified another small molecule, a xanthone compound, more capable of altering dimeric HSP27 than ZER and yielding sensitization in human lung cancer cells when combined with HSP90 inhibitors or standard anticancer modalities such as irradiation and cytotoxic anticancer drugs.	xanthone	55-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
27283788-0	2016	Design, synthesis, and anticancer activity of C8-substituted-4"-thionucleosides as potential HSP90 inhibitors.	c8-substituted-4"-thionucleosides	46-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
26764527-0	2016	A phase I trial of the intravenous Hsp90 inhibitor alvespimycin (17-DMAG) in patients with relapsed chronic lymphocytic leukemia/small lymphocytic lymphoma.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	65-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
27320785-3	2016	In parallel, molecular simulations were also performed on five other 3,4,5-trimethoxyphenyl-containing ligand targets including hsp90, VEGFR2, and human and microbial (Staphylococcus aureus and Candida albicans) dihydrofolate reductase, among which H-17, H-45, H-27, H-02, and H-19 were the most suitable compounds, respectively.	(3,4,5-trimethoxyphenyl)	69-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
27466407-4	2016	We show that the natural product, gambogic acid (GBA), binds selectively to a site in the middle domain of Hsp90beta, identifying GBA as an Hsp90beta-specific Hsp90 inhibitor.	gambogic acid	34-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
27399277-7	2016	In less than 1 ns of MD simulation with L-RIP, we observed distortions of the alpha-helix in the ATP binding site of HSP90 and flipping of the DFG loop in Src kinase.	Adenosine Triphosphate	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27499032-9	2016	Consistently, inhibition of HSP90 with its small molecule inhibitor 17AAG attenuated expression of TGF-beta1-induced Notch-1 target genes, HEY-1 and HES-1.	tanespimycin	68-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
27391062-0	2016	Reactivation of ERK and Akt confers resistance of mutant BRAF colon cancer cells to the HSP90 inhibitor AUY922.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
27233944-7	2016	The Hsp90 inhibitor radicicol disrupts the heterocomplex and favors the partial cytoplasmic relocalization of hTERT in similar manner as the overexpression of the TPR-domain peptide of the immunophilin.	monorden	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
27295069-4	2016	Most of Hsp90 inhibitors blocks the N terminal ATP binding pocket and prevents the conformational changes which are essential for the loading of co-chaperones and client proteins.	Adenosine Triphosphate	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
27205876-10	2016	Moreover, leptin-induced JAK2/STAT3 phosphorylation was markedly attenuated by the HSP90 inhibitors geldanamycin, radicicol and novobiocin.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
27205876-10	2016	Moreover, leptin-induced JAK2/STAT3 phosphorylation was markedly attenuated by the HSP90 inhibitors geldanamycin, radicicol and novobiocin.	monorden	114-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
27205876-10	2016	Moreover, leptin-induced JAK2/STAT3 phosphorylation was markedly attenuated by the HSP90 inhibitors geldanamycin, radicicol and novobiocin.	Novobiocin	128-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
27235383-1	2016	Celastrol (CEL), a plant-derived triterpenoid, is a known inhibitor of Hsp90 and NF-kappaB activation pathways and has recently been suggested to be of therapeutic importance in various cancers.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
27235383-1	2016	Celastrol (CEL), a plant-derived triterpenoid, is a known inhibitor of Hsp90 and NF-kappaB activation pathways and has recently been suggested to be of therapeutic importance in various cancers.	celastrol	11-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
27235383-1	2016	Celastrol (CEL), a plant-derived triterpenoid, is a known inhibitor of Hsp90 and NF-kappaB activation pathways and has recently been suggested to be of therapeutic importance in various cancers.	triterpenoid TP-222	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
27279135-7	2016	We found that after thermal stimulation, Act1 binding to HSP90alpha was significantly increased in the presence of IL-17 (100 ng/ml) and 17-N-allylamino-17-demethoxygeldanamycin (17-AAG, 1 microM).	tanespimycin	137-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-67
27279135-7	2016	We found that after thermal stimulation, Act1 binding to HSP90alpha was significantly increased in the presence of IL-17 (100 ng/ml) and 17-N-allylamino-17-demethoxygeldanamycin (17-AAG, 1 microM).	tanespimycin	179-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-67
27503726-10	2016	Moreover, the hepatic mRNA expression of HSP-90 was also significantly decreased by chronic oral administration of flavangenol in HT chicks.	flavangenol	115-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-47
27301716-4	2016	The effects of genetic modification of the C-terminus on NMDG(+) permeability were mimicked by preapplication of the HSP90 antagonist geldanamycin to the wild-type receptor.	geldanamycin	134-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27301716-6	2016	Taken together, the results suggest that HSP90 may be essential for stabilization and function of P2X7Rs through an action on the cysteine-rich domain of the cytoplasmic the C-terminus.	Cysteine	130-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
27467582-10	2016	CP-31398, a p53 rescue compound, suppressed levels of Aha1, Hsp90 ATPase activity, levels of PKM2 and HIF-1alpha, and aromatase expression in LFS stromal cells.	CP 31398	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
26959555-6	2016	ADMA exposure or overexpression of dominant-negative Hsp90 increased Hsp70 levels, and depletion of Hsp70 abolished ADMA-induced Akt1 phosphorylation.	N,N-dimethylarginine	116-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
27170753-4	2016	By using NVP-AUY922 and/or 17-dimethylaminoethylamino-17-demethoxygeldanamycin as specific inhibitors of cellular heat shock protein 90 (HSP90), we found that efficient chaperoning of L by HSP90 requires P in the measles, Nipah, and vesicular stomatitis viruses.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	27-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
27396341-6	2016	Importantly, EMT associated with depletion of AMH or AMHR2 results in chemoresistance but sensitizes cells to the heat shock protein 90 (HSP90) inhibitor ganetespib.	STA 9090	154-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-135
27396341-6	2016	Importantly, EMT associated with depletion of AMH or AMHR2 results in chemoresistance but sensitizes cells to the heat shock protein 90 (HSP90) inhibitor ganetespib.	STA 9090	154-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
27215381-2	2016	Genetic disruption of calpain attenuated the tumorigenic potential of breast cancer cells and hypersensitized cells to 17AAG, an inhibitor of the molecular chaperone HSP90.	tanespimycin	119-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
27215381-5	2016	Calpain knockdown was associated with increased 17AAG-induced degradation of the HSP90 clients cyclin D1 and AKT and multidrug resistance protein 2, which correlated with increased expression of antimitogenic p27(KIP1) and proapoptotic BIM proteins.	tanespimycin	48-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
26616860-8	2016	TAE684-resistant cells showed greater sensitivity to HSP90 inhibition than did their parental counterparts, with downregulation of AXL and AXL-mediated ERK signaling.	NVP-TAE684	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
27170753-4	2016	By using NVP-AUY922 and/or 17-dimethylaminoethylamino-17-demethoxygeldanamycin as specific inhibitors of cellular heat shock protein 90 (HSP90), we found that efficient chaperoning of L by HSP90 requires P in the measles, Nipah, and vesicular stomatitis viruses.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	27-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-194
27058144-0	2016	BIIB021, a synthetic Hsp90 inhibitor, induces mutant ataxin-1 degradation through the activation of heat shock factor 1.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
27058144-3	2016	Heat shock protein 90 (Hsp90) inhibitors have been shown to reduce polyQ-induced toxicity.	polyglutamine	67-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
27058144-3	2016	Heat shock protein 90 (Hsp90) inhibitors have been shown to reduce polyQ-induced toxicity.	polyglutamine	67-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
27058144-4	2016	This study was designed to examine the therapeutic effects of BIIB021, a purine-scaffold Hsp90 inhibitor, on the protein homeostasis of polyQ-expanded mutant ATXN1 in a cell culture model of SCA1.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
27563408-1	2016	Novobiocin is a natural product that binds the Hsp90 C-terminus and manifests Hsp90 inhibitory activity.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
27563408-1	2016	Novobiocin is a natural product that binds the Hsp90 C-terminus and manifests Hsp90 inhibitory activity.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
27156227-0	2016	Dose-escalation study of a second-generation non-ansamycin HSP90 inhibitor, onalespib (AT13387), in combination with imatinib in patients with metastatic gastrointestinal stromal tumour.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
27184196-7	2016	Herein, we report the therapeutic use of a newly developed GR-targeted liposomal concoction (DXE) coformulating a lipophilic drug (ESC8) and an anti-Hsp90 anticancer gene against aggressive tumor models.	dxe	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
27379708-0	2016	A Phase 2 Study of the Hsp90 Inhibitor AUY922 as Treatment for Patients with Refractory Gastrointestinal Stromal Tumors.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	39-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
27379708-1	2016	BACKGROUND: AUY922 is an inhibitor of heat shock protein 90 (Hsp90).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-59
27379708-1	2016	BACKGROUND: AUY922 is an inhibitor of heat shock protein 90 (Hsp90).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
27156227-3	2016	Onalespib (AT13387) is a potent non-ansamycin HSP90 inhibitor.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
27156227-3	2016	Onalespib (AT13387) is a potent non-ansamycin HSP90 inhibitor.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	11-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
27321499-0	2016	Re: First-in-Human Phase I Dose Escalation Study of a Second-Generation Non-Ansamycin HSP90 Inhibitor, AT13387, in Patients with Advanced Solid Tumors.	Rifabutin	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
27321499-0	2016	Re: First-in-Human Phase I Dose Escalation Study of a Second-Generation Non-Ansamycin HSP90 Inhibitor, AT13387, in Patients with Advanced Solid Tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	103-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
27347156-4	2016	In the present study, the efficacy of a second generation HSP90 inhibitor termed AUY922 was investigated in ATLL.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	81-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
27363520-6	2016	Further mechanistic studies revealed that GV1001 suppresses basal NF-kappaB activation, which is required for HIV-1 LTR transactivation in an HSP90-dependent manner.	gv1001	42-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
27259258-2	2016	Sorafenib and pazopanib inhibited the HSP90 ATPase activity with IC50 values of ~1.0 muM and ~75 nM, respectively.	Sorafenib	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
27251741-0	2016	The HSP90 inhibitor, 17AAG, protects the intestinal stem cell niche and inhibits graft versus host disease development.	tanespimycin	21-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26604096-0	2016	Bioluminescence Imaging to Monitor the Effects of the Hsp90 Inhibitor NVP-AUY922 on NF-kappaB Pathway in Endometrial Cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	74-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
27129177-0	2016	Phase 1B/2 study of the HSP90 inhibitor AUY922 plus trastuzumab in metastatic HER2-positive breast cancer patients who have progressed on trastuzumab-based regimen.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
27059856-6	2016	Despite being monomeric, the N-terminal region of Smchd1 exhibits ATPase activity, which can be antagonized by the reaction product, ADP, or the Hsp90 inhibitor, radicicol, at a nanomolar concentration.	monorden	162-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
27270209-4	2016	In SKOV-3 cells, citral induces the ER stress markers CHOP, GADD45, EDEM, ATF4, Hsp90, ATG5, and phospho-eIF2alpha.	citral	17-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
27254664-7	2016	NMNAT2"s refoldase activity requires a unique C-terminal ATP site, activated in the presence of HSP90.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
27259258-2	2016	Sorafenib and pazopanib inhibited the HSP90 ATPase activity with IC50 values of ~1.0 muM and ~75 nM, respectively.	pazopanib	14-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
27259258-3	2016	Pazopanib docked in silico with two possible poses into the HSP90 ATP binding pocket.	pazopanib	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
27259258-3	2016	Pazopanib docked in silico with two possible poses into the HSP90 ATP binding pocket.	Adenosine Triphosphate	66-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
27002306-6	2016	Y-632 inhibited Hsp90 function mainly through inducing intracellular thiol oxidation, which led to disruption of the Hsp90-Hsp70/Hsp90 organizing protein complex and further induced cell adhesion inhibition, G0 /G1 cell cycle arrest, and apoptosis.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
27002306-0	2016	Y-632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36
27002306-0	2016	Y-632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
27002306-0	2016	Y-632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
27002306-4	2016	In the present study, we show that Y-632, a novel pyrimidine derivative, inhibited Hsp90 in a different way from the conventional Hsp90 inhibitor geldanamycin.	Y-632	35-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
27002306-4	2016	In the present study, we show that Y-632, a novel pyrimidine derivative, inhibited Hsp90 in a different way from the conventional Hsp90 inhibitor geldanamycin.	pyrimidine	50-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
27002306-4	2016	In the present study, we show that Y-632, a novel pyrimidine derivative, inhibited Hsp90 in a different way from the conventional Hsp90 inhibitor geldanamycin.	geldanamycin	146-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
27002306-5	2016	Y-632 induced degradation of diverse Hsp90 client proteins through the ubiquitin-proteasome pathway, as geldanamycin did; however, it neither directly bound to Hsp90 nor inhibited Hsp90 ATPase activity.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
27075590-0	2016	HSP90 Inhibition Suppresses PGE2 Production via Modulating COX-2 and 15-PGDH Expression in HT-29 Colorectal Cancer Cells.	Dinoprostone	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27075590-4	2016	However, the relationship between chaperone activity of HSP90 and PGE2 levels remains unclear.	Dinoprostone	66-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
27075590-5	2016	We evaluated the inhibitory effects of 17-demethoxy-17-allylamino geldanamycin (1 7-AAG), an HSP90 inhibitor, on PGE2 levels in HT-29 colorectal cancer cells.	tanespimycin	39-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
27002306-6	2016	Y-632 inhibited Hsp90 function mainly through inducing intracellular thiol oxidation, which led to disruption of the Hsp90-Hsp70/Hsp90 organizing protein complex and further induced cell adhesion inhibition, G0 /G1 cell cycle arrest, and apoptosis.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27002306-6	2016	Y-632 inhibited Hsp90 function mainly through inducing intracellular thiol oxidation, which led to disruption of the Hsp90-Hsp70/Hsp90 organizing protein complex and further induced cell adhesion inhibition, G0 /G1 cell cycle arrest, and apoptosis.	Y-632	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27002306-6	2016	Y-632 inhibited Hsp90 function mainly through inducing intracellular thiol oxidation, which led to disruption of the Hsp90-Hsp70/Hsp90 organizing protein complex and further induced cell adhesion inhibition, G0 /G1 cell cycle arrest, and apoptosis.	Sulfhydryl Compounds	69-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
27002306-6	2016	Y-632 inhibited Hsp90 function mainly through inducing intracellular thiol oxidation, which led to disruption of the Hsp90-Hsp70/Hsp90 organizing protein complex and further induced cell adhesion inhibition, G0 /G1 cell cycle arrest, and apoptosis.	Sulfhydryl Compounds	69-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27002306-6	2016	Y-632 inhibited Hsp90 function mainly through inducing intracellular thiol oxidation, which led to disruption of the Hsp90-Hsp70/Hsp90 organizing protein complex and further induced cell adhesion inhibition, G0 /G1 cell cycle arrest, and apoptosis.	Sulfhydryl Compounds	69-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
27002306-8	2016	We believe that Y-632, acting as a novel small-molecule inhibitor of the Hsp90-Hsp70/Hsp90 organizing protein complex, has great potential to be a promising Hsp90 inhibitor for cancer therapy, such as for imatinib-resistant leukemia.	Y-632	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
27002306-8	2016	We believe that Y-632, acting as a novel small-molecule inhibitor of the Hsp90-Hsp70/Hsp90 organizing protein complex, has great potential to be a promising Hsp90 inhibitor for cancer therapy, such as for imatinib-resistant leukemia.	Y-632	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
27002306-8	2016	We believe that Y-632, acting as a novel small-molecule inhibitor of the Hsp90-Hsp70/Hsp90 organizing protein complex, has great potential to be a promising Hsp90 inhibitor for cancer therapy, such as for imatinib-resistant leukemia.	Y-632	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
27002306-8	2016	We believe that Y-632, acting as a novel small-molecule inhibitor of the Hsp90-Hsp70/Hsp90 organizing protein complex, has great potential to be a promising Hsp90 inhibitor for cancer therapy, such as for imatinib-resistant leukemia.	Imatinib Mesylate	205-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
27002306-8	2016	We believe that Y-632, acting as a novel small-molecule inhibitor of the Hsp90-Hsp70/Hsp90 organizing protein complex, has great potential to be a promising Hsp90 inhibitor for cancer therapy, such as for imatinib-resistant leukemia.	Imatinib Mesylate	205-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
27002306-8	2016	We believe that Y-632, acting as a novel small-molecule inhibitor of the Hsp90-Hsp70/Hsp90 organizing protein complex, has great potential to be a promising Hsp90 inhibitor for cancer therapy, such as for imatinib-resistant leukemia.	Imatinib Mesylate	205-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
27108782-0	2016	Exogenous hydrogen sulfide exerts proliferation, anti-apoptosis, angiopoiesis and migration effects via activating HSP90 pathway in EC109 cells.	Hydrogen Sulfide	10-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
27108782-4	2016	The present study demonstrated the effects of exogenous H2S on cancer cell growth via activating HSP90 pathways in EC109 esophageal cells.	Hydrogen Sulfide	56-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
27108782-11	2016	Notably, co-treatment of EC109 cells with NaHS and GA (an inhibitor of HSP90 pathway) largely suppressed the aforementioned NaHS-induced effects.	sodium bisulfide	42-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
27108782-11	2016	Notably, co-treatment of EC109 cells with NaHS and GA (an inhibitor of HSP90 pathway) largely suppressed the aforementioned NaHS-induced effects.	Gallium	51-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
27108782-11	2016	Notably, co-treatment of EC109 cells with NaHS and GA (an inhibitor of HSP90 pathway) largely suppressed the aforementioned NaHS-induced effects.	sodium bisulfide	124-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
27108782-12	2016	The findings of the present study provided novel evidence that HSP90 pathway was involved in NaHS-induced cancer cell proliferation, anti-apoptosis, angiopoiesis and migration in EC109 esophageal cells.	sodium bisulfide	93-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
27313682-0	2016	HSP90 expression and its association with wighteone metabolite response in HER2-positive breast cancer cells.	Wighteone	42-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27313682-9	2016	The expression level of HSP90 in the wighteone group was significantly lower than that in the control group.	Wighteone	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
27313682-10	2016	Our findings demonstrated that wighteone effectively inhibited the proliferation of HER2-positive cancer cell lines, and this is considered to be the result of downregulating HSP90 receptor and downstream signaling.	Wighteone	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
27398312-0	2016	Mutations Y493G and K546D in human HSP90 disrupt binding of celastrol and reduce interaction with Cdc37.	celastrol	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
27048660-0	2016	beta-Lapachone Induces NAD(P)H:Quinone Oxidoreductase-1- and Oxidative Stress-Dependent Heat Shock Protein 90 Cleavage and Inhibits Tumor Growth and Angiogenesis.	beta-lapachone	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
27048660-6	2016	Further results revealed that specific inhibitors of NQO1 and reactive oxygen species could dramatically reduce beta-lap-mediated Hsp90 cleavage.	Reactive Oxygen Species	62-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
27048660-9	2016	Unlike other NQO1-dependent cytotoxic quinones, such as streptonigrin, menadione, mitomycin, and 17-allylamino-17-demethoxygeldanamycin, beta-lap was the only agent that could cause Hsp90 cleavage.	beta-lapachone	137-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
26712686-0	2016	Blocking HSP90 Addiction Inhibits Tumor Cell Proliferation, Metastasis Development, and Synergistically Acts with Zoledronic Acid to Delay Osteosarcoma Progression.	Zoledronic Acid	114-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
27037933-0	2016	Synthesis and Biological Evaluation of Novobiocin Core Analogues as Hsp90 Inhibitors.	Novobiocin	39-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
27115471-10	2016	Reduced expression of heat shock proteins (HSPs) was observed in AA cells, whereas DCA induced expression of CHOP, C/EBP, HSP60, and HSP90 in CA cells.	Dichloroacetic Acid	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
27398312-1	2016	Celastrol, a natural compound derived from the Chinese herb Tripterygium wilfordii Hook F, has been proven to inhibit heat shock protein 90 (HSP90) activity and has attracted much attention because of its promising effects in cancer treatment and in ameliorating degenerative neuron diseases.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
27398312-2	2016	However, the HSP90 structure involved in celastrol interaction is not known.	celastrol	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
27398312-3	2016	Here, we report a novel celastrol-binding pocket in the HSP90 dimer, predicted by molecular docking.	celastrol	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
27398312-4	2016	Mutation of the two key binding pocket amino acids (Lys546 and Tyr493) disrupted the binding of celastrol to HSP90 dimers, as detected by isothermal titration calorimetry (ITC).	celastrol	96-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
27398312-5	2016	Interestingly, such mutations also reduced binding between HSP90 and the cochaperone Cdc37, thus providing a new explanation for reported findings that celastrol shows more obvious effects in disrupting binding between HSP90 and Cdc37 than between HSP90 and other cochaperones.	celastrol	152-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
27398312-5	2016	Interestingly, such mutations also reduced binding between HSP90 and the cochaperone Cdc37, thus providing a new explanation for reported findings that celastrol shows more obvious effects in disrupting binding between HSP90 and Cdc37 than between HSP90 and other cochaperones.	celastrol	152-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-224
27398312-5	2016	Interestingly, such mutations also reduced binding between HSP90 and the cochaperone Cdc37, thus providing a new explanation for reported findings that celastrol shows more obvious effects in disrupting binding between HSP90 and Cdc37 than between HSP90 and other cochaperones.	celastrol	152-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-224
27398312-6	2016	In short, our work discloses a novel binding pocket in HSP90 dimer for celastrol and provides an explanation as to why celastrol has a strong effect on HSP90 and Cdc37 binding.	celastrol	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27398312-6	2016	In short, our work discloses a novel binding pocket in HSP90 dimer for celastrol and provides an explanation as to why celastrol has a strong effect on HSP90 and Cdc37 binding.	celastrol	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
27398312-6	2016	In short, our work discloses a novel binding pocket in HSP90 dimer for celastrol and provides an explanation as to why celastrol has a strong effect on HSP90 and Cdc37 binding.	celastrol	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
27398312-6	2016	In short, our work discloses a novel binding pocket in HSP90 dimer for celastrol and provides an explanation as to why celastrol has a strong effect on HSP90 and Cdc37 binding.	celastrol	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
26945041-0	2016	Hsp90 protein interacts with phosphorothioate oligonucleotides containing hydrophobic 2"-modifications and enhances antisense activity.	Phosphorothioate Oligonucleotides	29-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26945041-7	2016	We found that Hsp90 protein binds PS-ASOs containing locked-nucleic-acid (LNA) or constrained-ethyl-bicyclic-nucleic-acid ((S)-cEt) modifications much more avidly than 2"-O-methoxyethyl (MOE).	ps-asos	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
26945041-7	2016	We found that Hsp90 protein binds PS-ASOs containing locked-nucleic-acid (LNA) or constrained-ethyl-bicyclic-nucleic-acid ((S)-cEt) modifications much more avidly than 2"-O-methoxyethyl (MOE).	locked-	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
26945041-8	2016	ASOs bind the mid-domain of Hsp90 protein.	Oligonucleotides, Antisense	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
26945041-9	2016	Hsp90 interacts with more hydrophobic 2" modifications, e.g. (S)-cEt or LNA, in the 5"-wing of the ASO.	Cephalothin	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26945041-10	2016	Reduction of Hsp90 protein decreased activity of PS-ASOs with 5"-LNA or 5"-cEt wings, but not with 5"-MOE wing.	ps-asos	49-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
27043285-7	2016	Therefore, we targeted mitochondrial biogenesis with a mitochondrium-targeted, small-molecule HSP90 inhibitor (Gamitrinib), which eradicated intrinsically resistant cells and augmented the efficacy of MAPKi by inducing mitochondrial dysfunction and inhibiting tumor bioenergetics.	Gamitrinib	111-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
27107422-3	2016	Following treatment with the Hsp90 inhibitor 17-DMAG, a significant number of these repressed genes were significantly re-expressed.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	45-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
27379696-5	2016	Heat shock protein 90 (HSP90) is an adenosine triphosphate (ATP)-dependent molecular chaperone that is critically required for the stability of its clientele, many of which are driver oncoproteins.	Adenosine Triphosphate	36-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26872308-3	2016	HSP90 inhibitors are promising new anticancer agents, in which the benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in clinical evaluation.	benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin	67-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26872308-6	2016	Cross-resistance was found with another HSP90 inhibitor 17-dimethylaminoethylamino-17-demethoxygeldanamycin.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	56-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
27379696-5	2016	Heat shock protein 90 (HSP90) is an adenosine triphosphate (ATP)-dependent molecular chaperone that is critically required for the stability of its clientele, many of which are driver oncoproteins.	Adenosine Triphosphate	36-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
27379696-5	2016	Heat shock protein 90 (HSP90) is an adenosine triphosphate (ATP)-dependent molecular chaperone that is critically required for the stability of its clientele, many of which are driver oncoproteins.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
27379696-5	2016	Heat shock protein 90 (HSP90) is an adenosine triphosphate (ATP)-dependent molecular chaperone that is critically required for the stability of its clientele, many of which are driver oncoproteins.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26627081-2	2016	AT13387 is a novel HSP90 inhibitor promoting degradation of oncogenic proteins upon binding, and may also act as a radiosensitizer.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
27197266-0	2016	Second-Generation HSP90 Inhibitor Onalespib Blocks mRNA Splicing of Androgen Receptor Variant 7 in Prostate Cancer Cells.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
27197266-8	2016	Bioinformatic analyses of transcriptome-wide RNA sequencing data confirmed that the second-generation HSP90 inhibitor onalespib altered the splicing of at least 557 genes in prostate cancer cells, including AR.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	118-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
27035072-3	2016	We report the synthesis of a series of novel imidazole-containing compounds fused with either phenanthrene or phenanthroline, which show enhanced growth inhibitory potency against human colon, breast and melanoma cancer cell lines, as well as evidence of inhibition of the molecular chaperone heat shock protein 70 (Hsp70) pathway in cells, as shown by depletion of downstream oncogenic client proteins of the Hsp90 chaperone pathway, and induction of apoptosis.	imidazole	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	410-415
27551334-3	2016	Here we showed that the HSP90-HMWNC is present in leukemia cells from CML patients in blast stage, and in Imatinib (IM)-resistant 32Dp210 (T315I) leukemia cells.	Imatinib Mesylate	106-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
27551334-4	2016	We found that the HSP90-HMWNC could be disassembled by depleting JAK2 with either Jak2-specific shRNA or treatment with JAK2 inhibitors (TG101209 or Ruxolitinib) and HSP90 inhibitor (AUY922).	TG101209	137-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
27551334-4	2016	We found that the HSP90-HMWNC could be disassembled by depleting JAK2 with either Jak2-specific shRNA or treatment with JAK2 inhibitors (TG101209 or Ruxolitinib) and HSP90 inhibitor (AUY922).	ruxolitinib	149-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
27551334-4	2016	We found that the HSP90-HMWNC could be disassembled by depleting JAK2 with either Jak2-specific shRNA or treatment with JAK2 inhibitors (TG101209 or Ruxolitinib) and HSP90 inhibitor (AUY922).	ruxolitinib	149-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
27551334-4	2016	We found that the HSP90-HMWNC could be disassembled by depleting JAK2 with either Jak2-specific shRNA or treatment with JAK2 inhibitors (TG101209 or Ruxolitinib) and HSP90 inhibitor (AUY922).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	183-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
26988132-0	2016	2-phenylethynesulphonamide (PFT-mu) enhances the anticancer effect of the novel hsp90 inhibitor NVP-AUY922 in melanoma, by reducing GSH levels.	2-phenylethynesulphonamide	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
26988132-0	2016	2-phenylethynesulphonamide (PFT-mu) enhances the anticancer effect of the novel hsp90 inhibitor NVP-AUY922 in melanoma, by reducing GSH levels.	Glutathione	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
26662567-0	2016	17-DMAG induces heat shock protein 90 functional impairment in human bladder cancer cells: knocking down the hallmark traits of malignancy.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
26662567-3	2016	17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) specifically targets Hsp90 and interferes with its function as a molecular chaperone, impairing its intrinsic ATPase activity and undermining proper folding of multiple protein clients.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
26662567-3	2016	17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) specifically targets Hsp90 and interferes with its function as a molecular chaperone, impairing its intrinsic ATPase activity and undermining proper folding of multiple protein clients.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
26662567-4	2016	In this study, we have examined the effects of 17-DMAG on the regulation of Hsp90-dependent tumorigenic signaling pathways directly implicated in cell cycle progression, survival, and motility of human urinary bladder cancer cell lines.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	47-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
26662567-7	2016	Furthermore, 17-DMAG administration induced pronounced downregulation of multiple Hsp90 protein clients and other downstream oncogenic effectors, therefore causing inhibition of cell proliferation and decline of cell motility due to the molecular "freezing" of critical cytoskeletal components.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	13-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
26662567-8	2016	In toto, we have clearly demonstrated the dose-dependent and cell type-specific effects of 17-DMAG on the hallmark traits of cancer, appointing Hsp90 as a key molecular component in bladder cancer targeted therapy.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	91-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
28446410-7	2016	Heat stress and ROS together cause protein denature, leading to increased HSP90 consumption and further to HSP90 deficiency for maintaining 26S proteasome assembly and stability.	Reactive Oxygen Species	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
27134115-0	2016	Synthesis and evaluation of 4-(2-hydroxypropyl)piperazin-1-yl) derivatives as Hsp90 inhibitors.	4-(2-hydroxypropyl)piperazin-1-yl	28-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
27134115-4	2016	We have found that compounds with a hydroxyl group at C-4 of the aryl ring on the piperazine moiety possess Hsp90 inhibition properties.	Piperazine	82-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
27165078-2	2016	Acetaminophen in a concentration of 10 mM did not induce expression of HIF1A and CASP3, but reduced expression of chaperone HSP90, which attested to activation of a caspase-3-independent mechanism of cell death.	Acetaminophen	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
26858237-0	2016	Hsp90 Inhibition Results in Glucocorticoid Receptor Degradation in Association with Increased Sensitivity to Paclitaxel in Triple-Negative Breast Cancer.	Paclitaxel	109-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26858237-2	2016	Recently, new-generation small-molecule Hsp90 inhibitors (e.g., ganetespib and NVP-AUY922) have demonstrated improved safety and activity profiles over the first-generation ansamycin class.	STA 9090	64-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26858237-2	2016	Recently, new-generation small-molecule Hsp90 inhibitors (e.g., ganetespib and NVP-AUY922) have demonstrated improved safety and activity profiles over the first-generation ansamycin class.	Rifabutin	173-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26858237-7	2016	The beneficial effect of the Hsp90 inhibitor on paclitaxel-induced cytotoxicity was reduced when GR was depleted in TNBC cells but could be recovered with GR overexpression.	Paclitaxel	48-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
26858237-8	2016	These findings suggest that GR-regulated anti-apoptotic and pro-proliferative signaling networks in TNBC are disrupted by Hsp90 inhibitors, thereby sensitizing TNBC to paclitaxel-induced cell death.	Paclitaxel	168-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
26858237-9	2016	Thus, GR+ TNBC patients may be a subgroup of breast cancer patients who are most likely to benefit from adding an Hsp90 inhibitor to taxane therapy.	taxane	133-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
26892093-0	2016	Hsp90 inhibitor, BIIB021, induces apoptosis and autophagy by regulating mTOR-Ulk1 pathway in imatinib-sensitive and -resistant chronic myeloid leukemia cells.	Imatinib Mesylate	93-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
27015562-6	2016	Sorafenib inhibited HSP90 and HSP70 chaperone ATPase activities and reduced the interactions of chaperones with clients including c-MYC, CDC37 and MCL-1.	Sorafenib	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
26805515-5	2016	We show that incorporating an N-methyl moiety controls the conformation of the macrocycle, which dramatically impacts cytotoxicity and binding affinity for Hsp90.	Nitrogen	30-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
26951197-0	2016	Hsp90 Maintains Proteostasis of the Galactose Utilization Pathway To Prevent Cell Lethality.	Galactose	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26951197-4	2016	Here, we observe that Hsp90 influences the protein abundance of multiple Gal proteins and the efficiency of galactose utilization even after the galactose utilization pathway (GAL pathway) is fully induced.	Galactose	108-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
26951197-4	2016	Here, we observe that Hsp90 influences the protein abundance of multiple Gal proteins and the efficiency of galactose utilization even after the galactose utilization pathway (GAL pathway) is fully induced.	Galactose	145-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
26639656-6	2016	In addition, HSP90 inhibitors ganetespib and 17-AAG were potent in inducing cell death in cell lines resistant to crizotinib and ceritinib.	STA 9090	30-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
26639656-6	2016	In addition, HSP90 inhibitors ganetespib and 17-AAG were potent in inducing cell death in cell lines resistant to crizotinib and ceritinib.	tanespimycin	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
26639656-6	2016	In addition, HSP90 inhibitors ganetespib and 17-AAG were potent in inducing cell death in cell lines resistant to crizotinib and ceritinib.	Crizotinib	114-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
26639656-6	2016	In addition, HSP90 inhibitors ganetespib and 17-AAG were potent in inducing cell death in cell lines resistant to crizotinib and ceritinib.	ceritinib	129-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
27035072-3	2016	We report the synthesis of a series of novel imidazole-containing compounds fused with either phenanthrene or phenanthroline, which show enhanced growth inhibitory potency against human colon, breast and melanoma cancer cell lines, as well as evidence of inhibition of the molecular chaperone heat shock protein 70 (Hsp70) pathway in cells, as shown by depletion of downstream oncogenic client proteins of the Hsp90 chaperone pathway, and induction of apoptosis.	phenanthrene	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	410-415
27035072-3	2016	We report the synthesis of a series of novel imidazole-containing compounds fused with either phenanthrene or phenanthroline, which show enhanced growth inhibitory potency against human colon, breast and melanoma cancer cell lines, as well as evidence of inhibition of the molecular chaperone heat shock protein 70 (Hsp70) pathway in cells, as shown by depletion of downstream oncogenic client proteins of the Hsp90 chaperone pathway, and induction of apoptosis.	Phenanthrolines	110-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	410-415
26797120-1	2016	Hsp90 is a dimeric ATP-dependent chaperone involved in the folding, maturation, and activation of diverse target proteins.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26884463-1	2016	Hsp90 is the ATP-consuming core component of a very abundant molecular chaperone machine that handles a substantial portion of the cytosolic proteome.	Adenosine Triphosphate	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26797120-2	2016	Extensive in vitro structural analysis has led to a working model of Hsp90"s ATP-driven conformational cycle.	Adenosine Triphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
26929380-0	2016	Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.	Adenosine Triphosphate	71-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
26887051-6	2016	AR-12 inhibited chaperone ATPase activity, which was enhanced by sildenafil; inhibited chaperone - chaperone and chaperone - client interactions; and docked in silico with the ATPase domains of HSP90 and of HSP70.	OSU 03012	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
26929380-1	2016	Heat-shock protein of 90 kDa (Hsp90) is an essential molecular chaperone that adopts different 3D structures associated with distinct nucleotide states: a wide-open, V-shaped dimer in the apo state and a twisted, N-terminally closed dimer with ATP.	Adenosine Triphosphate	244-247	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-28
26929380-1	2016	Heat-shock protein of 90 kDa (Hsp90) is an essential molecular chaperone that adopts different 3D structures associated with distinct nucleotide states: a wide-open, V-shaped dimer in the apo state and a twisted, N-terminally closed dimer with ATP.	Adenosine Triphosphate	244-247	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
26982469-7	2016	The region of aa 250-295 of BGLF4 is essential for the BGLF4/Hsp90 interaction and the mutation of Phe-254, Leu-266, and Leu-267 can disrupt this interaction.	Phenylalanine	99-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
27627558-1	2016	BACKGROUND: Hypertension-induced endothelial dysfunction is associated with an impaired bioavailability of nitric oxide regulated through interactions between nitric oxide synthase and heat shock protein-90 (Hsp-90).	Nitric Oxide	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-206
27627558-1	2016	BACKGROUND: Hypertension-induced endothelial dysfunction is associated with an impaired bioavailability of nitric oxide regulated through interactions between nitric oxide synthase and heat shock protein-90 (Hsp-90).	Nitric Oxide	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-214
27192836-5	2016	sulfates by heparinase I/III as well as treatment of cells with heparin lead to an abrupt reduction in the expression level of Hsp90 isoforms.	Sulfates	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
27192836-5	2016	sulfates by heparinase I/III as well as treatment of cells with heparin lead to an abrupt reduction in the expression level of Hsp90 isoforms.	Heparin	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
27192836-7	2016	The results obtained demonstrate that two isoforms of membrane-bound Hsp90 are involved in migration of tumor cells in vitro and that cell surface heparan sulfate proteoglycans play a pivotal role in the "anchoring" of Hsp90alpha and Hsp90beta to the plasma membrane.	Heparitin Sulfate	147-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-229
26982469-7	2016	The region of aa 250-295 of BGLF4 is essential for the BGLF4/Hsp90 interaction and the mutation of Phe-254, Leu-266, and Leu-267 can disrupt this interaction.	Leucine	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26982469-7	2016	The region of aa 250-295 of BGLF4 is essential for the BGLF4/Hsp90 interaction and the mutation of Phe-254, Leu-266, and Leu-267 can disrupt this interaction.	Leucine	121-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26379118-4	2016	Here, we assessed the therapeutic potential of the HSP90 inhibitor 17-DMAG in SCLC.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	67-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
26723875-0	2016	The HSP90 inhibitor, NVP-AUY922, sensitizes KRAS-mutant non-small cell lung cancer with intrinsic resistance to MEK inhibitor, trametinib.	trametinib	127-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26723875-4	2016	The HSP90 inhibitor AUY922 suppressed PI3K-AKT-mTOR and RAF-MEK-ERK, and rendered cells sensitive to trametinib (GSK1120212).	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26723875-4	2016	The HSP90 inhibitor AUY922 suppressed PI3K-AKT-mTOR and RAF-MEK-ERK, and rendered cells sensitive to trametinib (GSK1120212).	trametinib	101-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26723875-4	2016	The HSP90 inhibitor AUY922 suppressed PI3K-AKT-mTOR and RAF-MEK-ERK, and rendered cells sensitive to trametinib (GSK1120212).	trametinib	113-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26786409-0	2016	Hypoxia attenuates Hsp90 inhibitor 17-DMAG-induced cyclin B1 accumulation in hepatocellular carcinoma cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	35-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
26786409-5	2016	To determine whether hypoxia impairs the therapeutic effect of Hsp90 N-terminal inhibitor, 17-demethoxygeldanamycin hydrochloride (17-DMAG), in live cancer cells, we measured cell proliferation and cell cycle distribution.	17-demethoxygeldanamycin hydrochloride	91-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
26859680-8	2016	Studies reported here validate this hypothesis and demonstrate, both in vitro and in vivo, that HSP90 inhibition facilitates the intracellular delivery of Trastuzumab-conjugated ANPs carrying a model chemotherapeutic agent, Doxorubicin, specifically into ErbB2-overexpressing breast cancer cells, resulting in improved antitumor activity.	Doxorubicin	224-235	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
26721724-1	2016	6BrCaQ is a promising anti-cancer agent derived from novobiocin, which has been shown to inhibit Hsp90.	Novobiocin	53-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
26721724-6	2016	Several Hsp90 targeting molecules like geldanamycin induce accumulation of Hsp70, leading to cytoprotection and often correlated with poor prognosis.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
26927133-5	2016	Several therapeutic strategies that target survival proteins are based on mimicking BH3 domains or the IAP-binding motif or competing with ATP for the Hsp90 ATP-binding pocket.	Adenosine Triphosphate	139-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
26927133-5	2016	Several therapeutic strategies that target survival proteins are based on mimicking BH3 domains or the IAP-binding motif or competing with ATP for the Hsp90 ATP-binding pocket.	Adenosine Triphosphate	157-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
26271031-10	2016	The heat-shock protein-90 (Hsp90) inhibitor geldanamycin abolished estradiol-induced increase in IKCNH2.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
26271031-10	2016	The heat-shock protein-90 (Hsp90) inhibitor geldanamycin abolished estradiol-induced increase in IKCNH2.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
26271031-10	2016	The heat-shock protein-90 (Hsp90) inhibitor geldanamycin abolished estradiol-induced increase in IKCNH2.	Estradiol	67-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
26271031-10	2016	The heat-shock protein-90 (Hsp90) inhibitor geldanamycin abolished estradiol-induced increase in IKCNH2.	Estradiol	67-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
26271031-10	2016	The heat-shock protein-90 (Hsp90) inhibitor geldanamycin abolished estradiol-induced increase in IKCNH2.	ikcnh2	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
26271031-10	2016	The heat-shock protein-90 (Hsp90) inhibitor geldanamycin abolished estradiol-induced increase in IKCNH2.	ikcnh2	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
26271031-14	2016	Estradiol acts on KCNH2 channels via enhanced estradiol-receptor-alpha-mediated Hsp90 interaction, augments membrane trafficking and thereby increases repolarizing current.	Estradiol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
26745854-2	2016	The first Hsp90 C-terminus inhibitor, novobiocin, manifested a relatively high IC50 value of ~700 muM.	Novobiocin	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
26804907-3	2016	We report that the mitotic checkpoint kinase Mps1 phosphorylates a conserved threonine residue in the amino-domain of Hsp90.	Threonine	77-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
26787848-3	2016	Here we study the complete folding and assembly process of the 1,418 amino acid, dimeric chaperone Hsp90 using single-molecule optical tweezers.	1,418 amino acid	63-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
26645561-0	2016	Deguelin Analogue SH-1242 Inhibits Hsp90 Activity and Exerts Potent Anticancer Efficacy with Limited Neurotoxicity.	deguelin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
26645561-0	2016	Deguelin Analogue SH-1242 Inhibits Hsp90 Activity and Exerts Potent Anticancer Efficacy with Limited Neurotoxicity.	2-(3,4-dimethoxyphenyl)-1-(5-methoxy-2,2-dimethyl-2H-chromen-6-yl)ethanone	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
26645561-2	2016	The natural rotenoid deguelin was identified as an Hsp90 inhibitor, but concerns about neurotoxicity have limited prospects for clinical development.	Rotenone	12-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
26645561-7	2016	Mechanistic studies revealed that SH-1242 bound to the C-terminal ATP-binding pocket of Hsp90, disrupting the ability to interact with its co-chaperones and clients and triggering a degradation of client proteins without affecting Hsp70 expression.	Adenosine Triphosphate	66-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
26645561-8	2016	Taken together, our findings illustrate the superior properties of SH-1242 as an Hsp90 inhibitor and as an effective antitumor and minimally toxic agent, providing a foundation for advancing further preclinical and clinical studies.	2-(3,4-dimethoxyphenyl)-1-(5-methoxy-2,2-dimethyl-2H-chromen-6-yl)ethanone	67-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
26219406-0	2016	The heat shock protein 90 inhibitor SNX5422 has a synergistic activity with histone deacetylase inhibitors in induction of death of anaplastic thyroid carcinoma cells.	SNX-5422	36-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
26581400-0	2016	A phase II trial of ganetespib, a heat shock protein 90 Hsp90) inhibitor, in patients with docetaxel-pretreated metastatic castrate-resistant prostate cancer (CRPC)-a prostate cancer clinical trials consortium (PCCTC) study.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-55
26581400-0	2016	A phase II trial of ganetespib, a heat shock protein 90 Hsp90) inhibitor, in patients with docetaxel-pretreated metastatic castrate-resistant prostate cancer (CRPC)-a prostate cancer clinical trials consortium (PCCTC) study.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
26581400-2	2016	In preclinical trials, the Hsp90 ATPase inhibitor ganetespib demonstrated potent inhibition of solid tumor growth, with superior potency than prior Hsp90 inhibitors.	STA 9090	50-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
26581400-2	2016	In preclinical trials, the Hsp90 ATPase inhibitor ganetespib demonstrated potent inhibition of solid tumor growth, with superior potency than prior Hsp90 inhibitors.	STA 9090	50-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
27121714-1	2016	Histone deacetylase 6 (HDAC6) catalyses the removal of acetyl groups from the lysine residues of a series of non-histone proteins, e.g., alpha-tubulin, Hsp90 and cortactin.	Lysine	78-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
26808260-0	2016	Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone.	polyglutamine	76-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
26808260-6	2016	In conjunction with HSP90, the cytoplasmic USP19 may play a key role in triage decision for the disease-related polyQ-expanded substrates, suggesting a function of USP19 in quality control of misfolded proteins by regulating their protein levels.	polyglutamine	112-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
26631731-6	2016	Gamitrinib-triphenylphosphonium, a mitochondria-targeted Hsp90 inhibitor that increases cell death in HeLa and MCF7 cells, consistently inhibited cell death induced by oxidative stress and mitochondrial dysfunction induced by PINK1 mutation in mouse embryonic fibroblast cells and DA cell models such as SH-SY5Y and SN4741 cells.	gamitrinib-triphenylphosphonium	0-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
26748184-0	2016	The novel HSP90 inhibitor NVP-AUY922 shows synergistic anti-leukemic activity with cytarabine in vivo.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	30-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
26748184-0	2016	The novel HSP90 inhibitor NVP-AUY922 shows synergistic anti-leukemic activity with cytarabine in vivo.	Cytarabine	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
26748184-3	2016	Here we show that the HSP90 inhibitor NVP-AUY922 induced degradation of the fusion oncoprotein FOP2-FGFR1 in a human acute myeloid leukemia (AML) cell line, KG-1a.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	42-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
26694589-0	2016	2-Aroylquinoline-5,8-diones as potent anticancer agents displaying tubulin and heat shock protein 90 (HSP90) inhibition.	2-aroylquinoline-5,8-dione	0-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-100
26694589-0	2016	2-Aroylquinoline-5,8-diones as potent anticancer agents displaying tubulin and heat shock protein 90 (HSP90) inhibition.	2-aroylquinoline-5,8-dione	0-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
26695442-0	2016	Phase I study of KW-2478, a novel Hsp90 inhibitor, in patients with B-cell malignancies.	KW-2478	17-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
26695442-1	2016	BACKGROUND: KW-2478 is a novel, non-ansamycin, non-purine heat-shock protein 90 (Hsp90) inhibitor.	KW-2478	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-79
26695442-1	2016	BACKGROUND: KW-2478 is a novel, non-ansamycin, non-purine heat-shock protein 90 (Hsp90) inhibitor.	KW-2478	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
26643616-0	2016	Enhanced in vivo antitumor efficacy of dual-functional peptide-modified docetaxel nanoparticles through tumor targeting and Hsp90 inhibition.	Docetaxel	72-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
26643616-5	2016	Surprisingly, this peptide inhibited the expression of Hsp90 and induced apoptosis by preventing autophagy in A549 cells treated with docetaxel.	Docetaxel	134-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
26743233-0	2016	CPUY201112, a novel synthetic small-molecule compound and inhibitor of heat shock protein Hsp90, induces p53-mediated apoptosis in MCF-7 cells.	CPUY201112	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
26743233-3	2016	Using a fragment-based approach and subsequent structural optimization guided by medicinal chemistry principles, we identified the novel compound CPUY201112 as a potent Hsp90 inhibitor.	CPUY201112	146-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
26743233-4	2016	It binds to the ATP-binding pocket of Hsp90 with a kinetic dissociation (Kd) constant of 27 +- 2.3 nM.	Adenosine Triphosphate	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
26743233-10	2016	These results demonstrate that CPUY201112 is a novel Hsp90 inhibitor with potential use in treating wild-type p53 related cancers.	CPUY201112	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
26916000-5	2016	Hsp90 chaperone function relies on ATP binding and hydrolysis, which in turn guides its carefully orchestrated conformational changes.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26916001-4	2016	Currently, most Hsp90 inhibitors under clinical evaluation act by blocking the binding of ATP to the Hsp90 N-terminal domain and thereby, induce the degradation of many Hsp90-dependent oncoproteins.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
26916001-4	2016	Currently, most Hsp90 inhibitors under clinical evaluation act by blocking the binding of ATP to the Hsp90 N-terminal domain and thereby, induce the degradation of many Hsp90-dependent oncoproteins.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
26916001-4	2016	Currently, most Hsp90 inhibitors under clinical evaluation act by blocking the binding of ATP to the Hsp90 N-terminal domain and thereby, induce the degradation of many Hsp90-dependent oncoproteins.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
26916001-6	2016	Novobiocin derivatives, which do not bind the chaperone"s N-terminal ATPase pocket, have emerged over the past decade as an alternative strategy to inhibit Hsp90, but to date, no derivative has been investigated in the clinical setting.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
26916007-6	2016	Among protein homeostatic mechanisms that influence cancer biology, the essential ATP-driven molecular chaperone heat-shock protein 90 (Hsp90) is especially important.	Adenosine Triphosphate	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-134
26916007-6	2016	Among protein homeostatic mechanisms that influence cancer biology, the essential ATP-driven molecular chaperone heat-shock protein 90 (Hsp90) is especially important.	Adenosine Triphosphate	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
27268613-0	2016	Targeting HSP90 Gene Expression with 17-DMAG Nanoparticles in Breast Cancer Cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
27268613-2	2016	Here we used D,L-lactic-co-glycolic acid-polyethylene glycol-17-dimethylaminoethylamino-17-demethoxy geldanamycin (PLGA-PEG-17DMAG) complexes and free 17-DMAG to inhibit the expression of HSP90 gene in the T47D breast cancer cell line.	polyethylene glycol-17-dimethylaminoethylamino-17-demethoxy geldanamycin	41-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
27268613-11	2016	CONCLUSIONS: PLGA-PEG-17DMAG complexes can be more effective than free 17DMAG in down-regulating of HSP90 expression, at the saesm time exerting more potent cytotoxic effects.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	22-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
27804852-3	2016	For this purpose, a series of benzodiazepine derivatives were designed and synthesized as novel Hsp90 inhibitor.	Benzodiazepines	30-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
27804852-6	2016	In order to determine the anti-proliferative mechanism of the compounds, in silico molecular docking studies were performed between Hsp90 ATPase domain and the benzodiazepine derivatives.	Benzodiazepines	160-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
27804852-10	2016	RESULTS: A representative Benzodiazepine derivative D5 binds Hsp90 with Kd value of 3,93 muM and with estimated free energy of binding -7.99 (kcal/mol).	Benzodiazepines	26-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26480821-4	2016	Present study explored the effect of phenethyl isothiocyanate (PEITC), a natural isothiocyanate, found in cruciferous vegetables on the expression of HIF-1alpha and HSP90 in breast adenocarcinoma cell lines (MCF-7 and MDA-MB-231) under both normoxia and hypoxia.	phenethyl isothiocyanate	37-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
26480821-4	2016	Present study explored the effect of phenethyl isothiocyanate (PEITC), a natural isothiocyanate, found in cruciferous vegetables on the expression of HIF-1alpha and HSP90 in breast adenocarcinoma cell lines (MCF-7 and MDA-MB-231) under both normoxia and hypoxia.	phenethyl isothiocyanate	63-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
26480821-4	2016	Present study explored the effect of phenethyl isothiocyanate (PEITC), a natural isothiocyanate, found in cruciferous vegetables on the expression of HIF-1alpha and HSP90 in breast adenocarcinoma cell lines (MCF-7 and MDA-MB-231) under both normoxia and hypoxia.	isothiocyanic acid	47-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
26642940-1	2016	Heat shock protein 90 (Hsp90) is a ubiquitously expressed ATP-dependent molecular chaperone across all species that helps to the correct the folding of many proteins related to important signaling pathways.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26642940-1	2016	Heat shock protein 90 (Hsp90) is a ubiquitously expressed ATP-dependent molecular chaperone across all species that helps to the correct the folding of many proteins related to important signaling pathways.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26642940-2	2016	Tumor cells expressing Hsp90 have more ATP-binding affinity than normal cells.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26559972-3	2016	Here we found that HSP90 inhibitor PF-4942847 and heat shock also suppress FOXM1.	pyrazofurin	35-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
26806023-0	2016	Radiosynthesis of the iodine-124 labeled Hsp90 inhibitor PU-H71.	Iodine	22-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
26806023-0	2016	Radiosynthesis of the iodine-124 labeled Hsp90 inhibitor PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
26806023-1	2016	Heat shock protein 90 (Hsp90) is an ATP dependent molecular chaperone protein whose function is critical for maintaining several key proteins involved in survival and proliferation of cancer cells.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26806023-1	2016	Heat shock protein 90 (Hsp90) is an ATP dependent molecular chaperone protein whose function is critical for maintaining several key proteins involved in survival and proliferation of cancer cells.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26806023-2	2016	PU-H71 (1), is a potent purine-scaffold based ATP pocket binding Hsp90 inhibitor which has been shown to have potent activity in a broad range of in vivo cancer models and is currently in Phase I clinical trials in patients with advanced solid malignancies, lymphomas, and myeloproliferative neoplasms.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
26806023-2	2016	PU-H71 (1), is a potent purine-scaffold based ATP pocket binding Hsp90 inhibitor which has been shown to have potent activity in a broad range of in vivo cancer models and is currently in Phase I clinical trials in patients with advanced solid malignancies, lymphomas, and myeloproliferative neoplasms.	purine	24-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
26806023-2	2016	PU-H71 (1), is a potent purine-scaffold based ATP pocket binding Hsp90 inhibitor which has been shown to have potent activity in a broad range of in vivo cancer models and is currently in Phase I clinical trials in patients with advanced solid malignancies, lymphomas, and myeloproliferative neoplasms.	Adenosine Triphosphate	46-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
26481477-3	2016	Here, we report that UV irradiation and cisplatin treatment rapidly induce the expression of membrane-bound Hsp60, Hsp70, and Hsp90 upstream the phosphatidylserine exposure.	Cisplatin	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
26549368-0	2016	4-Hydroxybenzoic acid derivatives as HDAC6-specific inhibitors modulating microtubular structure and HSP90alpha chaperone activity against prostate cancer.	4-hydroxybenzoic acid	0-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-111
26549368-6	2016	Furthermore, 4-hydroxybenzoic acids decreased HSP90alpha regulation of the human androgen receptor in prostate cancer cells by increasing HSP90alpha acetylation levels.	Parabens	13-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-56
26549368-6	2016	Furthermore, 4-hydroxybenzoic acids decreased HSP90alpha regulation of the human androgen receptor in prostate cancer cells by increasing HSP90alpha acetylation levels.	Parabens	13-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-148
26638081-4	2016	RESULTS: Out of four Hsps, Hsp 70 and Hsp 90 yields 89% &amp; 88% sensitivity and 82% &amp; 89% specificity, respectively.	Adenosine Monophosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-44
26638081-4	2016	RESULTS: Out of four Hsps, Hsp 70 and Hsp 90 yields 89% &amp; 88% sensitivity and 82% &amp; 89% specificity, respectively.	Adenosine Monophosphate	87-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-44
27013225-6	2016	Notably, geldanamycin and its derivatives (17-AAG, 17-DMAG) have shown quite encouraging results in inhibiting HSP90 function in several cancers and currently almost 17 drug candidates known to be target HSP90 are being under clinical trials either as single agents or combinatorial therapy.	geldanamycin	9-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
27013225-6	2016	Notably, geldanamycin and its derivatives (17-AAG, 17-DMAG) have shown quite encouraging results in inhibiting HSP90 function in several cancers and currently almost 17 drug candidates known to be target HSP90 are being under clinical trials either as single agents or combinatorial therapy.	geldanamycin	9-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
27013225-6	2016	Notably, geldanamycin and its derivatives (17-AAG, 17-DMAG) have shown quite encouraging results in inhibiting HSP90 function in several cancers and currently almost 17 drug candidates known to be target HSP90 are being under clinical trials either as single agents or combinatorial therapy.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	51-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
27013225-6	2016	Notably, geldanamycin and its derivatives (17-AAG, 17-DMAG) have shown quite encouraging results in inhibiting HSP90 function in several cancers and currently almost 17 drug candidates known to be target HSP90 are being under clinical trials either as single agents or combinatorial therapy.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	51-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
26534988-4	2016	Proteasome inhibitors (calpain inhibitor I and MG132) and Hsp90 inhibitor geldanamycin, but not Hsp70 inhibitor pifithrin-mu, increased wild-type (WT) hPXR in the nucleus.	geldanamycin	74-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
26574568-3	2016	HSP90 regulates protein degradation of several growth-mediating kinases such as RET, and we hypothesized that HSP90 inhibitor (AUY922) could inhibit RET-mediated medullary thyroid cancer (MTC) as well as papillary thyroid cancer (PTC) cell growth and also radioactive iodine uptake by PTC cells.	Iodine	268-274	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26574568-3	2016	HSP90 regulates protein degradation of several growth-mediating kinases such as RET, and we hypothesized that HSP90 inhibitor (AUY922) could inhibit RET-mediated medullary thyroid cancer (MTC) as well as papillary thyroid cancer (PTC) cell growth and also radioactive iodine uptake by PTC cells.	Iodine	268-274	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
26682870-0	2016	Targeting the Janus-activated kinase-2-STAT3 signalling pathway in pancreatic cancer using the HSP90 inhibitor ganetespib.	STA 9090	111-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
26682870-3	2016	We hypothesised that ganetespib, an HSP90 inhibitor, can inhibit PC cell growth by interfering with multiple signalling cascades, including the Janus-activated kinase (JAK)-STAT pathway, and act synergistically with chemotherapeutic drugs.	STA 9090	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
27057371-6	2016	Furthermore, it was demonstrated that quercetin induces cancer cell apoptosis by downregulating the levels of Hsp90.	Quercetin	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
27057371-7	2016	In conclusion, we have shown that quercetin induces downregulation of Hsp90 expression that may be involved in the decrease of chymotrypsin-like proteasome activity which, in order, induces inhibition of growth and causes cell death in thyroid cancer cells.	Quercetin	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
27057371-8	2016	Thus, quercetin appears to be a promising candidate drug for Hsp90 downregulation and apoptosis of thyroid cancer cells.	Quercetin	6-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26760959-1	2016	L-Menthol Induces Apoptosis through Caspase 10 and by Suppressing HSP90.	Menthol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
27712589-1	2016	The histone deacetylase (HDAC) inhibitor belinostat increases the amount of unfolded proteins in cells by promoting the acetylation of heat shock protein 90 (HSP90), thereby disrupting its chaperone function.	belinostat	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-156
27712589-1	2016	The histone deacetylase (HDAC) inhibitor belinostat increases the amount of unfolded proteins in cells by promoting the acetylation of heat shock protein 90 (HSP90), thereby disrupting its chaperone function.	belinostat	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
27712589-2	2016	The human immunodeficiency virus protease inhibitor ritonavir, on the other hand, not only increases unfolded proteins by suppressing HSP90 but also acts as a proteasome inhibitor.	Ritonavir	52-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
26456056-0	2015	Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.	Superoxides	19-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
26517240-5	2015	In addition to being radioresistant these cells were also found to be resistant to cisplatin.HSP90 is a molecular chaperone involved in stabilization and function of multiple client proteins implicated in NSCLC cell survival and radioresistance.	Cisplatin	83-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
26517240-9	2015	Combining IR with ganetespib completely abrogates clonogenic survival of radioresistant cells.Our data show that HSP90 inhibition can potentiate the effect of radiotherapy and eliminate radioresistant and cisplatin -resistant residual cells, thus it may aid in reducing NSCLC tumor recurrence after fractionated radiotherapy.	STA 9090	18-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
26517240-9	2015	Combining IR with ganetespib completely abrogates clonogenic survival of radioresistant cells.Our data show that HSP90 inhibition can potentiate the effect of radiotherapy and eliminate radioresistant and cisplatin -resistant residual cells, thus it may aid in reducing NSCLC tumor recurrence after fractionated radiotherapy.	Cisplatin	205-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
26819668-1	2016	KU-32 and KU-596 are novobiocin-derived, C-terminal heat shock protein 90 (Hsp90) modulators that induce Hsp70 levels and manifest neuroprotective activity.	Novobiocin	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-73
26819668-1	2016	KU-32 and KU-596 are novobiocin-derived, C-terminal heat shock protein 90 (Hsp90) modulators that induce Hsp70 levels and manifest neuroprotective activity.	Novobiocin	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
26630652-2	2015	We previously reported that the novel, orally available HSP90alpha/beta inhibitor TAS-116 shows significant anti-MM activities.	TAS-116	82-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
26456056-2	2015	We have previously shown that Hsp90 controls the production of reactive oxygen species by modulating the activity of Noxes1-3 and 5, but not Nox4.	Reactive Oxygen Species	63-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
26456056-4	2015	In isolated enzyme activity assays, we found that Hsp90 inhibitors selectively decrease superoxide, but not hydrogen peroxide, production.	Superoxides	88-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
26456056-5	2015	The addition of Hsp90 alone only modestly increases Nox5 enzyme activity but in combination with the co-chaperones, Hsp70, HOP, Hsp40, and p23 it robustly stimulated superoxide, but not hydrogen peroxide, production.	Superoxides	166-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
26456056-7	2015	In cell lysates using a co-IP approach, Hsp90 binds to Nox5 but not Nox4, and the degree of binding can be influenced by calcium-dependent stimuli.	Calcium	121-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26456056-17	2015	Collectively these results show that the C-terminal region of Nox5 binds to the M domain of Hsp90 and that the binding of Hsp90 and select co-chaperones facilitate oligomerization and the efficient production of superoxide.	Superoxides	212-222	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
26556859-8	2015	This data suggests that dual HSP90 and HSP70 inhibition can simultaneously disrupt the key signaling pathways in MIBC.	4-METHYL-2-PENTANOL	113-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
26556860-0	2015	The Hsp90 inhibitor SNX-7081 is synergistic with fludarabine nucleoside via DNA damage and repair mechanisms in human, p53-negative chronic lymphocytic leukemia.	SNX-7081	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26556860-0	2015	The Hsp90 inhibitor SNX-7081 is synergistic with fludarabine nucleoside via DNA damage and repair mechanisms in human, p53-negative chronic lymphocytic leukemia.	fludarabine nucleoside	49-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26556860-2	2015	We previously showed that the Hsp90 inhibitor, SNX-7081, synergizes with and restores sensitivity to fludarabine nucleoside (2-FaraA) in human chronic lymphocytic leukemia (CLL) cells with lesions in the p53 pathway (Best OG, et al., Leukemia Lymphoma 53:1367-75, 2012).	SNX-7081	47-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
26556860-2	2015	We previously showed that the Hsp90 inhibitor, SNX-7081, synergizes with and restores sensitivity to fludarabine nucleoside (2-FaraA) in human chronic lymphocytic leukemia (CLL) cells with lesions in the p53 pathway (Best OG, et al., Leukemia Lymphoma 53:1367-75, 2012).	fludarabine nucleoside	101-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
26556860-2	2015	We previously showed that the Hsp90 inhibitor, SNX-7081, synergizes with and restores sensitivity to fludarabine nucleoside (2-FaraA) in human chronic lymphocytic leukemia (CLL) cells with lesions in the p53 pathway (Best OG, et al., Leukemia Lymphoma 53:1367-75, 2012).	2-faraa	125-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
26475763-10	2015	Role of Hsp90 inhibition on signaling pathways was elucidated by using specific chemical inhibitor, radicicol.	monorden	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
26405178-2	2015	Targeting Hsp90 is an attractive strategy to halt neurodegenerative diseases, and benzoquinone ansamycin (BQA) Hsp90 inhibitors such as geldanamycin (GA) and 17-(allylamino)-17-demethoxygeldanamycin have been shown to be beneficial in mutant A53T alpha-synuclein PD models.	benzoquinone ansamycin	82-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
26405178-2	2015	Targeting Hsp90 is an attractive strategy to halt neurodegenerative diseases, and benzoquinone ansamycin (BQA) Hsp90 inhibitors such as geldanamycin (GA) and 17-(allylamino)-17-demethoxygeldanamycin have been shown to be beneficial in mutant A53T alpha-synuclein PD models.	bqa	106-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
26405178-2	2015	Targeting Hsp90 is an attractive strategy to halt neurodegenerative diseases, and benzoquinone ansamycin (BQA) Hsp90 inhibitors such as geldanamycin (GA) and 17-(allylamino)-17-demethoxygeldanamycin have been shown to be beneficial in mutant A53T alpha-synuclein PD models.	geldanamycin	136-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
26405178-2	2015	Targeting Hsp90 is an attractive strategy to halt neurodegenerative diseases, and benzoquinone ansamycin (BQA) Hsp90 inhibitors such as geldanamycin (GA) and 17-(allylamino)-17-demethoxygeldanamycin have been shown to be beneficial in mutant A53T alpha-synuclein PD models.	geldanamycin	150-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
26405178-2	2015	Targeting Hsp90 is an attractive strategy to halt neurodegenerative diseases, and benzoquinone ansamycin (BQA) Hsp90 inhibitors such as geldanamycin (GA) and 17-(allylamino)-17-demethoxygeldanamycin have been shown to be beneficial in mutant A53T alpha-synuclein PD models.	tanespimycin	158-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
26405178-2	2015	Targeting Hsp90 is an attractive strategy to halt neurodegenerative diseases, and benzoquinone ansamycin (BQA) Hsp90 inhibitors such as geldanamycin (GA) and 17-(allylamino)-17-demethoxygeldanamycin have been shown to be beneficial in mutant A53T alpha-synuclein PD models.	tanespimycin	158-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
26443624-3	2015	Here, we demonstrate that heat shock protein 90 (HSP90) inhibition using a purine-scaffold HSP90 inhibitor in early clinical development is an effective therapeutic approach in JAK-dependent ALL and can overcome persistence to JAK-inhibitor therapy in ALL cells.	purine	75-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-47
26443624-3	2015	Here, we demonstrate that heat shock protein 90 (HSP90) inhibition using a purine-scaffold HSP90 inhibitor in early clinical development is an effective therapeutic approach in JAK-dependent ALL and can overcome persistence to JAK-inhibitor therapy in ALL cells.	purine	75-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
26443624-3	2015	Here, we demonstrate that heat shock protein 90 (HSP90) inhibition using a purine-scaffold HSP90 inhibitor in early clinical development is an effective therapeutic approach in JAK-dependent ALL and can overcome persistence to JAK-inhibitor therapy in ALL cells.	purine	75-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
26599366-3	2015	Several small molecule inhibitors of Hsp90, such as geldanamycin derivatives, that display antitumor activity, have been developed and are under clinical trials.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
26599366-5	2015	Here we report the first crystal structure of a peptide bound at the ATP binding site of the N-terminal domain of Hsp90.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
26352211-10	2015	In this way, we demonstrate that oxohygrolidin, one of the eukaryote-active compounds we identified through activity-independent screening, targets the V1 ATPase in yeast and human cells and secondarily HSP90.	oxohygrolidin	33-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
26483201-0	2015	Discovery of an L-alanine ester prodrug of the Hsp90 inhibitor, MPC-3100.	l-alanine ester	16-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
26483201-2	2015	One development candidate is the purine-based, synthetic Hsp90 inhibitor 1 (MPC-3100), which successfully completed a phase I clinical study.	purine	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
26483201-2	2015	One development candidate is the purine-based, synthetic Hsp90 inhibitor 1 (MPC-3100), which successfully completed a phase I clinical study.	1-(4-(2-(6-amino-8-((6-bromo-1,3-benzodioxol-5-yl)sulfanyl)-9H-purin-9-yl)ethyl)piperidin-1-yl)-2-hydroxypropan-1-one	76-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
26483201-0	2015	Discovery of an L-alanine ester prodrug of the Hsp90 inhibitor, MPC-3100.	1-(4-(2-(6-amino-8-((6-bromo-1,3-benzodioxol-5-yl)sulfanyl)-9H-purin-9-yl)ethyl)piperidin-1-yl)-2-hydroxypropan-1-one	64-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
26622167-5	2015	Such findings prompted us to investigate the potential anticancer activity of all other FDA-approved HIV-1 PIs against human Hsp90.	Monothiopyrophosphoric acid	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
26617583-6	2015	Chemical inhibition of Hsp90 resulted in increased susceptibility of the fungus to itraconazole and micafungin, and decreased its growth in human nails in vitro.	Itraconazole	83-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26617583-6	2015	Chemical inhibition of Hsp90 resulted in increased susceptibility of the fungus to itraconazole and micafungin, and decreased its growth in human nails in vitro.	Micafungin	100-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
25638023-7	2015	We show SIM-XL to be more sensitive and faster than a competing tool when analyzing a data set obtained from the human HSP90.	sim-xl	8-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
26391399-6	2015	A pull-down assay revealed that (-)-maackiain disrupted the interaction of Hsp90 with PKCdelta, resulting in the suppression of phorbol 12-myristate 13-acetate (PMA)-induced up-regulation of H1R gene expression in HeLa cells.	Tetradecanoylphorbol Acetate	161-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
26391399-7	2015	Additional Hsp90 inhibitors, including 17-(allylamino)-17-demethoxygeldanamycin, celastrol, and novobiocin also suppressed PMA-induced H1R gene up-regulation.	tanespimycin	39-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
26391399-7	2015	Additional Hsp90 inhibitors, including 17-(allylamino)-17-demethoxygeldanamycin, celastrol, and novobiocin also suppressed PMA-induced H1R gene up-regulation.	celastrol	81-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
26391399-7	2015	Additional Hsp90 inhibitors, including 17-(allylamino)-17-demethoxygeldanamycin, celastrol, and novobiocin also suppressed PMA-induced H1R gene up-regulation.	Novobiocin	96-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
26391399-10	2015	The underlying mechanism of the suppression of PMA-induced up-regulation of H1R gene expression by (-)-maackiain and Hsp90 inhibitors is the inhibition of PKCdelta activation through the disruption of Hsp90-PKCdelta interaction.	Tetradecanoylphorbol Acetate	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
26391399-10	2015	The underlying mechanism of the suppression of PMA-induced up-regulation of H1R gene expression by (-)-maackiain and Hsp90 inhibitors is the inhibition of PKCdelta activation through the disruption of Hsp90-PKCdelta interaction.	Tetradecanoylphorbol Acetate	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
26416354-3	2015	SIRT1 knock-down or SIRT1 inhibitors (amurensin G and EX527) effectively suppressed the resistance to Hsp90 inhibitors (17-AAG and AUY922) in several MDR variants of human lymphoblastic leukemia and human breast cancer cell lines.	tanespimycin	120-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
26416354-3	2015	SIRT1 knock-down or SIRT1 inhibitors (amurensin G and EX527) effectively suppressed the resistance to Hsp90 inhibitors (17-AAG and AUY922) in several MDR variants of human lymphoblastic leukemia and human breast cancer cell lines.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	131-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
26457742-5	2015	The docking study indicates that 25 occupied the C-terminal ATP-binding pocket of HSP90 in a similar mode as 1, which implies that the anticancer and antiangiogenic activities of 25 are derived from HIF-1alpha destabilization by binding to the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
26457742-5	2015	The docking study indicates that 25 occupied the C-terminal ATP-binding pocket of HSP90 in a similar mode as 1, which implies that the anticancer and antiangiogenic activities of 25 are derived from HIF-1alpha destabilization by binding to the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	275-281
26457742-5	2015	The docking study indicates that 25 occupied the C-terminal ATP-binding pocket of HSP90 in a similar mode as 1, which implies that the anticancer and antiangiogenic activities of 25 are derived from HIF-1alpha destabilization by binding to the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	255-258	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
26457742-5	2015	The docking study indicates that 25 occupied the C-terminal ATP-binding pocket of HSP90 in a similar mode as 1, which implies that the anticancer and antiangiogenic activities of 25 are derived from HIF-1alpha destabilization by binding to the C-terminal ATP-binding site of hHSP90.	Adenosine Triphosphate	255-258	heat shock protein 90 alpha family class A member 1	Homo sapiens	275-281
25855505-0	2015	Synthesis of 5,6-dihydro-4H-benzo[d]isoxazol-7-one and 5,6-dihydro-4H-isoxazolo[5,4-c]pyridin-7-one derivatives as potential Hsp90 inhibitors.	5,6-dihydro-4h-benzo[d]isoxazol-7-one	13-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
25855505-0	2015	Synthesis of 5,6-dihydro-4H-benzo[d]isoxazol-7-one and 5,6-dihydro-4H-isoxazolo[5,4-c]pyridin-7-one derivatives as potential Hsp90 inhibitors.	5,6-dihydro-4h-isoxazolo[5,4-c]pyridin-7-one	55-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
25855505-1	2015	A novel class of 5,6-dihydro-4H-benzo[d]isoxazol-7-ones and 5,6-dihydro-4H-isoxazolo[5,4-c]pyridin-7-ones was designed, synthesized, and assayed to investigate the affinity toward Hsp90 protein.	5,6-dihydro-4h-benzo[d]isoxazol-7-ones	17-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
25855505-1	2015	A novel class of 5,6-dihydro-4H-benzo[d]isoxazol-7-ones and 5,6-dihydro-4H-isoxazolo[5,4-c]pyridin-7-ones was designed, synthesized, and assayed to investigate the affinity toward Hsp90 protein.	5,6-dihydro-4h-isoxazolo[5,4-c]pyridin-7-ones	60-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
25855505-3	2015	Whereas all the compounds bearing a benzamide group on the bicyclic scaffold were devoid of activity, the derivatives carrying a resorcinol-like fragment showed a remarkable inhibitory effect on Hsp90.	resorcinol	129-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
26253285-3	2015	The present study, focused on the functional study of those candidate polymorphisms by electrophoretic mobility shift assay (EMSA) and in vitro luciferase expression assays, has revealed that the observed differences in the transcriptional activity of the HSP90AA1 gene as response to heat stress are caused by the presence of a cytosine insertion (rs397514115) and a C to G transversion (rs397514116) at the promoter region.	Cytosine	329-337	heat shock protein 90 alpha family class A member 1	Homo sapiens	256-264
26623018-3	2015	In the present study, we hypothesized that the histone deacetylase inhibitor belinostat would increase the amount of unfolded proteins in cells by inhibiting heat-shock protein (HSP) 90, and that the proteasome inhibitor bortezomib would inhibit their degradation by inhibiting the proteasome, thus causing ubiquitinated protein accumulation and ER stress synergistically.	belinostat	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-185
25843003-5	2015	These studies have shown that Hsp90 is a homodimeric protein that requires ATP hydrolysis and a host of accessory proteins termed co-chaperones to facilitate the maturation of clients to their active states.	Adenosine Triphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
26351876-0	2015	Targeted inhibition of mitochondrial Hsp90 induces mitochondrial elongation in Hep3B hepatocellular carcinoma cells undergoing apoptosis by increasing the ROS level.	Reactive Oxygen Species	155-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
26351876-1	2015	Previous studies reported that a Gamitrinib variant containing triphenylphosphonium (G-TPP) binds to mitochondrial Hsp90 and rapidly inhibits its activity to induce apoptosis.	Gamitrinib	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
26351876-1	2015	Previous studies reported that a Gamitrinib variant containing triphenylphosphonium (G-TPP) binds to mitochondrial Hsp90 and rapidly inhibits its activity to induce apoptosis.	3-(bromopropyl)triphenylphosphonium	63-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
26351876-1	2015	Previous studies reported that a Gamitrinib variant containing triphenylphosphonium (G-TPP) binds to mitochondrial Hsp90 and rapidly inhibits its activity to induce apoptosis.	UNII-M6LC47TUG3	85-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
26252737-2	2015	In this study, we used molecular dynamics to examine the interaction of gallium corroles with Hsp90, and found that they can bind preferentially to the ATP-binding N-terminal site.	Gallium	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
26252737-2	2015	In this study, we used molecular dynamics to examine the interaction of gallium corroles with Hsp90, and found that they can bind preferentially to the ATP-binding N-terminal site.	Adenosine Triphosphate	152-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
26271675-0	2015	HSP90 Inhibitor-SN-38 Conjugate Strategy for Targeted Delivery of Topoisomerase I Inhibitor to Tumors.	Irinotecan	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26271675-4	2015	STA-12-8666 is an HDC that comprises an HSP90 inhibitor fused to SN-38, the active metabolite of irinotecan.	sta-12	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26271675-6	2015	In vivo modeling showed that the HSP90 inhibitor moiety was required for selective retention of STA-12-8666, and this enrichment promoted extended release of active SN-38 within the tumor compartment.	sta-12	96-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
26271675-6	2015	In vivo modeling showed that the HSP90 inhibitor moiety was required for selective retention of STA-12-8666, and this enrichment promoted extended release of active SN-38 within the tumor compartment.	Irinotecan	165-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
26517842-4	2015	In this report, we compare the relative interaction strength of both HSP90alpha and HSP90beta with the transcription factors HSF1 and HIF1alpha, the kinases ERBB2 and MET, the E3-ubiquitin ligases KEAP1 and RHOBTB2, and the HSP90 inhibitors geldanamycin and ganetespib.	geldanamycin	241-253	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-79
26517842-4	2015	In this report, we compare the relative interaction strength of both HSP90alpha and HSP90beta with the transcription factors HSF1 and HIF1alpha, the kinases ERBB2 and MET, the E3-ubiquitin ligases KEAP1 and RHOBTB2, and the HSP90 inhibitors geldanamycin and ganetespib.	geldanamycin	241-253	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
26517842-4	2015	In this report, we compare the relative interaction strength of both HSP90alpha and HSP90beta with the transcription factors HSF1 and HIF1alpha, the kinases ERBB2 and MET, the E3-ubiquitin ligases KEAP1 and RHOBTB2, and the HSP90 inhibitors geldanamycin and ganetespib.	STA 9090	258-268	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-79
26517842-4	2015	In this report, we compare the relative interaction strength of both HSP90alpha and HSP90beta with the transcription factors HSF1 and HIF1alpha, the kinases ERBB2 and MET, the E3-ubiquitin ligases KEAP1 and RHOBTB2, and the HSP90 inhibitors geldanamycin and ganetespib.	STA 9090	258-268	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
26517842-7	2015	Using a defined set of HSP90 conformational mutants, we found that some clients interact strongly with a single, ATP-stabilized HSP90 conformation, only transiently populated during the dynamic HSP90 chaperone cycle, while other clients interact equally with multiple HSP90 conformations.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26517842-7	2015	Using a defined set of HSP90 conformational mutants, we found that some clients interact strongly with a single, ATP-stabilized HSP90 conformation, only transiently populated during the dynamic HSP90 chaperone cycle, while other clients interact equally with multiple HSP90 conformations.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
26517842-7	2015	Using a defined set of HSP90 conformational mutants, we found that some clients interact strongly with a single, ATP-stabilized HSP90 conformation, only transiently populated during the dynamic HSP90 chaperone cycle, while other clients interact equally with multiple HSP90 conformations.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
26517842-7	2015	Using a defined set of HSP90 conformational mutants, we found that some clients interact strongly with a single, ATP-stabilized HSP90 conformation, only transiently populated during the dynamic HSP90 chaperone cycle, while other clients interact equally with multiple HSP90 conformations.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
26517842-8	2015	These data suggest different functional requirements among HSP90 clientele that, for some clients, are likely to be ATP-independent.	Adenosine Triphosphate	116-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
26225840-0	2015	Hsp90 inhibition by AUY922 as an effective treatment strategy against myxoid liposarcoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26225840-12	2015	In conclusion, our results provide evidence that Hsp90-inhibition by AUY922 may be a promising alternative therapeutic strategy for myxoid liposarcoma patients.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
26416450-0	2015	Acquired resistance to 5-fluorouracil via HSP90/Src-mediated increase in thymidylate synthase expression in colon cancer.	Fluorouracil	23-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
26416450-3	2015	Here, we demonstrate that the enhanced HSP90 function and subsequent activation of Src induce expression of TYMS and acquired resistance to 5-FU in colon cancer.	Fluorouracil	140-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
26416450-5	2015	HCT116/R, a HCT116 colon cancer cell subline carrying acquired resistance to 5-FU, showed increased expression and activation of HSP90"s client proteins and transcriptional up-regulation of TYMS.	Fluorouracil	77-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
26416450-7	2015	Conversely, pharmacological blockade of HSP90 or Src in HCT116/R cells effectively suppressed the changes involved in 5-FU resistance in vitro and xenograft tumor growth, hematogenous spread, and metastatic tumor development in vivo.	Fluorouracil	118-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26416450-8	2015	This study suggests a novel function of HSP90-Src pathway in regulation of TYMS expression and acquisition of 5-FU resistance.	Fluorouracil	110-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26447544-5	2015	Treatment with celastrol alone led to the decreased expressions of HSP90 client proteins including survivin, AKT, EGFR, which was enhanced by the addition of triptolide.	celastrol	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
26447544-5	2015	Treatment with celastrol alone led to the decreased expressions of HSP90 client proteins including survivin, AKT, EGFR, which was enhanced by the addition of triptolide.	triptolide	158-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
25855012-0	2015	Discovery of 2",4"-dimethoxychalcone as a Hsp90 inhibitor and its effect on iressa-resistant non-small cell lung cancer (NSCLC).	2',4'-dimethoxychalcone	13-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
25855012-1	2015	Heat shock protein 90 (Hsp90) is a ATP dependent molecular chaperone and has emerged as an attractive therapeutic target in the war on cancer due to its role in regulating maturation and stabilization of numerous oncogenic proteins.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
25855012-1	2015	Heat shock protein 90 (Hsp90) is a ATP dependent molecular chaperone and has emerged as an attractive therapeutic target in the war on cancer due to its role in regulating maturation and stabilization of numerous oncogenic proteins.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
25855012-2	2015	In this study, we discovered that 2",4"-dimethoxychalcone (1b) disrupted Hsp90 chaperoning function and inhibited the growth of iressa-resistant non-small cell lung cancer (NSCLC, H1975).	2',4'-dimethoxychalcone	34-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
26112988-4	2015	ANP32C was also found to be associated with oncogenic Hsp90 complexes by virtue of its ability to interact and be immunoprecipitated by the Hsp90 inhibitor PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	156-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
26112988-4	2015	ANP32C was also found to be associated with oncogenic Hsp90 complexes by virtue of its ability to interact and be immunoprecipitated by the Hsp90 inhibitor PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	156-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
26112988-5	2015	Further studies treating cells with the Hsp90 inhibitors PU-H71 and 17-AAG showed atypical increased protein stability and prevention of ANP32C degradation compared to the Hsp90 client AKT.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26187127-4	2015	In this study, enhanced anti-proliferative activity of the Hsp90 inhibitors 17-allylamino-demethoxygeldanamycin (17-AAG) and AUY922 in androgen-sensitive and CRPC cells was achieved when the agents were used in combination with AR antagonists bicalutamide or enzalutamide.	17-allylamino-demethoxygeldanamycin	76-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
26187127-4	2015	In this study, enhanced anti-proliferative activity of the Hsp90 inhibitors 17-allylamino-demethoxygeldanamycin (17-AAG) and AUY922 in androgen-sensitive and CRPC cells was achieved when the agents were used in combination with AR antagonists bicalutamide or enzalutamide.	tanespimycin	113-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
26187127-4	2015	In this study, enhanced anti-proliferative activity of the Hsp90 inhibitors 17-allylamino-demethoxygeldanamycin (17-AAG) and AUY922 in androgen-sensitive and CRPC cells was achieved when the agents were used in combination with AR antagonists bicalutamide or enzalutamide.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	125-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
26187127-4	2015	In this study, enhanced anti-proliferative activity of the Hsp90 inhibitors 17-allylamino-demethoxygeldanamycin (17-AAG) and AUY922 in androgen-sensitive and CRPC cells was achieved when the agents were used in combination with AR antagonists bicalutamide or enzalutamide.	bicalutamide	243-255	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
26187127-4	2015	In this study, enhanced anti-proliferative activity of the Hsp90 inhibitors 17-allylamino-demethoxygeldanamycin (17-AAG) and AUY922 in androgen-sensitive and CRPC cells was achieved when the agents were used in combination with AR antagonists bicalutamide or enzalutamide.	enzalutamide	259-271	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
26323360-0	2015	17-Demethoxy-reblastatin, an Hsp90 inhibitor, induces mitochondria-mediated apoptosis through downregulation of Mcl-1 in human hepatocellular carcinoma cells.	17-demethoxy-reblastatin	0-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
26323360-2	2015	Geldanamycin (GA), the first identified Hsp90 inhibitor, exhibited potent antitumor activity, but possessed significant hepatotoxicity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26323360-2	2015	Geldanamycin (GA), the first identified Hsp90 inhibitor, exhibited potent antitumor activity, but possessed significant hepatotoxicity.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26579577-2	2015	We have reported previously that melatonin stimulates expression and phosphorylation of heat shock protein (HSP) 27, as well as production of HSP70 and HSP90alphabeta in pancreatic carcinoma cells (PANC-1).	Melatonin	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
26414348-0	2015	The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein.	polyalanine	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
26286886-4	2015	Based on the characterization of a first set of 2-phenylbenzofurans showing stimulatory effects on Hsp90 ATPase and conformational dynamics, new ligands were developed that activate Hsp90 by targeting an allosteric site, located 65 A from the active site.	2-phenylbenzofurans	48-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
26286886-4	2015	Based on the characterization of a first set of 2-phenylbenzofurans showing stimulatory effects on Hsp90 ATPase and conformational dynamics, new ligands were developed that activate Hsp90 by targeting an allosteric site, located 65 A from the active site.	2-phenylbenzofurans	48-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
26887616-0	2015	[The Hsp90 inhibitor FW-04-806 suppresses Bcr/Abl-mediated growth of leukemia cells by inhibiting proliferation and inducing apoptosis].	conglobatin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
26887616-0	2015	[The Hsp90 inhibitor FW-04-806 suppresses Bcr/Abl-mediated growth of leukemia cells by inhibiting proliferation and inducing apoptosis].	lauric acid	46-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
26887616-1	2015	OBJECTIVE: To investigate the antitumor efficacy and mechanism of HSP90 inhibitor FW-04-806 against Bcr/Abl(+) leukemia K562 and HL60 cells and their mechanisms of action.	conglobatin	82-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
26408708-3	2015	RESULTS: In FRO ATC cells, 17-AAG and HMA caused cell death with concomitant changes in the expression of HSP90 client proteins, increased beta-catenin protein levels, and inhibited PI3K/AKT signaling.	tanespimycin	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
26408708-3	2015	RESULTS: In FRO ATC cells, 17-AAG and HMA caused cell death with concomitant changes in the expression of HSP90 client proteins, increased beta-catenin protein levels, and inhibited PI3K/AKT signaling.	herbimycin	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
26408708-5	2015	CONCLUSION: 17-AAG and HMA have cytotoxic activities accompanied by regulation of HSP90 client proteins, and cytotoxicity is associated with overexpression of beta-catenin and suppression of PI3K/AKT signaling in FRO ATC cells.	tanespimycin	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
26408708-5	2015	CONCLUSION: 17-AAG and HMA have cytotoxic activities accompanied by regulation of HSP90 client proteins, and cytotoxicity is associated with overexpression of beta-catenin and suppression of PI3K/AKT signaling in FRO ATC cells.	herbimycin	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
26151834-2	2015	In a previous work, we focused on the Mg2+-induced oligomerization process of Hsp90, and characterized the oligomers.	magnesium ion	38-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
26517911-5	2015	Both physically interact with orthologues of the FK506-binding proteins that chaperon both transporters to the plasma membrane in an action that seems to involve heat shock protein (Hsp)90.	Tacrolimus	49-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-188
26256798-5	2015	Molecular docking studies indicated that all nine compounds presented one conformation in the ATP-binding site of HSP90alpha N-terminal domain.	Adenosine Triphosphate	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-124
26358385-1	2015	The novel Hsp90 inhibitor XL888 is undergoing clinical investigation for use in conjunction with the rapidly accelerated fibrosarcoma (RAF) kinase inhibitor vemurafenib to treat unresectable melanoma.	XL 888	26-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
26693070-0	2015	The HSP90 inhibitor 17-PAG effectively inhibits the proliferation and migration of androgen-independent prostate cancer cells.	17-pag	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
26693070-5	2015	Geldanamycin (GA), which was recognized as the first natural HSP90 inhibitor, has demonstrated potent anti-tumor efficacy in large-scale pre-clinical studies, but its application in the clinic is not permitted due to its liver toxicity and unstable physical properties.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26693070-5	2015	Geldanamycin (GA), which was recognized as the first natural HSP90 inhibitor, has demonstrated potent anti-tumor efficacy in large-scale pre-clinical studies, but its application in the clinic is not permitted due to its liver toxicity and unstable physical properties.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26693070-9	2015	17-PAG also downregulated the HSP90 client proteins, including Her2, EGFR, C-Raf, AKT, p-AKT, and CDK4.	17-pag	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
25633180-5	2015	In this study, we investigated the effects of a combined application of the heat shock protein (Hsp) 90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) with PS-341 in lung cancer cells.	tanespimycin	114-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-103
26501082-3	2015	Our data show that 17-N-Allylamino-17-demethoxygeldanamycin (17-AAG), a well-studied Hsp90 inhibitor, synergized with FAK inhibitor, PF-573228, on the growth inhibition of NSCLC cells.	tanespimycin	19-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
25633180-6	2015	Hsp90 inhibition with 17-AAG was effective in enhancing PS-341-induced lung cancer cell death in vitro and in vivo.	tanespimycin	22-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25633180-10	2015	17-AAG mediated the dissociation of its client proteins (IRAK-1, IKKs, and Akt) from the Hsp90 complex.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
26227505-1	2015	Hsp90 is an evolutionarily conserved adenosine triphosphate-dependent molecular chaperone and is one of the most abundant proteins in the cells (1-3 %).	Adenosine Triphosphate	37-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26159484-2	2015	Here, we evaluate the utility of a dendritic hexadecapeptide comprised of four arms, each having a tetrapeptide sequence recognized by an enzyme cathepsin B as a carrier system for heat shock protein 90 (HSP90) inhibitor geldanamycin (GDM).	geldanamycin	221-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-202
26159484-2	2015	Here, we evaluate the utility of a dendritic hexadecapeptide comprised of four arms, each having a tetrapeptide sequence recognized by an enzyme cathepsin B as a carrier system for heat shock protein 90 (HSP90) inhibitor geldanamycin (GDM).	geldanamycin	221-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
26159484-2	2015	Here, we evaluate the utility of a dendritic hexadecapeptide comprised of four arms, each having a tetrapeptide sequence recognized by an enzyme cathepsin B as a carrier system for heat shock protein 90 (HSP90) inhibitor geldanamycin (GDM).	geldanamycin	235-238	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
26277488-5	2015	In this study, one of the mutant p53 activators is suggested as an Hsp90 inhibitor according to a pyrazole scaffold.	pyrazole	98-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
26277488-7	2015	Molecular dynamic simulations were also conducted to evaluate the obtained results on the other two pyrazole structures, one known as Hsp90 inhibitor and the other as the reported mutant p53 activator.	pyrazole	100-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
26084290-6	2015	In addition, TRAP1 targeting by the mitochondria-directed HSP90 chaperones inhibitor gamitrinib induces apoptosis and inhibits colony formation in BRAF-driven CRC cells.	Gamitrinib	85-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
26195286-1	2015	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is involved in the folding, activation, and stabilization of numerous oncogenic proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26195286-1	2015	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is involved in the folding, activation, and stabilization of numerous oncogenic proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26100249-0	2015	Curcumin inhibits human cytomegalovirus by downregulating heat shock protein 90.	Curcumin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-79
26100249-2	2015	The present study reported that the pharmacogenomics of curcumin are similar to that of the antiviral drug, geldanamycin, which targets heat shock protein 90 (Hsp90).	Curcumin	56-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-157
26100249-2	2015	The present study reported that the pharmacogenomics of curcumin are similar to that of the antiviral drug, geldanamycin, which targets heat shock protein 90 (Hsp90).	Curcumin	56-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
26100249-2	2015	The present study reported that the pharmacogenomics of curcumin are similar to that of the antiviral drug, geldanamycin, which targets heat shock protein 90 (Hsp90).	geldanamycin	108-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-157
26100249-2	2015	The present study reported that the pharmacogenomics of curcumin are similar to that of the antiviral drug, geldanamycin, which targets heat shock protein 90 (Hsp90).	geldanamycin	108-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
26227505-2	2015	Hsp90 is induced when a cell undergoes various types of environmental stresses such as heat, cold, or oxygen deprivation.	Oxygen	102-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26227505-6	2015	Recently, several plant-derived small molecules have been discovered exhibiting inhibitory activity towards Hsp90, such as epigallocatechin gallate, gedunin, lentiginosine, celastrol, and deguelin.	epigallocatechin gallate	123-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
26227505-6	2015	Recently, several plant-derived small molecules have been discovered exhibiting inhibitory activity towards Hsp90, such as epigallocatechin gallate, gedunin, lentiginosine, celastrol, and deguelin.	gedunin	149-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
26227505-6	2015	Recently, several plant-derived small molecules have been discovered exhibiting inhibitory activity towards Hsp90, such as epigallocatechin gallate, gedunin, lentiginosine, celastrol, and deguelin.	lentiginosine	158-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
26227505-6	2015	Recently, several plant-derived small molecules have been discovered exhibiting inhibitory activity towards Hsp90, such as epigallocatechin gallate, gedunin, lentiginosine, celastrol, and deguelin.	celastrol	173-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
26227505-6	2015	Recently, several plant-derived small molecules have been discovered exhibiting inhibitory activity towards Hsp90, such as epigallocatechin gallate, gedunin, lentiginosine, celastrol, and deguelin.	deguelin	188-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
26112442-0	2015	Synthesis and biological evaluation of 3,5-disubstituted-4-alkynylisoxozales as a novel class of HSP90 inhibitors.	3,5-disubstituted-4-alkynylisoxozales	39-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
26100249-4	2015	Molecular docking simulation analysis revealed that curcumin fit well in the binding pocket of Hsp90, with hydrogen bonds, hydrophobic interactions and conjugation to maintain adhesion.	Curcumin	52-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
26100249-4	2015	Molecular docking simulation analysis revealed that curcumin fit well in the binding pocket of Hsp90, with hydrogen bonds, hydrophobic interactions and conjugation to maintain adhesion.	Hydrogen	107-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
26100249-5	2015	Consistently, HCMV infection of human embryonic lung fibroblast cells resulted in increased expression of Hsp90alpha, which was significantly inhibited by treatment with curcumin.	Curcumin	170-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
26100249-6	2015	These findings suggested that targeting Hsp90 contributed to the anti-HCMV activity of curcumin.	Curcumin	87-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26156660-1	2015	The synthesis and biological evaluation of a series of bifunctional acridine-HSP90 inhibitor ligands as telomerase inhibitors is herein described.	Acridines	68-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
26156660-2	2015	Four hybrid acridine-HSP90 inhibitor conjugates were prepared using a click-chemistry approach, and subsequently shown to display comparable results to the established telomerase inhibitor BRACO-19 in the TRAP-LIG telomerase assay.	Acridines	12-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
26134567-0	2015	Heat Shock Protein 90 Associates with the Per-Arnt-Sim Domain of Heme-free Soluble Guanylate Cyclase: IMplications for Enzyme Maturation.	Heme	65-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26134567-1	2015	Heat shock protein 90 (hsp90) drives heme insertion into the beta1 subunit of soluble guanylate cyclase (sGC) beta1, which enables it to associate with a partner sGCalpha1 subunit and mature into a nitric oxide (NO)-responsive active form.	Heme	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26134567-1	2015	Heat shock protein 90 (hsp90) drives heme insertion into the beta1 subunit of soluble guanylate cyclase (sGC) beta1, which enables it to associate with a partner sGCalpha1 subunit and mature into a nitric oxide (NO)-responsive active form.	Heme	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26134567-1	2015	Heat shock protein 90 (hsp90) drives heme insertion into the beta1 subunit of soluble guanylate cyclase (sGC) beta1, which enables it to associate with a partner sGCalpha1 subunit and mature into a nitric oxide (NO)-responsive active form.	Nitric Oxide	198-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26134567-1	2015	Heat shock protein 90 (hsp90) drives heme insertion into the beta1 subunit of soluble guanylate cyclase (sGC) beta1, which enables it to associate with a partner sGCalpha1 subunit and mature into a nitric oxide (NO)-responsive active form.	Nitric Oxide	198-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26112442-1	2015	A series of 3,5-disubstitute-4-alkynylisoxazole derivatives were designed and synthesized through palladium(II)-copper(I) catalyzed Sonogashira cross-coupling reaction of an alkynyl moiety and an isoxazole scaffold as novel HSP90 inhibitors.	3,5-disubstitute-4-alkynylisoxazole	12-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
26112442-1	2015	A series of 3,5-disubstitute-4-alkynylisoxazole derivatives were designed and synthesized through palladium(II)-copper(I) catalyzed Sonogashira cross-coupling reaction of an alkynyl moiety and an isoxazole scaffold as novel HSP90 inhibitors.	palladium(ii)-copper	98-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
26112442-1	2015	A series of 3,5-disubstitute-4-alkynylisoxazole derivatives were designed and synthesized through palladium(II)-copper(I) catalyzed Sonogashira cross-coupling reaction of an alkynyl moiety and an isoxazole scaffold as novel HSP90 inhibitors.	alkynyl	31-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
26112442-1	2015	A series of 3,5-disubstitute-4-alkynylisoxazole derivatives were designed and synthesized through palladium(II)-copper(I) catalyzed Sonogashira cross-coupling reaction of an alkynyl moiety and an isoxazole scaffold as novel HSP90 inhibitors.	Isoxazoles	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
26235616-1	2015	The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36
26235616-1	2015	The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
26235616-4	2015	Here, we show that c-Abl kinase phosphorylates Y223 in human Aha1 (hAha1), promoting its interaction with Hsp90.	y223	47-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
26248657-3	2015	Heat shock protein 90 (Hsp90) inhibition is a potential strategy to reduce IRI, and AT13387 is a novel Hsp90 inhibitor with low toxicity.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
26059743-0	2015	17-ABAG, a novel geldanamycin derivative, inhibits LNCaP-cell proliferation through heat shock protein 90 inhibition.	17-abag	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-105
26070982-9	2015	Recombinant WDR73 p.Phe296Leufs*26 and p.Arg256Profs*18 proteins are truncated, unstable, and show increased interaction with alpha- and beta-tubulin and HSP-70/HSP-90.	phe296leufs	20-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-167
26070982-9	2015	Recombinant WDR73 p.Phe296Leufs*26 and p.Arg256Profs*18 proteins are truncated, unstable, and show increased interaction with alpha- and beta-tubulin and HSP-70/HSP-90.	arg256profs	41-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-167
26231043-6	2015	However, DCA synergized with the Hsp90 inhibitor 17-AAG to specifically eliminate these cells.	Dichloroacetic Acid	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
26059743-0	2015	17-ABAG, a novel geldanamycin derivative, inhibits LNCaP-cell proliferation through heat shock protein 90 inhibition.	geldanamycin	17-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-105
26059743-7	2015	Geldanamycin (GA) was identified as the first Hsp90 inhibitor, but shows hepatotoxicity at its effective concentrations, limiting its clinical use.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
26059743-7	2015	Geldanamycin (GA) was identified as the first Hsp90 inhibitor, but shows hepatotoxicity at its effective concentrations, limiting its clinical use.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
26059743-10	2015	17-ABAG also downregulated the Hsp90 client protein and inhibited androgen receptor nuclear localization in LNCaP cells.	17-abag	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
25952464-3	2015	Gemcitabine, which has modest activity in pancreas cancer, activates Chk1, a client protein of HSP90.	gemcitabine	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
26082332-0	2015	Phase I study of the heat shock protein 90 (Hsp90) inhibitor onalespib (AT13387) administered on a daily for 2 consecutive days per week dosing schedule in patients with advanced solid tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-42
25976766-6	2015	Biochemical analyses and molecular docking simulation revealed that L80 disrupted Hsp90 function by binding to the C-terminal ATP-binding pocket of Hsp90, leading to the disruption of the interaction between hypoxia-inducible factor (HIF)-1alpha and Hsp90, downregulation of HIF-1alpha and its target genes, including vascular endothelial growth factor (VEGF) and insulin-like growth factor 2 (IGF2), and decreased the expression of various Hsp90 client proteins.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
26082332-0	2015	Phase I study of the heat shock protein 90 (Hsp90) inhibitor onalespib (AT13387) administered on a daily for 2 consecutive days per week dosing schedule in patients with advanced solid tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
26082332-0	2015	Phase I study of the heat shock protein 90 (Hsp90) inhibitor onalespib (AT13387) administered on a daily for 2 consecutive days per week dosing schedule in patients with advanced solid tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-42
26082332-0	2015	Phase I study of the heat shock protein 90 (Hsp90) inhibitor onalespib (AT13387) administered on a daily for 2 consecutive days per week dosing schedule in patients with advanced solid tumors.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
25736380-3	2015	Treatment of cells with OSU-03012/sildenafil: abolished the expression of multiple oncogenic growth factor receptors and plasma membrane drug efflux pumps and caused a rapid degradation of GRP78 and other HSP70 and HSP90 family chaperone proteins.	OSU 03012	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
25736380-3	2015	Treatment of cells with OSU-03012/sildenafil: abolished the expression of multiple oncogenic growth factor receptors and plasma membrane drug efflux pumps and caused a rapid degradation of GRP78 and other HSP70 and HSP90 family chaperone proteins.	Sildenafil Citrate	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
25955495-0	2015	Role of the novel HSP90 inhibitor AUY922 in hepatocellular carcinoma: Potential for therapy.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	34-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
25976766-6	2015	Biochemical analyses and molecular docking simulation revealed that L80 disrupted Hsp90 function by binding to the C-terminal ATP-binding pocket of Hsp90, leading to the disruption of the interaction between hypoxia-inducible factor (HIF)-1alpha and Hsp90, downregulation of HIF-1alpha and its target genes, including vascular endothelial growth factor (VEGF) and insulin-like growth factor 2 (IGF2), and decreased the expression of various Hsp90 client proteins.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
25976766-6	2015	Biochemical analyses and molecular docking simulation revealed that L80 disrupted Hsp90 function by binding to the C-terminal ATP-binding pocket of Hsp90, leading to the disruption of the interaction between hypoxia-inducible factor (HIF)-1alpha and Hsp90, downregulation of HIF-1alpha and its target genes, including vascular endothelial growth factor (VEGF) and insulin-like growth factor 2 (IGF2), and decreased the expression of various Hsp90 client proteins.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
25976766-6	2015	Biochemical analyses and molecular docking simulation revealed that L80 disrupted Hsp90 function by binding to the C-terminal ATP-binding pocket of Hsp90, leading to the disruption of the interaction between hypoxia-inducible factor (HIF)-1alpha and Hsp90, downregulation of HIF-1alpha and its target genes, including vascular endothelial growth factor (VEGF) and insulin-like growth factor 2 (IGF2), and decreased the expression of various Hsp90 client proteins.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
26622600-8	2015	It was also indicated that the specific HSP90 inhibitor AUY922 plays a therapeutic role in the treatment of RCC, and therefore, HSP90 may be a selective target for molecular-targeted treatments of RCC.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
26622600-8	2015	It was also indicated that the specific HSP90 inhibitor AUY922 plays a therapeutic role in the treatment of RCC, and therefore, HSP90 may be a selective target for molecular-targeted treatments of RCC.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
26244021-7	2015	This article provides a review on ganetespib, a small molecule HSP90 inhibitor that is currently under evaluation in a broad range of cancer types in combination with other therapeutic agents with the hope of further enhancing its efficacy and overcoming drug resistance.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
26219569-2	2015	We investigated the mechanism of acquired resistance to 17-(Dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), a geldanamycin analogue Hsp90 inhibitor, in H3122 and H2228 non-small cell lung cancer cell lines with ALK rearrangement.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	56-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
26219569-2	2015	We investigated the mechanism of acquired resistance to 17-(Dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), a geldanamycin analogue Hsp90 inhibitor, in H3122 and H2228 non-small cell lung cancer cell lines with ALK rearrangement.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	111-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
26219569-2	2015	We investigated the mechanism of acquired resistance to 17-(Dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), a geldanamycin analogue Hsp90 inhibitor, in H3122 and H2228 non-small cell lung cancer cell lines with ALK rearrangement.	geldanamycin	97-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
26244021-8	2015	Based on our current understanding of the complex HSP90 machinery combined with the emerging data from these key clinical trials, ganetespib has the potential to be the first-in-class HSP90 inhibitor to be approved as a new anticancer therapy.	STA 9090	130-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
26244021-8	2015	Based on our current understanding of the complex HSP90 machinery combined with the emerging data from these key clinical trials, ganetespib has the potential to be the first-in-class HSP90 inhibitor to be approved as a new anticancer therapy.	STA 9090	130-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
26185541-2	2015	Proteomic analysis showed that inhibiting HSP90 by the geldanamycin derivative, 17-AAG elevated the expression of the co-chaperone Hsp70.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
26185541-2	2015	Proteomic analysis showed that inhibiting HSP90 by the geldanamycin derivative, 17-AAG elevated the expression of the co-chaperone Hsp70.	tanespimycin	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
26185541-3	2015	In this study we used HSP90 selective inhibitor 17-AAG and HSP70/90 dual inhibitor, VER155008 (VER) in U87-MG glioma cells.	tanespimycin	48-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
26185541-3	2015	In this study we used HSP90 selective inhibitor 17-AAG and HSP70/90 dual inhibitor, VER155008 (VER) in U87-MG glioma cells.	VER 155008	84-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
26134508-0	2015	Hsp90 Is a Novel Target Molecule of CDDO-Me in Inhibiting Proliferation of Ovarian Cancer Cells.	bardoxolone methyl	36-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26134508-3	2015	Here, we demonstrate that CDDO-Me directly interacts with Hsp90 in cells by cellular thermal shift assay.	bardoxolone methyl	26-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
26134508-4	2015	CDDO-Me treatment leads to upregulation of Hsp70 and degradation of Hsp90 clients (ErbB2 and Akt), indicating the inhibition of Hsp90 by CDDO-Me in cells.	bardoxolone methyl	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
26134508-4	2015	CDDO-Me treatment leads to upregulation of Hsp70 and degradation of Hsp90 clients (ErbB2 and Akt), indicating the inhibition of Hsp90 by CDDO-Me in cells.	bardoxolone methyl	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
26134508-4	2015	CDDO-Me treatment leads to upregulation of Hsp70 and degradation of Hsp90 clients (ErbB2 and Akt), indicating the inhibition of Hsp90 by CDDO-Me in cells.	bardoxolone methyl	137-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
26134508-4	2015	CDDO-Me treatment leads to upregulation of Hsp70 and degradation of Hsp90 clients (ErbB2 and Akt), indicating the inhibition of Hsp90 by CDDO-Me in cells.	bardoxolone methyl	137-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
26134508-5	2015	Knockdown of Hsp90 significantly inhibits cell proliferation and enhances the anti-proliferation effect of CDDO-Me in H08910 ovarian cancer cells.	bardoxolone methyl	107-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
26134508-6	2015	Dithiothreitol inhibits the interaction of CDDO-Me with Hsp90 in cells and abrogates CDDO-Me induced upregulation of Hsp70, degradation of Akt and cell proliferation inhibition.	Dithiothreitol	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
26134508-6	2015	Dithiothreitol inhibits the interaction of CDDO-Me with Hsp90 in cells and abrogates CDDO-Me induced upregulation of Hsp70, degradation of Akt and cell proliferation inhibition.	bardoxolone methyl	43-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
26134508-7	2015	This suggests the anti-ovarian cancer effect of CDDO-Me is possibly mediated by the formation of Michael adducts between CDDO-Me and reactive nucleophiles on Hsp90.	bardoxolone methyl	48-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
26134508-7	2015	This suggests the anti-ovarian cancer effect of CDDO-Me is possibly mediated by the formation of Michael adducts between CDDO-Me and reactive nucleophiles on Hsp90.	bardoxolone methyl	121-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
26134508-8	2015	This study identifies Hsp90 as a novel target protein of CDDO-Me, and provides a novel insight into the mechanism of action of CDDO-Me in ovarian cancer cells.	bardoxolone methyl	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
26134508-8	2015	This study identifies Hsp90 as a novel target protein of CDDO-Me, and provides a novel insight into the mechanism of action of CDDO-Me in ovarian cancer cells.	bardoxolone methyl	127-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
25939977-0	2015	KU675, a Concomitant Heat-Shock Protein Inhibitor of Hsp90 and Hsc70 that Manifests Isoform Selectivity for Hsp90alpha in Prostate Cancer Cells.	CHEMBL2326381	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
26056257-3	2015	To elucidate how Hsp90 chaperones kinases, we reconstituted v-Src kinase chaperoning in vitro and show that its activation is ATP-dependent, with the cochaperone Cdc37 increasing the efficiency.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
26056257-6	2015	Molecular dynamics simulations and hydrogen/deuterium exchange of Hsp90-dependent Src kinase variants further reveal increased transitions between inactive and active states and exposure of specific kinase regions.	Hydrogen	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
26056257-6	2015	Molecular dynamics simulations and hydrogen/deuterium exchange of Hsp90-dependent Src kinase variants further reveal increased transitions between inactive and active states and exposure of specific kinase regions.	Deuterium	44-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
25820332-0	2015	Experience with HSP90 inhibitor AUY922 in patients with relapsed or refractory non-Hodgkin lymphoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	32-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
25939977-3	2015	Here we report a novel C-terminal Hsp90 inhibitor, designated KU675, that exhibits potent antiproliferative and cytotoxic activity along with client protein degradation without induction of the heat-shock response in both androgen-dependent and -independent prostate cancer cell lines.	CHEMBL2326381	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
25939977-4	2015	In addition, KU675 demonstrates direct inhibition of Hsp90 complexes as measured by the inhibition of luciferase refolding in prostate cancer cells.	CHEMBL2326381	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
25939977-7	2015	Western blot experiments with four different prostate cancer cell lines treated with KU675 supported this selectivity by inducing the degradation of Hsp90alpha -: dependent client proteins.	CHEMBL2326381	85-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-159
25939977-9	2015	Overall, these findings suggest that KU675 is an Hsp90 C-terminal inhibitor, as well as a dual inhibitor of Hsc70, and may have potential use for the treatment of cancer.	CHEMBL2326381	37-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
25813406-0	2015	17-DMCHAG, a new geldanamycin derivative, inhibits prostate cancer cells through Hsp90 inhibition and survivin downregulation.	17-(6-(3,4-dimethoxycinnamamido)hexylamino)-17-demethoxy-geldanamycin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
25813406-0	2015	17-DMCHAG, a new geldanamycin derivative, inhibits prostate cancer cells through Hsp90 inhibition and survivin downregulation.	geldanamycin	17-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
25813406-3	2015	Geldanamycin is a well-known inhibitor of Hsp90, but its associated liver toxicity limited its clinical development.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
25813406-7	2015	Furthermore, 17-DMCHAG treatment damaged the Hsp90/AR and Hsp90/survivin complexes and induced the proteasome-dependent degradation of AR and survivin, then inhibited the activity of these two proteins.	17-(6-(3,4-dimethoxycinnamamido)hexylamino)-17-demethoxy-geldanamycin	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
25813406-7	2015	Furthermore, 17-DMCHAG treatment damaged the Hsp90/AR and Hsp90/survivin complexes and induced the proteasome-dependent degradation of AR and survivin, then inhibited the activity of these two proteins.	17-(6-(3,4-dimethoxycinnamamido)hexylamino)-17-demethoxy-geldanamycin	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
25408479-7	2015	In a radioresistant CTOS, an inhibitor of heat shock protein 90 (HSP90) suppressed radiation-induced HIF-1alpha expression.	ctos	20-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
25408479-7	2015	In a radioresistant CTOS, an inhibitor of heat shock protein 90 (HSP90) suppressed radiation-induced HIF-1alpha expression.	ctos	20-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
26157347-5	2015	Moreover, 17-AAG-mediated activation of HSF1/Hsps and P-gp-mediated efflux, major causes of Hsp90 inhibitor resistance, was suppressed by SIRT1 inhibitor in K562-CD44(high) cells.	tanespimycin	10-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
26423731-2	2015	The present investigation focused on the molecular docking simulation studies of flavanols as inhibitors of Hsp90 at the high affinity adenosine triphosphate (ATP) binding site and analyzed absorption, distribution, metabolism, excretion and toxicity (ADME-toxicity).	Adenosine Triphosphate	135-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
26423731-2	2015	The present investigation focused on the molecular docking simulation studies of flavanols as inhibitors of Hsp90 at the high affinity adenosine triphosphate (ATP) binding site and analyzed absorption, distribution, metabolism, excretion and toxicity (ADME-toxicity).	Adenosine Triphosphate	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
25957766-2	2015	Time- and dose dependent induction of HSPA6 (confirmed by qPCR and Western Blots) occurred also upon treatment with Radicicol, another HSP90 inhibitor.	monorden	116-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
26036303-5	2015	As EGFR is a client protein of heat-shock protein 90 (HSP90) and sulforaphane is known to functionally regulate HSP90, we hypothesized that sulforaphane could attenuate EGFR-related signaling and potentially be used to treat NSCLC.	sulforaphane	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
26036303-5	2015	As EGFR is a client protein of heat-shock protein 90 (HSP90) and sulforaphane is known to functionally regulate HSP90, we hypothesized that sulforaphane could attenuate EGFR-related signaling and potentially be used to treat NSCLC.	sulforaphane	140-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-52
26036303-5	2015	As EGFR is a client protein of heat-shock protein 90 (HSP90) and sulforaphane is known to functionally regulate HSP90, we hypothesized that sulforaphane could attenuate EGFR-related signaling and potentially be used to treat NSCLC.	sulforaphane	140-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
26036303-5	2015	As EGFR is a client protein of heat-shock protein 90 (HSP90) and sulforaphane is known to functionally regulate HSP90, we hypothesized that sulforaphane could attenuate EGFR-related signaling and potentially be used to treat NSCLC.	sulforaphane	140-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
26036303-8	2015	Combined treatment of NSCLC cells with sulforaphane plus another HSP90 inhibitor (17-AAG) enhanced the inhibition of EGFR-related signaling both in vitro and in vivo.	sulforaphane	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25948110-0	2015	Heat shock protein 90 mediates the apoptosis and autophage in nicotinic-mycoepoxydiene-treated HeLa cells.	nicotinic-	62-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
25948110-0	2015	Heat shock protein 90 mediates the apoptosis and autophage in nicotinic-mycoepoxydiene-treated HeLa cells.	mycoepoxydiene	72-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
25948110-3	2015	Here, we identified nicotinic-mycoepoxydiene (NMD), a structurally novel compound as Hsp90 inhibitor to perform the anti-tumor activity.	nicotinic-mycoepoxydiene	20-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
25948110-3	2015	Here, we identified nicotinic-mycoepoxydiene (NMD), a structurally novel compound as Hsp90 inhibitor to perform the anti-tumor activity.	NMDBA	46-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
25395240-9	2015	Meanwhile, the expression of Hsp90 and hERG was rescued by transfection with AMO-23a.	amo-23a	77-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25939977-0	2015	KU675, a Concomitant Heat-Shock Protein Inhibitor of Hsp90 and Hsc70 that Manifests Isoform Selectivity for Hsp90alpha in Prostate Cancer Cells.	CHEMBL2326381	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-118
25855731-5	2015	Small-molecule-mediated inhibition of Hsp90 activity using 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) revealed that Hsp90 plays a pleiotropic role in the norovirus life cycle but that the stability of the viral capsid protein is integrally linked to Hsp90 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	68-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
25855731-5	2015	Small-molecule-mediated inhibition of Hsp90 activity using 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) revealed that Hsp90 plays a pleiotropic role in the norovirus life cycle but that the stability of the viral capsid protein is integrally linked to Hsp90 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	59-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25855731-5	2015	Small-molecule-mediated inhibition of Hsp90 activity using 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) revealed that Hsp90 plays a pleiotropic role in the norovirus life cycle but that the stability of the viral capsid protein is integrally linked to Hsp90 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	59-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
25855731-5	2015	Small-molecule-mediated inhibition of Hsp90 activity using 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) revealed that Hsp90 plays a pleiotropic role in the norovirus life cycle but that the stability of the viral capsid protein is integrally linked to Hsp90 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	59-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
25855731-5	2015	Small-molecule-mediated inhibition of Hsp90 activity using 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) revealed that Hsp90 plays a pleiotropic role in the norovirus life cycle but that the stability of the viral capsid protein is integrally linked to Hsp90 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	68-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25739426-3	2015	First, the Hsp90 antagonist 17-DMAG dose-dependently inhibited dermal-epidermal separation ex vivo in cryosections of human skin induced by co-incubation of EBA patient autoantibodies with neutrophils from healthy blood donors.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	28-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
25855885-7	2015	RESULTS: Surprisingly, in engineered cell lines, the hotspot E545K and H1047R mutations conferred increased, rather than reduced, IC50 assay measurements when treated with the respective HSP90, PI3K, and MEK inhibitors, 17-AAG, GDC-0941, and trametinib, compared with the SCC25 control cell lines.	tanespimycin	220-226	heat shock protein 90 alpha family class A member 1	Homo sapiens	187-192
25855885-7	2015	RESULTS: Surprisingly, in engineered cell lines, the hotspot E545K and H1047R mutations conferred increased, rather than reduced, IC50 assay measurements when treated with the respective HSP90, PI3K, and MEK inhibitors, 17-AAG, GDC-0941, and trametinib, compared with the SCC25 control cell lines.	2-(1H-indazol-4-yl)-6-(4-methanesulfonylpiperazin-1-ylmethyl)-4-morpholin-4-ylthieno(3,2-d)pyrimidine	228-236	heat shock protein 90 alpha family class A member 1	Homo sapiens	187-192
25855885-7	2015	RESULTS: Surprisingly, in engineered cell lines, the hotspot E545K and H1047R mutations conferred increased, rather than reduced, IC50 assay measurements when treated with the respective HSP90, PI3K, and MEK inhibitors, 17-AAG, GDC-0941, and trametinib, compared with the SCC25 control cell lines.	trametinib	242-252	heat shock protein 90 alpha family class A member 1	Homo sapiens	187-192
25855731-5	2015	Small-molecule-mediated inhibition of Hsp90 activity using 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) revealed that Hsp90 plays a pleiotropic role in the norovirus life cycle but that the stability of the viral capsid protein is integrally linked to Hsp90 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	68-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
26010604-0	2015	The HSP90 Inhibitor Ganetespib Radiosensitizes Human Lung Adenocarcinoma Cells.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
25882550-0	2015	The HSP90 inhibitor ganetespib: A potential effective agent for Acute Myeloid Leukemia in combination with cytarabine.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
25882550-0	2015	The HSP90 inhibitor ganetespib: A potential effective agent for Acute Myeloid Leukemia in combination with cytarabine.	Cytarabine	107-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
25077897-0	2015	The HSP90 inhibitor ganetespib potentiates the antitumor activity of EGFR tyrosine kinase inhibition in mutant and wild-type non-small cell lung cancer.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
25077897-11	2015	Thus, selective HSP90 blockade by ganetespib represents a potentially important complementary strategy to targeted TKI inhibition alone for inducing substantial antitumor responses and overcoming resistance, in both the mutant and WT-EGFR settings.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
26017782-1	2015	The heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA) has been shown to alter endosomal sorting, diverting cargo destined for the recycling pathway into the lysosomal pathway.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
26017782-1	2015	The heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA) has been shown to alter endosomal sorting, diverting cargo destined for the recycling pathway into the lysosomal pathway.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
26017782-1	2015	The heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA) has been shown to alter endosomal sorting, diverting cargo destined for the recycling pathway into the lysosomal pathway.	geldanamycin	58-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
26017782-1	2015	The heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA) has been shown to alter endosomal sorting, diverting cargo destined for the recycling pathway into the lysosomal pathway.	geldanamycin	58-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
25870087-0	2015	Phase I/II Study of HSP90 Inhibitor AUY922 and Erlotinib for EGFR-Mutant Lung Cancer With Acquired Resistance to Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
25905789-0	2015	ATP Acyl Phosphate Reactivity Reveals Native Conformations of  Hsp90 Paralogs and Inhibitor Target Engagement.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
25905789-0	2015	ATP Acyl Phosphate Reactivity Reveals Native Conformations of  Hsp90 Paralogs and Inhibitor Target Engagement.	Phosphates	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
25905789-1	2015	Hsp90 is an ATP-dependent chaperone of widespread interest as a drug target.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25905789-2	2015	Here, using an LC-MS/MS chemoproteomics platform based on a lysine-reactive ATP acyl phosphate probe, several Hsp90 inhibitors were profiled in native cell lysates.	Lysine	60-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
25905789-4	2015	Equipotent inhibition of probe labeling in each paralog occurred at sites both proximal to and distal from bound ATP observed in Hsp90 cocrystal structures, suggesting that the ATP probe is assaying a native conformation not predicted by available structures.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
25905789-4	2015	Equipotent inhibition of probe labeling in each paralog occurred at sites both proximal to and distal from bound ATP observed in Hsp90 cocrystal structures, suggesting that the ATP probe is assaying a native conformation not predicted by available structures.	Adenosine Triphosphate	177-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
25905789-10	2015	Overall, the ATP probe-based assay methodology enabled a broad characterization of Hsp90 inhibitor activity and specificity in native cell lysates.	Adenosine Triphosphate	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
25662161-0	2015	Down-regulation of ERK1/2 and AKT-mediated X-ray repair cross-complement group 1 protein (XRCC1) expression by Hsp90 inhibition enhances the gefitinib-induced cytotoxicity in human lung cancer cells.	Gefitinib	141-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
25662161-7	2015	Combining treatment of gefitinib with an Hsp90 inhibitor resulted in enhancing the reduction of XRCC1 protein and mRNA levels in gefitinib-exposed A549 and H1975 cells.	Gefitinib	23-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
25662161-7	2015	Combining treatment of gefitinib with an Hsp90 inhibitor resulted in enhancing the reduction of XRCC1 protein and mRNA levels in gefitinib-exposed A549 and H1975 cells.	Gefitinib	129-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
25662161-8	2015	Compared to a single agent alone, gefitinib combined with an Hsp90 inhibitor resulted in cytotoxicity and cell growth inhibition synergistically in NSCLC cells.	Gefitinib	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
26221207-0	2015	Reversing drug resistance of cisplatin by hsp90 inhibitors in human ovarian cancer cells.	Cisplatin	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
26221207-1	2015	OBJECTIVE: To investigate the mechanisms for reversing drug resistance of cisplatin (DDP) by Hsp90 inhibitors (geldanamycin (GA), 17-AAG, 17-DMAG) in human ovarian cancer.	Cisplatin	74-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
26221207-1	2015	OBJECTIVE: To investigate the mechanisms for reversing drug resistance of cisplatin (DDP) by Hsp90 inhibitors (geldanamycin (GA), 17-AAG, 17-DMAG) in human ovarian cancer.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
26221207-1	2015	OBJECTIVE: To investigate the mechanisms for reversing drug resistance of cisplatin (DDP) by Hsp90 inhibitors (geldanamycin (GA), 17-AAG, 17-DMAG) in human ovarian cancer.	geldanamycin	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
25901531-0	2015	Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94.	purine	37-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
26010604-3	2015	The antitumor activity of ganetespib, HSP90 inhibitor, was evaluated in human lung adenocarcinoma (AC) cells for its ability to potentiate the effects of IR treatment in both in vitro and in vivo.	STA 9090	26-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25935150-0	2015	Amyloid beta peptide-induced inhibition of endothelial nitric oxide production involves oxidative stress-mediated constitutive eNOS/HSP90 interaction and disruption of agonist-mediated Akt activation.	Nitric Oxide	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
25882550-3	2015	Ganetespib is a highly potent second generation HSP90 inhibitor which we show is significantly more effective against primary AML blasts at nanomolar concentrations when compared with cytarabine (p&lt;0.001).	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
25882550-7	2015	The combination of cytotoxic cell death, suppression of cytoprotective/drug resistance mechanisms such as AKT and reduced clinical toxicity compared to other HSP90 inhibitors provide strong rationale for the clinical assessment of ganetespib in AML.	STA 9090	231-241	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
25946558-7	2015	TBBX induced Hsp90 hyper-acetylation and led to the disruption of cyclin D1/Hsp90 and CDK4/Hsp90 association following the degradation of cyclin D1 and CDK4 proteins through proteasome.	tbbx	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
25946558-7	2015	TBBX induced Hsp90 hyper-acetylation and led to the disruption of cyclin D1/Hsp90 and CDK4/Hsp90 association following the degradation of cyclin D1 and CDK4 proteins through proteasome.	tbbx	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
25946558-7	2015	TBBX induced Hsp90 hyper-acetylation and led to the disruption of cyclin D1/Hsp90 and CDK4/Hsp90 association following the degradation of cyclin D1 and CDK4 proteins through proteasome.	tbbx	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
25946558-9	2015	Conclusively, the data suggested that TBBX induced G1 growth arrest may mediate HDAC6-caused Hsp90 hyper-acetylation and consequently increased the degradation of cyclin D1 and CDK4.	tbbx	38-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
26674599-0	2015	HSP90 Inhibitor Geldanamycin as a Radiation Response Modificator in Human Blood Cells.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
26674599-2	2015	Geldanamycin (GA), a natural benzoquinone, can inhibit the chaperone activity of Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
26674599-2	2015	Geldanamycin (GA), a natural benzoquinone, can inhibit the chaperone activity of Hsp90.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
26674599-2	2015	Geldanamycin (GA), a natural benzoquinone, can inhibit the chaperone activity of Hsp90.	quinone	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
26674599-3	2015	It has been shown that GA can produce superoxide anions and increase the intracellular oxidative stress, which, in addition to the direct inhibition of Hsp90, might also contribute to the modifying effects of the inhibitor on the early response in human mononuclear cells exposed to ionizing radiation.	geldanamycin	23-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
25945584-7	2015	Dimerization of Tah1 restores the normal binding environment of the bound Hsp90 methionine residue by reconstituting a TPR binding site similar to that in seven-helix-containing TPR domain proteins.	Methionine	80-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
25935150-6	2015	Furthermore, Abeta stimulated the production of reactive oxygen species in endothelial cells and concomitant treatments of the cells with the antioxidant N-acetyl-cysteine (NAC) prevented Abeta effects in promoting HSP90/eNOS interaction and rescued agonist-mediated Akt and eNOS phosphorylation.	Reactive Oxygen Species	48-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
25935150-6	2015	Furthermore, Abeta stimulated the production of reactive oxygen species in endothelial cells and concomitant treatments of the cells with the antioxidant N-acetyl-cysteine (NAC) prevented Abeta effects in promoting HSP90/eNOS interaction and rescued agonist-mediated Akt and eNOS phosphorylation.	Acetylcysteine	154-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
25935150-6	2015	Furthermore, Abeta stimulated the production of reactive oxygen species in endothelial cells and concomitant treatments of the cells with the antioxidant N-acetyl-cysteine (NAC) prevented Abeta effects in promoting HSP90/eNOS interaction and rescued agonist-mediated Akt and eNOS phosphorylation.	Acetylcysteine	173-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
25721082-7	2015	When combined with the Hsp90 inhibitor NVP-AUY922 the concentration of NZ28 could be significantly reduced (1/10th-1/20th) to achieve the same radiosensitization.	nz28	71-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
25756299-0	2015	Cucurbitacin D Is a Disruptor of the HSP90 Chaperone Machinery.	cucurbitacin D	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
26033609-3	2015	Dipeptides stimulate cell renewal processes by activating synthesis of Ki-67 and reducing expression of caspase-9 and enhance antioxidant function of the cells by stimulating the expression of Hsp-90 and inducible NO-synthase.	Dipeptides	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-199
25433307-9	2015	Furthermore, belinostat attenuated the 5-fluorouracil mediated induction of thymidylate synthase via HSP90 hyperacetylation.	belinostat	13-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
25433307-9	2015	Furthermore, belinostat attenuated the 5-fluorouracil mediated induction of thymidylate synthase via HSP90 hyperacetylation.	Fluorouracil	39-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
25756299-9	2015	Cucurbitacin D also disrupted interactions between Hsp90 and two cochaperones, Cdc37 and p23.	cucurbitacin D	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
25652452-4	2015	In our earlier study we demonstrated an inhibitor-kappaB kinase-beta (IKKbeta)-Hsp90 interaction in a high-glucose environment.	Glucose	107-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
25782750-3	2015	We used stable isotope labeling and antibody-based peptide enrichment to quantify more than 1500 protein sites modified with a Gly-Gly motif, the remnant of ubiquitination, in human T-cells treated with an Hsp90 inhibitor.	Glycylglycine	127-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
25782750-4	2015	We observed rapid changes in GlyGly-modification sites, with strong increases for some Hsp90 clients but also decreases for a majority of cellular proteins.	Glycylglycine	29-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
25782750-6	2015	Overall the data support the notion that for Hsp90 clients GlyGly-modification correlates with targeting by the ubiquitin-proteasome system and decay, while for other proteins levels of GlyGly-modification appear to be mainly influenced by their synthesis rates.	Glycylglycine	59-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
25782750-6	2015	Overall the data support the notion that for Hsp90 clients GlyGly-modification correlates with targeting by the ubiquitin-proteasome system and decay, while for other proteins levels of GlyGly-modification appear to be mainly influenced by their synthesis rates.	Glycylglycine	186-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
26097875-0	2015	FS-93, an Hsp90 inhibitor, induces G2/M arrest and apoptosis via the degradation of client proteins in oncogene addicted and derived resistant cancer cells.	fs-93	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
25652452-11	2015	These studies not only reinforce the significance of maintaining a homeostatic balance of eNOS and IKKbeta within the cell system that regulates NO production, but they also confirm that the IKKbeta-Hsp90 interaction is favored in a high-glucose environment, leading to impairment of the eNOS-Hsp90 interaction, which contributes to endothelial dysfunction and vascular complications in diabetes.	Glucose	238-245	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
25778412-6	2015	Furthermore, geldanamycin, an inhibitor of ATPase activity in HSP90, caused BES1 hyperphosphorylation and disrupted the expression of BR-responsive genes.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
25785725-4	2015	The isopropyl amine of the Hsp90 inhibitor PU-H71 was replaced with the mitochondria-targeting moiety triphenylphosphonium to produce SMTIN-P01.	2-propylamine	4-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
25785725-4	2015	The isopropyl amine of the Hsp90 inhibitor PU-H71 was replaced with the mitochondria-targeting moiety triphenylphosphonium to produce SMTIN-P01.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
25681003-10	2015	The compound 1b (17-[2-(piperidinyl-1"-yl)-ethylamino]-17-demethoxygeldanamycin) exhibited the highest anti-proliferation activity in MCF7, HeLa and HCT116 cells, which was much more effective than GA and the developing Hsp90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin).	17-[2-(piperidinyl-1"-yl)-ethylamino]-17-demethoxygeldanamycin	17-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
25096912-7	2015	In 17-AAG- and paclitaxel-treated cells, compared with paclitaxel alone-treated cells, the protein levels of hsp90, hsp70, and hsc70 increased.	Paclitaxel	15-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
25096912-7	2015	In 17-AAG- and paclitaxel-treated cells, compared with paclitaxel alone-treated cells, the protein levels of hsp90, hsp70, and hsc70 increased.	Paclitaxel	55-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
25645596-2	2015	The induction of the HO-1 by solanesol is majorly achieved via enhancing the nuclear translocation and transactivity of Nrf2 through enhancement of Hsp90-Keap1 interaction, while solanesol-elevated Hsp70 is related with promoting the nuclear translocation of HSF1 through the involvement of chaperones interaction.	solanesol	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
25940182-1	2015	OBJECTIVE: To explore the effect of heat shock protein 90 (HSP90) inhibitor (17-DMAG) and oxaliplatin on the proliferation and invasion of colorectal cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	77-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-57
25940182-1	2015	OBJECTIVE: To explore the effect of heat shock protein 90 (HSP90) inhibitor (17-DMAG) and oxaliplatin on the proliferation and invasion of colorectal cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	77-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
25874011-1	2015	Previously, we found that the unconventional small human heat-shock protein HSPB11 inhibits cell death by HSP90 mediated cholesterol-rich membrane microdomain dependent activation of phosphatidylinositol-3 kinase/protein kinase B pathway and by stabilising the mitochondrial membrane systems.	Cholesterol	121-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
25668752-9	2015	These later efforts have led to the discovery of a uniquely selective benzoquinone ansamycin-inspired Hsp90 inhibitor that lacks the problematic quinone present in the natural series.	benzoquinone ansamycin	70-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
25668752-9	2015	These later efforts have led to the discovery of a uniquely selective benzoquinone ansamycin-inspired Hsp90 inhibitor that lacks the problematic quinone present in the natural series.	quinone	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
25689674-4	2015	Examples are prodrugs derived from mycophenolic acid as immunosuppressants and the Hsp-90 inhibitor, AT13387, which is in phase-II clinical trials for the treatment of small cell lung cancer and melanoma.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	101-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-89
25677667-1	2015	Two novel series of oxazepine and diazepine based HSP90 inhibitors are reported.	Diazepine	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25677667-3	2015	Computational modelling was used to build into a solvent exposed pocket near the opening of the ATP binding site, which led to potent inhibitors of HSP90 (25-30).	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
25867902-0	2015	A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
25867902-3	2015	However, the molecular mechanism for the ATP-dependent working cycle of Hsp90 is still not fully understood.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
25867902-4	2015	In this study, we use NMR techniques to investigate the structural characteristics and dynamic behaviors of Hsp90 N-terminal domain in its free and AMPPCP (ATP analogue) or ADP-bound states.	5'-adenylyl (beta,gamma-methylene)diphosphonate	148-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
25867902-4	2015	In this study, we use NMR techniques to investigate the structural characteristics and dynamic behaviors of Hsp90 N-terminal domain in its free and AMPPCP (ATP analogue) or ADP-bound states.	Adenosine Triphosphate	156-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
25867902-4	2015	In this study, we use NMR techniques to investigate the structural characteristics and dynamic behaviors of Hsp90 N-terminal domain in its free and AMPPCP (ATP analogue) or ADP-bound states.	Adenosine Diphosphate	173-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
25867902-5	2015	We demonstrated that although AMPPCP and ADP bind to almost the same region of Hsp90, significantly different effects on the dynamics behaviors of the key structural elements were observed.	5'-adenylyl (beta,gamma-methylene)diphosphonate	30-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
25867902-5	2015	We demonstrated that although AMPPCP and ADP bind to almost the same region of Hsp90, significantly different effects on the dynamics behaviors of the key structural elements were observed.	Adenosine Diphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
25867902-6	2015	AMPPCP binding favors the formation of the active homodimer of Hsp90 by enhancing the slow-motion featured conformational exchanges of those residues (A117-A141) within the lid segment (A111-G135) and around region, while ADP binding keeps Hsp90 staying at the inactive state by increasing the conformational rigidity of the lid segment and around region.	Adenosine Diphosphate	222-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
25867902-7	2015	Based on our findings, a dynamic working model for the ATP-dependent functioning cycle of Hsp90 was proposed.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
25497213-10	2015	GENERAL SIGNIFICANCE: The results obtained suggested that the strong antiproliferative activity of isoxazolo naphthoquinones is not due to the Hsp90 inhibition, but mainly to the interaction at the level of telomeres and/or at the level of gene promoter.	isoxazolo naphthoquinones	99-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
25778412-6	2015	Furthermore, geldanamycin, an inhibitor of ATPase activity in HSP90, caused BES1 hyperphosphorylation and disrupted the expression of BR-responsive genes.	Brassinosteroids	134-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
26579773-8	2015	These findings are applied to a challenging test set involving a series of geldanamycin-based inhibitors of heat shock protein 90 (Hsp90).	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-129
25680466-2	2015	Here, we identify a small molecule Hsp90 inhibitor radicicol that induces intracellular accumulation of cytotoxic clusterin variant.	monorden	51-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
25742791-0	2015	Identification of epipolythiodioxopiperazines HDN-1 and chaetocin as novel inhibitor of heat shock protein 90.	epipolythiodioxopiperazines	18-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
25742791-0	2015	Identification of epipolythiodioxopiperazines HDN-1 and chaetocin as novel inhibitor of heat shock protein 90.	chaetocin	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
25742791-2	2015	HDN-1, an epipolythiopiperazine-2, 5-diones (ETPs) compound, was here identified as a new Hsp90 inhibitor.	sirodesmin	10-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
25742791-2	2015	HDN-1, an epipolythiopiperazine-2, 5-diones (ETPs) compound, was here identified as a new Hsp90 inhibitor.	sirodesmin	45-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
25742791-3	2015	HDN-1 bound directly to C-terminus of Hsp90alpha, resulting in a potential conformational change that interfered with the binding of 17-AAG and novobiocin to Hsp90alpha.	tanespimycin	133-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-48
25742791-3	2015	HDN-1 bound directly to C-terminus of Hsp90alpha, resulting in a potential conformational change that interfered with the binding of 17-AAG and novobiocin to Hsp90alpha.	tanespimycin	133-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-168
25742791-3	2015	HDN-1 bound directly to C-terminus of Hsp90alpha, resulting in a potential conformational change that interfered with the binding of 17-AAG and novobiocin to Hsp90alpha.	Novobiocin	144-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-48
25742791-3	2015	HDN-1 bound directly to C-terminus of Hsp90alpha, resulting in a potential conformational change that interfered with the binding of 17-AAG and novobiocin to Hsp90alpha.	Novobiocin	144-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-168
25742791-4	2015	In contrast, association of 17-AAG, novobiocin or ATP with Hsp90alpha did not prevent the binding HDN-1 to Hsp90alpha.	Adenosine Triphosphate	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-69
25742791-8	2015	Notably, chaetocin, used as a SUV39H1 inhibitor with similar structure to HDN-1, bound to Hsp90 and degraded Hsp90 client proteins and SUV39H1 as did HDN-1.	chaetocin	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
25742791-8	2015	Notably, chaetocin, used as a SUV39H1 inhibitor with similar structure to HDN-1, bound to Hsp90 and degraded Hsp90 client proteins and SUV39H1 as did HDN-1.	chaetocin	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
25742791-9	2015	These results indicate that HDN-1 and chaetocin are inhibitors of Hsp90 and that SUV39H1 is a novel client protein of Hsp90.	chaetocin	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
26579773-8	2015	These findings are applied to a challenging test set involving a series of geldanamycin-based inhibitors of heat shock protein 90 (Hsp90).	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
25501619-2	2015	The natural inhibitors, ansamycins influence the Hsp90 chaperone function by preventing its binding to client proteins and resulting in their proteasomal degradation.	Lactams, Macrocyclic	24-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
25656927-0	2015	Targeting the Hsp90 C-terminal domain by the chemically accessible dihydropyrimidinone scaffold.	thiazolo(2,3-b)dihydropyrimidinone	67-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
25656927-2	2015	Here we report the identification of a new dihydropyrimidinone binding the C-terminus, which is not structurally related to other well-known natural and nature-inspired inhibitors of this second druggable Hsp90 site.	thiazolo(2,3-b)dihydropyrimidinone	43-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
25604133-10	2015	In addition, EGCG bound HSP90 mutants that mimic both complexed and uncomplexed HSP90.	epigallocatechin gallate	13-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
25604133-10	2015	In addition, EGCG bound HSP90 mutants that mimic both complexed and uncomplexed HSP90.	epigallocatechin gallate	13-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
25604133-11	2015	Consistent with HSP90 inhibitory activity, EGCG, novobiocin, and 17-AAG induced changes in HSP90-client proteins in NT cells and larger differences in metastatic cells.	epigallocatechin gallate	43-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
25604133-11	2015	Consistent with HSP90 inhibitory activity, EGCG, novobiocin, and 17-AAG induced changes in HSP90-client proteins in NT cells and larger differences in metastatic cells.	epigallocatechin gallate	43-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
25604133-11	2015	Consistent with HSP90 inhibitory activity, EGCG, novobiocin, and 17-AAG induced changes in HSP90-client proteins in NT cells and larger differences in metastatic cells.	Novobiocin	49-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
25604133-11	2015	Consistent with HSP90 inhibitory activity, EGCG, novobiocin, and 17-AAG induced changes in HSP90-client proteins in NT cells and larger differences in metastatic cells.	Novobiocin	49-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
25604133-11	2015	Consistent with HSP90 inhibitory activity, EGCG, novobiocin, and 17-AAG induced changes in HSP90-client proteins in NT cells and larger differences in metastatic cells.	tanespimycin	65-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
25604133-11	2015	Consistent with HSP90 inhibitory activity, EGCG, novobiocin, and 17-AAG induced changes in HSP90-client proteins in NT cells and larger differences in metastatic cells.	tanespimycin	65-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
25654488-6	2015	In addition, triazoles active as HSP90 inhibitors (as compound 41, IC50 = 29 nM) were synthesized.	Triazoles	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
25818779-0	2015	[Effect of anacardic acid, a Hsp90 inhibitor, on proliferation, invasion and migration of breast cancer MDA-MB-231 cells].	anacardic acid	11-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25853099-1	2015	Heat shock protein 90 (Hsp90) is an adenosine triphosphate dependent molecular chaperone in eukaryotic cells that regulates the activation and maintenance of numerous regulatory and signaling proteins including epidermal growth factor receptor, human epidermal growth factor receptor 2, mesenchymal-epithelial transition factor, cyclin-dependent kinase-4, protein kinase B, hypoxia-inducible factor 1alpha, and matrix metalloproteinase-2.	Adenosine Triphosphate	36-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
25853099-1	2015	Heat shock protein 90 (Hsp90) is an adenosine triphosphate dependent molecular chaperone in eukaryotic cells that regulates the activation and maintenance of numerous regulatory and signaling proteins including epidermal growth factor receptor, human epidermal growth factor receptor 2, mesenchymal-epithelial transition factor, cyclin-dependent kinase-4, protein kinase B, hypoxia-inducible factor 1alpha, and matrix metalloproteinase-2.	Adenosine Triphosphate	36-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
25818779-1	2015	OBJECTIVE: To explore the effect of the Hsp90 inhibitor anacardic acid on cell proliferation, invasion and migration of breast cancer MDA-MB-231 cells.	anacardic acid	56-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
25818779-2	2015	METHODS: The inhibitory effect of anacardic acid on Hsp90 was assessed with in vitro ATPase inhibition assay and ATP-sepharose binding assay.	anacardic acid	34-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
25818779-2	2015	METHODS: The inhibitory effect of anacardic acid on Hsp90 was assessed with in vitro ATPase inhibition assay and ATP-sepharose binding assay.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
25818779-2	2015	METHODS: The inhibitory effect of anacardic acid on Hsp90 was assessed with in vitro ATPase inhibition assay and ATP-sepharose binding assay.	Sepharose	117-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
25818779-5	2015	Western blotting was performed to assess the effect of anacardic acid in triggering the degradation of MMP-9, TIMP-1, Hsp90, and Hsp70.	anacardic	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
25818779-10	2015	CONCLUSION: Anacardic acid can significantly inhibit the proliferation, invasion, and migration of MDA-MB-231 cells, the mechanism of which may involve the inhibition of Hsp90 ATPse activity and down-regulation of MMP-9 expression.	anacardic acid	12-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
25719250-5	2015	Indeed, withanolide E treatment altered the stability of a number of HSP90 client proteins, but with greater apparent specificity than the well-known HSP90 inhibitor geldanamycin.	Withanolides	8-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
25719250-5	2015	Indeed, withanolide E treatment altered the stability of a number of HSP90 client proteins, but with greater apparent specificity than the well-known HSP90 inhibitor geldanamycin.	geldanamycin	166-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
25719250-8	2015	Owing to its novel activity, withanolide E is a promising reagent for the analysis of mechanisms of TRAIL resistance, for understanding HSP90 function, and for further therapeutic development.	Withanolides	29-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
25619116-0	2015	Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.	Serine	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
25402753-8	2015	Structure-function studies determined that disruption of Hsp90alpha/Aha1 association and inhibition of cell migration correlated with the presence of a benzamide side chain, since an acetamide substituted analog was less effective.	benzamide	152-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-67
25604133-0	2015	The heat shock protein 90 inhibitor, (-)-epigallocatechin gallate, has anticancer activity in a novel human prostate cancer progression model.	epigallocatechin gallate	37-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
25604133-3	2015	Our laboratory previously showed that EGCG inhibits heat shock protein 90 (HSP90).	epigallocatechin gallate	38-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-73
25604133-3	2015	Our laboratory previously showed that EGCG inhibits heat shock protein 90 (HSP90).	epigallocatechin gallate	38-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
25604133-8	2015	To elucidate the mechanism of EGCG action, we performed binding assays with EGCG-Sepharose, a C-terminal HSP90 antibody, and HSP90 mutants.	epigallocatechin gallate	30-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
25604133-8	2015	To elucidate the mechanism of EGCG action, we performed binding assays with EGCG-Sepharose, a C-terminal HSP90 antibody, and HSP90 mutants.	epigallocatechin gallate	30-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
25604133-9	2015	These experiments revealed that EGCG-Sepharose bound more HSP90 from metastatic cells compared with NT cells and binding occurred through the HSP90 C-terminus.	epigallocatechin gallate	32-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
25604133-9	2015	These experiments revealed that EGCG-Sepharose bound more HSP90 from metastatic cells compared with NT cells and binding occurred through the HSP90 C-terminus.	epigallocatechin gallate	32-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
25604133-9	2015	These experiments revealed that EGCG-Sepharose bound more HSP90 from metastatic cells compared with NT cells and binding occurred through the HSP90 C-terminus.	Sepharose	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
25604133-9	2015	These experiments revealed that EGCG-Sepharose bound more HSP90 from metastatic cells compared with NT cells and binding occurred through the HSP90 C-terminus.	Sepharose	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
25501124-0	2015	Dual inhibition of Bcr-Abl and Hsp90 by C086 potently inhibits the proliferation of imatinib-resistant CML cells.	Imatinib Mesylate	84-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
25576869-0	2015	Reactive oxygen species promote heat shock protein 90-mediated HBV capsid assembly.	Reactive Oxygen Species	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
25576869-4	2015	Hsp90 prevents cellular component from oxidative stress, and GSH acts as antioxidants scavenging ROS in the cell.	Reactive Oxygen Species	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25576869-6	2015	Based on the previous study that Hsp90 facilitates HBV capsid assembly, which is an important step for the packing of viral particles, here, we show that ROS enrich Hsp90-driven HBV capsid formation.	Reactive Oxygen Species	154-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
25576869-6	2015	Based on the previous study that Hsp90 facilitates HBV capsid assembly, which is an important step for the packing of viral particles, here, we show that ROS enrich Hsp90-driven HBV capsid formation.	Reactive Oxygen Species	154-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
25576869-7	2015	In cell-free system, HBV capsid assembly was facilitated by ROS with Hsp90, whereas it was decreased without Hsp90.	Reactive Oxygen Species	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
25576869-8	2015	In addition, GSH inhibited the function of Hsp90 to decrease HBV capsid assembly.	Glutathione	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
25588944-0	2015	A Tetrahymena Hsp90 co-chaperone promotes siRNA loading by ATP-dependent and ATP-independent mechanisms.	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
25588944-0	2015	A Tetrahymena Hsp90 co-chaperone promotes siRNA loading by ATP-dependent and ATP-independent mechanisms.	Adenosine Triphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
25588944-3	2015	We show that the Tetrahymena Hsp90 co-chaperone Coi12p promotes siRNA loading into the Argonaute protein Twi1p in both ATP-dependent and ATP-independent manners in vitro.	coi12p	48-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25588944-3	2015	We show that the Tetrahymena Hsp90 co-chaperone Coi12p promotes siRNA loading into the Argonaute protein Twi1p in both ATP-dependent and ATP-independent manners in vitro.	Adenosine Triphosphate	119-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25588944-3	2015	We show that the Tetrahymena Hsp90 co-chaperone Coi12p promotes siRNA loading into the Argonaute protein Twi1p in both ATP-dependent and ATP-independent manners in vitro.	Adenosine Triphosphate	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25588944-4	2015	The ATP-dependent activity requires Hsp90 and the tetratricopeptide repeat (TPR) domain of Coi12p, whereas these factors are dispensable for the ATP-independent activity.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
25588944-6	2015	Although Coi12p lacking its TPR domain does not bind to Hsp90, it can partially restore the siRNA loading and DNA elimination defects of COI12 knockout cells, suggesting that Hsp90- and ATP-independent loading of siRNA occurs in vivo and plays a physiological role in Tetrahymena.	coi12p	9-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
25402753-9	2015	Our results show that disruption of Hsp90alpha/Aha1 interactions with novobiocin-based Hsp90 C-terminal inhibitors may limit the metastatic potential of tumors.	Novobiocin	70-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-46
25402753-9	2015	Our results show that disruption of Hsp90alpha/Aha1 interactions with novobiocin-based Hsp90 C-terminal inhibitors may limit the metastatic potential of tumors.	Novobiocin	70-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
25567070-4	2015	Critical proteins that bind with high affinity to elemental selenium during SeNPs self-assembly were identified through proteomics analysis; these include glycolytic enzymes, insoluble tubulin, and heat shock proteins 90 (HSP90).	Selenium	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-220
25567070-4	2015	Critical proteins that bind with high affinity to elemental selenium during SeNPs self-assembly were identified through proteomics analysis; these include glycolytic enzymes, insoluble tubulin, and heat shock proteins 90 (HSP90).	Selenium	60-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	222-227
25184514-0	2015	Progesterone receptor chaperone complex-based high-throughput screening assay: identification of capsaicin as an inhibitor of the Hsp90 machine.	Capsaicin	97-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
25490978-2	2015	In particular, a novel 2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazine structure was prepared exclusively with this new method and was found to have moderate Hsp90 inhibitory activity.	2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazine	23-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
25490978-3	2015	A crystalline complex with N-terminus ATP domain of Hsp90 and one of the new Hsp90 inhibitors was also obtained to elucidate the origin of activity of 2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazines.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
25490978-3	2015	A crystalline complex with N-terminus ATP domain of Hsp90 and one of the new Hsp90 inhibitors was also obtained to elucidate the origin of activity of 2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazines.	2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazines	151-197	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
25490978-3	2015	A crystalline complex with N-terminus ATP domain of Hsp90 and one of the new Hsp90 inhibitors was also obtained to elucidate the origin of activity of 2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazines.	2-piperonyl 3,8-diaminoimidazo[1,2-a]pyrazines	151-197	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
24903735-0	2015	Discovery of novel 17-phenylethylaminegeldanamycin derivatives as potent Hsp90 inhibitors.	17-phenylethylaminegeldanamycin	19-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
24903735-6	2015	Preliminary structure-activity relationship (SAR) and molecular dynamics (MD) simulations of this new series of geldanamycin derivatives were also investigated, suggesting a theoretical model of 17-phenylethylaminegeldanamycins binding to Hsp90.	geldanamycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	239-244
24903735-6	2015	Preliminary structure-activity relationship (SAR) and molecular dynamics (MD) simulations of this new series of geldanamycin derivatives were also investigated, suggesting a theoretical model of 17-phenylethylaminegeldanamycins binding to Hsp90.	17-phenylethylaminegeldanamycins	195-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	239-244
23836447-0	2015	Humic acid induces the endothelial nitric oxide synthase phosphorylation at Ser1177 and Thr495 Via Hsp90alpha and Hsp90beta upregulation in human umbilical vein endothelial cells.	Humic Substances	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-109
25743134-8	2015	Interesting reagents such as PARP and HSP90 inhibitors have been proposed as cancer cell- specific sensitizers for carbon-ion irradiation during basic biological studies, especially those from the Research Project with Heavy Ions at NIRS-HIMAC.	Carbon	115-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25579468-1	2015	The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
25615645-2	2015	HSP90 is a 90kDa protein which functions as an ATP-dependent molecular chaperone that regulates the signalling conformation and expression of multiple protein client proteins especially oncogenic mediators.	Adenosine Triphosphate	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25590805-0	2015	Targeting heat-shock protein 90 with ganetespib for molecularly targeted therapy of gastric cancer.	STA 9090	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-31
25590805-3	2015	Several successful cases of HSP90 inhibitors capable of inhibiting GC inspired us to try ganetespib, a clinically promising and actively investigated second-generation HSP90 inhibitor in GC treatment.	STA 9090	89-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
25590805-3	2015	Several successful cases of HSP90 inhibitors capable of inhibiting GC inspired us to try ganetespib, a clinically promising and actively investigated second-generation HSP90 inhibitor in GC treatment.	STA 9090	89-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
25590805-6	2015	Mechanistically, ganetespib caused pronounced decrease of expression of classic HSP90 client proteins.	STA 9090	17-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
26600741-1	2015	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
26600741-1	2015	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
25490383-0	2015	Down-regulation of MSH2 expression by Hsp90 inhibition enhances cytotoxicity affected by tamoxifen in human lung cancer cells.	Tamoxifen	89-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25490383-8	2015	Compared to a single agent alone, tamoxifen combined with an Hsp90 inhibitor resulted in cytotoxicity and cell growth inhibition synergistically in NSCLC cells, accompanied with reduced MSH2 expression.	Tamoxifen	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
25846761-10	2015	Novel thiazolyl coumarine compounds were determined as valuable C-terminal Hsp90 inhibitors and provide promising templates for the drug design.	thiazolyl coumarine	6-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
25714412-4	2015	Here, we report on the induction of autophagy initiated by the pathogen receptor HSP90AA1 (heat shock protein 90 kDa alpha [cytosolic], class A member 1) via the AKT-MTOR (mechanistic target of rapamycin)-dependent pathway.	Sirolimus	194-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-89
25714412-4	2015	Here, we report on the induction of autophagy initiated by the pathogen receptor HSP90AA1 (heat shock protein 90 kDa alpha [cytosolic], class A member 1) via the AKT-MTOR (mechanistic target of rapamycin)-dependent pathway.	Sirolimus	194-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-152
25497868-7	2015	Treatment with UBS109, EF31 or curcumin inhibited HSP90, NF-kappaB, and HIF-1alpha transcription in PC cell lines.	UBS109	15-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25497868-7	2015	Treatment with UBS109, EF31 or curcumin inhibited HSP90, NF-kappaB, and HIF-1alpha transcription in PC cell lines.	Curcumin	31-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25497868-9	2015	Finally, we demonstrate for the first time that curcumin analogues EF31 and UBS109 induce the downregulation of HIF-1alpha, Hsp90, COX-2 and VEGF in tumor samples from xenograft models compared to untreated xenografts.	Curcumin	48-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
25497868-9	2015	Finally, we demonstrate for the first time that curcumin analogues EF31 and UBS109 induce the downregulation of HIF-1alpha, Hsp90, COX-2 and VEGF in tumor samples from xenograft models compared to untreated xenografts.	UBS109	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
25389633-9	2015	CONCLUSION: Our results demonstrate that AUY922 potently induces cytotoxicity with concomitant modulation of hsp90 client proteins in ATC cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
25449780-0	2015	Novel Hsp90 inhibitor FW-04-806 displays potent antitumor effects in HER2-positive breast cancer cells as a single agent or in combination with lapatinib.	conglobatin	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
25449780-0	2015	Novel Hsp90 inhibitor FW-04-806 displays potent antitumor effects in HER2-positive breast cancer cells as a single agent or in combination with lapatinib.	Lapatinib	144-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
25572106-0	2015	New, non-quinone fluorogeldanamycin derivatives strongly inhibit Hsp90.	quinone	9-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25572106-0	2015	New, non-quinone fluorogeldanamycin derivatives strongly inhibit Hsp90.	fluorogeldanamycin	17-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25477506-4	2015	Fluorescence polarization-based experiments revealed that aurin displays activity as a geldanamycin-competitive Hsp90alpha-antagonist, a finding further substantiated by molecular docking and ATPase inhibition analysis.	aurin	58-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-122
25477506-4	2015	Fluorescence polarization-based experiments revealed that aurin displays activity as a geldanamycin-competitive Hsp90alpha-antagonist, a finding further substantiated by molecular docking and ATPase inhibition analysis.	geldanamycin	87-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-122
25462258-0	2015	Design, synthesis and biological evaluation of biphenylamide derivatives as Hsp90 C-terminal inhibitors.	biphenylamide	47-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
25462258-2	2015	Current drug discovery efforts toward Hsp90 C-terminal inhibition focus on novobiocin, an antibiotic that was transformed into an Hsp90 inhibitor.	Novobiocin	75-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25462258-2	2015	Current drug discovery efforts toward Hsp90 C-terminal inhibition focus on novobiocin, an antibiotic that was transformed into an Hsp90 inhibitor.	Novobiocin	75-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
25462258-3	2015	Based on structural information obtained during the development of novobiocin derivatives and molecular docking studies, scaffolds containing a biphenyl moiety in lieu of the coumarin ring present in novobiocin were identified as new Hsp90 C-terminal inhibitors.	Novobiocin	67-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
25462258-3	2015	Based on structural information obtained during the development of novobiocin derivatives and molecular docking studies, scaffolds containing a biphenyl moiety in lieu of the coumarin ring present in novobiocin were identified as new Hsp90 C-terminal inhibitors.	coumarin	175-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
25462258-3	2015	Based on structural information obtained during the development of novobiocin derivatives and molecular docking studies, scaffolds containing a biphenyl moiety in lieu of the coumarin ring present in novobiocin were identified as new Hsp90 C-terminal inhibitors.	Novobiocin	200-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
25014191-0	2015	Heat shock protein 90 inhibitor mycoepoxydiene modulates kinase signaling in cervical cancer cells and inhibits in-vivo tumor growth.	mycoepoxydiene	32-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
25014191-3	2015	Mycoepoxydiene (MED) can inhibit Hsp90 function and induce apoptosis in cervical cancer cells.	mycoepoxydiene	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
25014191-3	2015	Mycoepoxydiene (MED) can inhibit Hsp90 function and induce apoptosis in cervical cancer cells.	mycoepoxydiene	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
26745117-3	2015	The aim of this study was to evaluate the effects of an ethanol extract Glycyrrhiza glabra on the expression of HSP90, growth and apoptosis in the HT-29 colon cancer cell line.	Ethanol	56-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
25184514-8	2015	Cell survival assays showed that capsaicin selectively kills cancer cells and destabilizes several Hsp90 client proteins.	Capsaicin	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
25920748-0	2015	The HSP90 inhibitor alvespimycin enhances the potency of telomerase inhibition by imetelstat in human osteosarcoma.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
25920748-3	2015	Because the chaperone molecule HSP90 facilitates the assembly of telomerase protein, the ability of the HSP90 inhibitor alvespimycin to potentiate the effect of the telomerase inhibitor was assessed.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	120-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
26460795-0	2015	A Phase I Study of the Hsp90 Inhibitor AUY922 plus Capecitabine for the Treatment of Patients with Advanced Solid Tumors.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	39-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	sodium chlorate	88-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
25692408-7	2015	Further, treatment with the mTOR kinase inhibitor AZD8055 or the Hsp90 inhibitor 17-AAG reversed expression of IAPs and overcame lapatinib resistance in LapR cells.	tanespimycin	81-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25692408-7	2015	Further, treatment with the mTOR kinase inhibitor AZD8055 or the Hsp90 inhibitor 17-AAG reversed expression of IAPs and overcame lapatinib resistance in LapR cells.	Lapatinib	129-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
24973890-4	2015	Significant cell death response upon mEHT treatment was accompanied by the early upregulation (4-h post-treatment) of heat shock protein (Hsp70 and Hsp90) mRNA levels.	meht	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	sodium chlorate	88-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-194
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	sodium chlorate	88-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-194
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
26651243-4	2015	We revealed that Hsp90alpha and Hsp90beta are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.	Heparin	174-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-27
25692408-0	2015	PI3K-independent mTOR activation promotes lapatinib resistance and IAP expression that can be effectively reversed by mTOR and Hsp90 inhibition.	Lapatinib	42-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
25119188-0	2015	Suberoylanilide hydroxamic acid induces ROS-mediated cleavage of HSP90 in leukemia cells.	Vorinostat	0-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25119188-0	2015	Suberoylanilide hydroxamic acid induces ROS-mediated cleavage of HSP90 in leukemia cells.	Reactive Oxygen Species	40-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25119188-2	2015	We found that HSP90 was cleaved to 55 kDa protein after treatment with histone deacetylase (HDAC) inhibitors including suberoylanilide hydroxamic acid (SAHA) in several leukemia cell lines.	Vorinostat	119-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
25119188-2	2015	We found that HSP90 was cleaved to 55 kDa protein after treatment with histone deacetylase (HDAC) inhibitors including suberoylanilide hydroxamic acid (SAHA) in several leukemia cell lines.	Vorinostat	152-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
25119188-4	2015	The SAHA-induced cleavage of HSP90 was blocked by a pan-caspase inhibitor, z-VAD-fmk, implying that the process is dependent on caspase activity.	Vorinostat	4-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25119188-4	2015	The SAHA-induced cleavage of HSP90 was blocked by a pan-caspase inhibitor, z-VAD-fmk, implying that the process is dependent on caspase activity.	benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25119188-6	2015	SAHA induced generation of reactive oxygen species (ROS), and the cleavage of HSP90 was blocked by a ROS scavenger N-acetylcystein (NAC).	Vorinostat	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25119188-6	2015	SAHA induced generation of reactive oxygen species (ROS), and the cleavage of HSP90 was blocked by a ROS scavenger N-acetylcystein (NAC).	Reactive Oxygen Species	27-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25119188-6	2015	SAHA induced generation of reactive oxygen species (ROS), and the cleavage of HSP90 was blocked by a ROS scavenger N-acetylcystein (NAC).	Reactive Oxygen Species	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25119188-6	2015	SAHA induced generation of reactive oxygen species (ROS), and the cleavage of HSP90 was blocked by a ROS scavenger N-acetylcystein (NAC).	N-Acetyl-L-cysteine	115-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25119188-6	2015	SAHA induced generation of reactive oxygen species (ROS), and the cleavage of HSP90 was blocked by a ROS scavenger N-acetylcystein (NAC).	nac	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25119188-7	2015	We also confirmed that hydrogen peroxide (H2O2) induced cleavage of HSP90 in a similar manner.	Hydrogen Peroxide	23-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
25119188-7	2015	We also confirmed that hydrogen peroxide (H2O2) induced cleavage of HSP90 in a similar manner.	Hydrogen Peroxide	42-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
26303164-9	2015	From the western blot and immunoprecipitation analyses, we found that high glucose induced trafficking inhibition through an effect on the expression of Hsp90 and its interaction with hERG.	Glucose	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
25336693-1	2015	PURPOSE: AT13387 is a potent second-generation, fragment-derived HSP90 inhibitor.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	9-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
25989799-0	2015	Withaferin A Regulates LRRK2 Levels by Interfering with the Hsp90- Cdc37 Chaperone Complex.	withaferin A	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
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
25119188-9	2015	Treatment of the cells with caspase 10 inhihitor, but not other inhibitors of caspases activated by SAHA, prevented cleavage of HSP90 by SAHA.	Vorinostat	137-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
25119188-10	2015	SAHA-induced ROS generation and HSP90 cleavage were dependent on newly synthesized unknown proteins.	Vorinostat	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
25119188-11	2015	Taken together, our results suggest that the cleavage of HSP90 by SAHA is mediated by ROS generation and caspase 10 activation.	Vorinostat	66-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
25119188-11	2015	Taken together, our results suggest that the cleavage of HSP90 by SAHA is mediated by ROS generation and caspase 10 activation.	Reactive Oxygen Species	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
25367763-3	2015	The relative resistance of K562 cells to bortezomib correlated well with significantly higher expression of HSP27, HSP70, HSP90alpha, HSP90beta and GRP75 in these cells.	Bortezomib	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-132
25367763-4	2015	Incubation of both HL-60 and K562 cells with bortezomib induced a cleavage of HSP90beta as well as expression of HSP70 and HSP90beta but bortezomib did not affect levels of HSP27, HSP90alpha, GRP75 and GRP78.	Bortezomib	45-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-190
25821558-0	2015	HSP90 inhibitor AUY922 induces cell death by disruption of the Bcr-Abl, Jak2 and HSP90 signaling network complex in leukemia cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25821558-0	2015	HSP90 inhibitor AUY922 induces cell death by disruption of the Bcr-Abl, Jak2 and HSP90 signaling network complex in leukemia cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
25333998-2	2015	SNX-2112, a selective heat shock protein 90 (Hsp90) inhibitor, was recently reported as being effective in combination with cisplatin and paclitaxel.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-43
25333998-2	2015	SNX-2112, a selective heat shock protein 90 (Hsp90) inhibitor, was recently reported as being effective in combination with cisplatin and paclitaxel.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
25333998-2	2015	SNX-2112, a selective heat shock protein 90 (Hsp90) inhibitor, was recently reported as being effective in combination with cisplatin and paclitaxel.	Cisplatin	124-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-43
25333998-2	2015	SNX-2112, a selective heat shock protein 90 (Hsp90) inhibitor, was recently reported as being effective in combination with cisplatin and paclitaxel.	Cisplatin	124-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
25333998-2	2015	SNX-2112, a selective heat shock protein 90 (Hsp90) inhibitor, was recently reported as being effective in combination with cisplatin and paclitaxel.	Paclitaxel	138-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-43
25333998-2	2015	SNX-2112, a selective heat shock protein 90 (Hsp90) inhibitor, was recently reported as being effective in combination with cisplatin and paclitaxel.	Paclitaxel	138-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
25333998-9	2015	Moreover, 5-FU partly recovered Hsp90 client proteins, including Akt, p-Akt, inhibitor of kappaB kinase (IKK)alpha, extracellular signal-regulated kinase (ERK)1/2, and glycogen synthase kinase (GSK)-3beta, which SNX-2112 had downregulated.	Fluorouracil	10-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
25333998-10	2015	Taken together, this is the first report that the combination of SNX-2112 with 5-FU exhibited antagonistic effect in esophageal cancer cells by affecting growth inhibition, cell cycle, apoptosis, and Hsp90 client proteins, suggesting that care is required in the clinical application of combined SNX-2112 and 5-FU.	SNX 2112	65-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
25333998-10	2015	Taken together, this is the first report that the combination of SNX-2112 with 5-FU exhibited antagonistic effect in esophageal cancer cells by affecting growth inhibition, cell cycle, apoptosis, and Hsp90 client proteins, suggesting that care is required in the clinical application of combined SNX-2112 and 5-FU.	Fluorouracil	79-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
25351442-7	2015	The aim of this study was to examine the effects of the Hsp90 inhibitor, geldanamycin (GA), on KTHOS osteosarcoma cells.	geldanamycin	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
25989799-5	2015	In the current study, we explore the regulation of LRRK2 by withaferin A (WA), a potent inhibitor of the interaction between Hsp90 and Cdc37.	withaferin A	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
25989799-8	2015	Additionally, treatment with celastrol, which is also an inhibitor of the Hsp90-Cdc37 complex, decreased LRRK2 levels.	celastrol	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
25145901-11	2015	Geldanamycin increased Hsp70, but elicited cleavage of Hsp90 and subsequently resulted in an increase in H2O2-induced apoptosis.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
25537129-0	2015	In vitro and in vivo Evaluation of 17-phenylpropylamine/phenoxyethylamine- 17-demethoxygeldanamycins as Potent Hsp90 Inhibitors.	17-phenylpropylamine	35-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
25537129-0	2015	In vitro and in vivo Evaluation of 17-phenylpropylamine/phenoxyethylamine- 17-demethoxygeldanamycins as Potent Hsp90 Inhibitors.	phenoxyethylamine- 17-demethoxygeldanamycins	56-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
25537129-5	2015	Additionally, the Hsp90 inhibitory activity of compound 3 was more active than 17-AAG.	tanespimycin	79-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
25537129-6	2015	Docking and molecular dynamics (MD) refinements of this new series of GA derivatives were also investigated, suggesting a theoretical model between 17- phenylpropylamine/phenoxyethyl-amines and Hsp90.	17- phenylpropylamine/phenoxyethyl-amines	148-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
25254964-6	2015	Three compound clusters are studied; (i) the target-driven cluster involving HSP90 inhibitors, geldanamycin and tanespimycin induces differential expression for HSP90-related genes and overlap with pathway response to unfolded protein.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
25254964-6	2015	Three compound clusters are studied; (i) the target-driven cluster involving HSP90 inhibitors, geldanamycin and tanespimycin induces differential expression for HSP90-related genes and overlap with pathway response to unfolded protein.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
25254964-6	2015	Three compound clusters are studied; (i) the target-driven cluster involving HSP90 inhibitors, geldanamycin and tanespimycin induces differential expression for HSP90-related genes and overlap with pathway response to unfolded protein.	tanespimycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
25254964-6	2015	Three compound clusters are studied; (i) the target-driven cluster involving HSP90 inhibitors, geldanamycin and tanespimycin induces differential expression for HSP90-related genes and overlap with pathway response to unfolded protein.	tanespimycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
25564462-0	2015	Translational downregulation of HSP90 expression by iron chelators in neuroblastoma cells.	Iron	52-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
25564462-7	2015	We functionally confirmed iron-dependent depletion of HSP90 and its client proteins at pharmacologically achievable concentrations of CPX, and we extended this effect to piroctone, 8-hydroxyquinoline, and deferasirox.	Iron	26-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
25564462-7	2015	We functionally confirmed iron-dependent depletion of HSP90 and its client proteins at pharmacologically achievable concentrations of CPX, and we extended this effect to piroctone, 8-hydroxyquinoline, and deferasirox.	cpx	134-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
25564462-8	2015	Given the documented sensitivity of NB cells to HSP90 inhibition, we propose CPX and other iron chelators as investigational antitumor agents in NB therapy.	cpx	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
25383758-0	2015	Terazosin activates Pgk1 and Hsp90 to promote stress resistance.	Terazosin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25383758-4	2015	Mechanistically, the ATP generated from Pgk1 may enhance the chaperone activity of Hsp90, an ATPase known to associate with Pgk1.	Adenosine Triphosphate	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
25866220-3	2015	Here we found that Hsp90 inhibitor 17-AAG can sensitize mantle cell lymphoma (MCL) cells to flavopiridol by suppressing flavopiridol-triggered protective autophagy.	tanespimycin	35-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
25866220-3	2015	Here we found that Hsp90 inhibitor 17-AAG can sensitize mantle cell lymphoma (MCL) cells to flavopiridol by suppressing flavopiridol-triggered protective autophagy.	alvocidib	92-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
25866220-3	2015	Here we found that Hsp90 inhibitor 17-AAG can sensitize mantle cell lymphoma (MCL) cells to flavopiridol by suppressing flavopiridol-triggered protective autophagy.	alvocidib	120-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
25334086-0	2015	Comparative effects of SNX-7081 and SNX-2112 on cell cycle, apoptosis and Hsp90 client proteins in human cancer cells.	2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
25334086-1	2015	SNX-2112, a novel 2-aminobenzamide inhibitor of Hsp90, previously showed a broad spectrum of anticancer activity.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
25334086-1	2015	SNX-2112, a novel 2-aminobenzamide inhibitor of Hsp90, previously showed a broad spectrum of anticancer activity.	anthranilamide	18-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
25334086-3	2015	SNX-7081, another closely related Hsp90 inhibitor with a side chain of indole instead of indazole, has recently attracted attention.	SNX-7081	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
25334086-3	2015	SNX-7081, another closely related Hsp90 inhibitor with a side chain of indole instead of indazole, has recently attracted attention.	indole	71-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
25334086-8	2015	Compared with SNX-2112, SNX-7081 exhibited more potent effects on cell apoptosis in four sixths of the human cancer cell lines, and was more active in the downregulation of Hsp90 client proteins.	SNX-7081	24-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
25334086-9	2015	In addition, SNX-7081 exhibited a stronger binding affinity to Hsp90 than SNX-2112 in molecular docking experiments.	SNX-7081	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
25351442-7	2015	The aim of this study was to examine the effects of the Hsp90 inhibitor, geldanamycin (GA), on KTHOS osteosarcoma cells.	geldanamycin	87-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
25351442-11	2015	It was considered that the autophagy inhibitor 3-MA suppressed a protective mechanism induced by Hsp90 inhibitor in tumor cells and induced apoptosis.	3-methyladenine	47-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
25378400-3	2014	In our current study, we find that Aha1 plays a novel, additional role beyond regulating the Hsp90 ATP hydrolysis rate.	Adenosine Triphosphate	99-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
25542032-2	2014	Therefore, we investigated the molecular mechanism of action of IPI-504 (retaspimycin HCl), a potent and selective inhibitor of HSP90, in combination with the microtubule targeting agent (MTA) docetaxel, in preclinical models of NSCLC.	tanespimycin	64-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
25542032-2	2014	Therefore, we investigated the molecular mechanism of action of IPI-504 (retaspimycin HCl), a potent and selective inhibitor of HSP90, in combination with the microtubule targeting agent (MTA) docetaxel, in preclinical models of NSCLC.	tanespimycin	73-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
25699150-0	2015	Design, synthesis, and biological evaluation of ring-constrained novobiocin analogues as hsp90 C-terminal inhibitors.	Novobiocin	65-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
25699150-2	2015	Novobiocin was the first natural product identified as an Hsp90 C-terminal inhibitor; however, it manifests poor antiproliferative activity.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
25383915-0	2014	Discovery and optimization of 4,5-diarylisoxazoles as potent dual inhibitors of pyruvate dehydrogenase kinase and heat shock protein 90.	4,5-diarylisoxazoles	30-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-135
25383915-3	2014	To obtain novel PDHK inhibitors, we took advantage of the homology of the ATP-binding pocket between Heat Shock Protein 90 (HSP90) and PDHK, and utilized 4,5-diarylisoxazole based HSP90 inhibitor for structural design.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-122
25383915-3	2014	To obtain novel PDHK inhibitors, we took advantage of the homology of the ATP-binding pocket between Heat Shock Protein 90 (HSP90) and PDHK, and utilized 4,5-diarylisoxazole based HSP90 inhibitor for structural design.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
25383915-3	2014	To obtain novel PDHK inhibitors, we took advantage of the homology of the ATP-binding pocket between Heat Shock Protein 90 (HSP90) and PDHK, and utilized 4,5-diarylisoxazole based HSP90 inhibitor for structural design.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
25383915-3	2014	To obtain novel PDHK inhibitors, we took advantage of the homology of the ATP-binding pocket between Heat Shock Protein 90 (HSP90) and PDHK, and utilized 4,5-diarylisoxazole based HSP90 inhibitor for structural design.	4,5-diarylisoxazole	154-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-122
25383915-3	2014	To obtain novel PDHK inhibitors, we took advantage of the homology of the ATP-binding pocket between Heat Shock Protein 90 (HSP90) and PDHK, and utilized 4,5-diarylisoxazole based HSP90 inhibitor for structural design.	4,5-diarylisoxazole	154-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
25383915-3	2014	To obtain novel PDHK inhibitors, we took advantage of the homology of the ATP-binding pocket between Heat Shock Protein 90 (HSP90) and PDHK, and utilized 4,5-diarylisoxazole based HSP90 inhibitor for structural design.	4,5-diarylisoxazole	154-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
25349308-7	2014	Cell lines with acquired vemurafenib resistance, derived from these models (A375R and SK-MEL-28R) were also sensitive to HSP90 inhibitor treatment; key clients were depleted, apoptosis was induced, and growth in 3D culture was inhibited.	Vemurafenib	25-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
25487024-2	2015	Molecular chaperones like Hsp70 and Hsp90 fulfil well-defined roles in protein folding and conformational stability via ATP dependent reaction cycles.	Adenosine Triphosphate	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
25484226-3	2014	The N (N-terminal)-M (middle) domain of human Trap1 was crystallized in complex with Hsp90 inhibitors (PU-H71 and BIIB-021) by the hanging-drop vapour-diffusion method at pH 6.5 and 293 K using 15% PEG 8K as a precipitant.	Plutonium	103-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
25218692-6	2014	Reactive oxygen species mediated caspase activation causes degradation of autophagic proteins, cleavage of molecular chaperones (Hsp90 and GRP-78) and adaptor proteins (p62 and NBR1).	Reactive Oxygen Species	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
25444464-0	2014	Ganetespib, a novel Hsp90 inhibitor in patients with KRAS mutated and wild type, refractory metastatic colorectal cancer.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
25444464-2	2014	The primary objective of the current study was to define the safety and efficacy of ganetespib, a novel, selective small-molecule Hsp90 inhibitor, in patients with refractory metastatic colorectal cancer.	STA 9090	84-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
25403416-0	2014	Tumour eradication using synchronous thermal ablation and Hsp90 chemotherapy with protein engineered triblock biopolymer-geldanamycin conjugates.	triblock biopolymer	101-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
25403416-4	2014	MATERIALS AND METHODS: A thermo-responsive, elastin-like polypeptide (ELP)-based tri-block biopolymer was developed and conjugated with a potent Hsp90 inhibitor, geldanamycin (GA).	geldanamycin	162-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
25403416-4	2014	MATERIALS AND METHODS: A thermo-responsive, elastin-like polypeptide (ELP)-based tri-block biopolymer was developed and conjugated with a potent Hsp90 inhibitor, geldanamycin (GA).	geldanamycin	176-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
25280831-0	2014	Low dose Hsp90 inhibitor 17AAG protects neural progenitor cells from ischemia induced death.	tanespimycin	25-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
25280831-4	2014	We report here that treatment with 17-N-Allylamino-17-demethoxygeldanamycin (17AAG), an Hsp90 inhibitor, protected neural progenitor cells (NPCs) against oxygen glucose deprivation (OGD) induced cell death in a dose dependent fashion.	tanespimycin	35-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
25280831-4	2014	We report here that treatment with 17-N-Allylamino-17-demethoxygeldanamycin (17AAG), an Hsp90 inhibitor, protected neural progenitor cells (NPCs) against oxygen glucose deprivation (OGD) induced cell death in a dose dependent fashion.	tanespimycin	77-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
25115740-0	2014	Profiling Hsp90 differential expression and the molecular effects of the Hsp90 inhibitor IPI-504 in high-grade glioma models.	tanespimycin	89-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
25115740-1	2014	Retaspimycin hydrochloride (IPI-504), an Hsp90 (heat shock protein 90) inhibitor, has shown activity in multiple preclinical cancer models, such as lung, breast and ovarian cancers.	tanespimycin	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
25115740-1	2014	Retaspimycin hydrochloride (IPI-504), an Hsp90 (heat shock protein 90) inhibitor, has shown activity in multiple preclinical cancer models, such as lung, breast and ovarian cancers.	tanespimycin	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
25115740-1	2014	Retaspimycin hydrochloride (IPI-504), an Hsp90 (heat shock protein 90) inhibitor, has shown activity in multiple preclinical cancer models, such as lung, breast and ovarian cancers.	tanespimycin	28-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
25115740-1	2014	Retaspimycin hydrochloride (IPI-504), an Hsp90 (heat shock protein 90) inhibitor, has shown activity in multiple preclinical cancer models, such as lung, breast and ovarian cancers.	tanespimycin	28-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
25115740-7	2014	Hsp90 inhibition by IPI-504 induced apoptosis, blocked migration and invasion, and significantly decreased epidermal growth factor receptor levels, mitogen-activated protein kinase and/or Akt activities, and secretion of vascular endothelial growth factor in glioma cell lines.	tanespimycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25115740-9	2014	These findings suggest that targeting Hsp90 by IPI-504 has the potential to become an active therapeutic strategy in gliomas in a selective group of patients, but further research into combination therapies is still needed.	tanespimycin	47-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
25349308-9	2014	These data suggest that treatment with an HSP90 inhibitor, such as AT13387, is a potential approach for combating resistance to BRAF and MEK inhibition in melanoma.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	67-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
25313505-0	2014	Discovery of potent N-(isoxazol-5-yl)amides as HSP90 inhibitors.	n-(isoxazol-5-yl)amides	20-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
25310629-2	2014	Moreover, we aimed to determine the effect of geldanamycin (GA), an inhibitor of Hsp90, on the proliferation and apoptosis of human gastric carcinoma cells.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
25310629-2	2014	Moreover, we aimed to determine the effect of geldanamycin (GA), an inhibitor of Hsp90, on the proliferation and apoptosis of human gastric carcinoma cells.	geldanamycin	60-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
24752588-7	2014	In addition, co-immunoprecipitation was used to investigate the interaction between Akt and Hsp90, Akt and protein phosphatase-2A (PP2A) in the MG132-treated organotypic hippocampal slices.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	144-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
25375091-1	2014	Our previous study demonstrated NVP-AUY922, a HSP90AA1 inhibitor, could enhance mutant KIT degradation in gastrointestinal stromal tumor (GIST) cells through both proteasome- and autophagy-mediated pathways.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-54
25320090-7	2014	Only the ATP-bound form of Hsp90 interacts with disordered CTA1, and refolding of CTA1 by Hsp90 is dependent upon ATP hydrolysis.	Adenosine Triphosphate	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
25320090-7	2014	Only the ATP-bound form of Hsp90 interacts with disordered CTA1, and refolding of CTA1 by Hsp90 is dependent upon ATP hydrolysis.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
25320090-7	2014	Only the ATP-bound form of Hsp90 interacts with disordered CTA1, and refolding of CTA1 by Hsp90 is dependent upon ATP hydrolysis.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
25313505-2	2014	Here, we described the fragment screening, synthesis and structure-activity relationship studies of small molecule inhibitors with 4,5-diarylisoxazole scaffold targeting HSP90.	4,5-diarylisoxazole	131-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
24706460-0	2014	HSP90 inhibitor AUY922 abrogates up-regulation of RTKs by mTOR inhibitor AZD8055 and potentiates its antiproliferative activity in human breast cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25277067-0	2014	Discovery of diamine-linked 17-aroylamido-17-demethoxygeldanamycins as potent Hsp90 inhibitors.	Diamines	13-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25277067-0	2014	Discovery of diamine-linked 17-aroylamido-17-demethoxygeldanamycins as potent Hsp90 inhibitors.	17-aroylamido-17-demethoxygeldanamycins	28-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
25277067-2	2014	Geldanamycin (GA), the first Hsp90 inhibitor, has potent antitumor activity, but showed significant hepatotoxicity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25277067-2	2014	Geldanamycin (GA), the first Hsp90 inhibitor, has potent antitumor activity, but showed significant hepatotoxicity.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
24706460-0	2014	HSP90 inhibitor AUY922 abrogates up-regulation of RTKs by mTOR inhibitor AZD8055 and potentiates its antiproliferative activity in human breast cancer.	(5-(2,4-bis((3S)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol	73-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25368984-1	2014	Utilizing structure-based drug design, a novel dihydropyridopyrimidinone series which exhibited potent Hsp90 inhibition, good pharmacokinetics upon oral administration, and an excellent pharmacokinetic/pharmacodynamic relationship in vivo was developed from a commercial hit.	3,4-Dihydropyrido[3,2-d]pyrimidin-2(1H)-one	47-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
25268573-4	2014	In this study, using the Hsp90/Aha1 macrocomplex as a model (where Hsp denotes a heat shock protein), we optimized a double cross-linking protocol with 1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide (EDC).	Ethyldimethylaminopropyl Carbodiimide	152-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
24706460-11	2014	The combination of AZD8055 and AUY922 demonstrated synergistic activity against various types of breast cancer and established a mechanistic rationale for a combination approach using catalytic mTOR kinase inhibitor and HSP90 inhibitor in the treatment of breast cancer.	(5-(2,4-bis((3S)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol	19-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
24706460-11	2014	The combination of AZD8055 and AUY922 demonstrated synergistic activity against various types of breast cancer and established a mechanistic rationale for a combination approach using catalytic mTOR kinase inhibitor and HSP90 inhibitor in the treatment of breast cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	31-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
25268573-4	2014	In this study, using the Hsp90/Aha1 macrocomplex as a model (where Hsp denotes a heat shock protein), we optimized a double cross-linking protocol with 1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide (EDC).	Ethyldimethylaminopropyl Carbodiimide	201-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
25225290-4	2014	We used a high-content immunofluorescence imaging-based kinase inhibitor screen on SKBR-3 breast cancer cells to identify kinases whose inhibition alters the clearance of cell surface ErbB2 induced by Hsp90 inhibitor 17-AAG.	tanespimycin	217-223	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
25244159-1	2014	The molecular chaperone Hsp90 undergoes an ATP-driven cycle of conformational changes in which large structural rearrangements precede ATP hydrolysis.	Adenosine Triphosphate	43-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
25244159-1	2014	The molecular chaperone Hsp90 undergoes an ATP-driven cycle of conformational changes in which large structural rearrangements precede ATP hydrolysis.	Adenosine Triphosphate	135-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
25244159-2	2014	Well-established small-molecule inhibitors of Hsp90 compete with ATP-binding.	Adenosine Triphosphate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
24604074-0	2014	Debio 0932, a new oral Hsp90 inhibitor, alleviates psoriasis in a xenograft transplantation model.	CUDC 305	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24604074-1	2014	Debio 0932 is a novel oral heat shock protein 90 (Hsp90) inhibitor developed for anti-cancer therapy.	CUDC 305	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-48
24604074-1	2014	Debio 0932 is a novel oral heat shock protein 90 (Hsp90) inhibitor developed for anti-cancer therapy.	CUDC 305	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25205430-6	2014	Using HPV-positive and HPV-negative SCC cell lines, we compared baseline HSP90 expression levels and the effect of the HSP90 inhibitor ganetespib on viability and apoptosis.	STA 9090	135-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
24796797-4	2014	HaCaT cells were treated with purified human BP or normal IgG in the absence or presence of the Hsp90 blocker 17-DMAG and effects on viability, interleukin 6 (IL-6) and IL-8 (cytokines critical for BP pathology), NFkappaB (their major transcription factor), and Hsp70 (marker of effective Hsp90 inhibition and potent negative regulator of inflammatory responses) were investigated.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	110-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
25244257-8	2014	Patients taking fluoxetine showed increased HSP90 expression in CA1, and those taking haloperidol decreased HSP90 in the granular layer and subiculum.	Fluoxetine	16-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
25244257-8	2014	Patients taking fluoxetine showed increased HSP90 expression in CA1, and those taking haloperidol decreased HSP90 in the granular layer and subiculum.	Haloperidol	86-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
25262379-0	2014	Phase I dose-escalation studies of SNX-5422, an orally bioavailable heat shock protein 90 inhibitor, in patients with refractory solid tumours.	SNX-5422	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
25262379-1	2014	BACKGROUND: Orally administered SNX-5422, a novel, selective prodrug of the Heat shock protein 90 (Hsp90) inhibitor SNX-2112, was investigated in two sequential phase I studies to determine the safety, maximum tolerated doses (MTDs) and pharmacokinetic profile of SNX-5422.	SNX-5422	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-97
25262379-1	2014	BACKGROUND: Orally administered SNX-5422, a novel, selective prodrug of the Heat shock protein 90 (Hsp90) inhibitor SNX-2112, was investigated in two sequential phase I studies to determine the safety, maximum tolerated doses (MTDs) and pharmacokinetic profile of SNX-5422.	SNX-5422	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
25196280-0	2014	Hsp90 inhibitor 17-AAG sensitizes Bcl-2 inhibitor (-)-gossypol by suppressing ERK-mediated protective autophagy and Mcl-1 accumulation in hepatocellular carcinoma cells.	Gossypol	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25196280-3	2014	In the present study, we are the first to report that Hsp90 inhibitor 17-AAG enhanced (-)-gossypol-induced apoptosis via suppressing (-)-gossypol-triggered protective autophagy and Mcl-1 accumulation.	Gossypol	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
25196280-3	2014	In the present study, we are the first to report that Hsp90 inhibitor 17-AAG enhanced (-)-gossypol-induced apoptosis via suppressing (-)-gossypol-triggered protective autophagy and Mcl-1 accumulation.	Gossypol	133-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
25289059-1	2014	The aim of the present study was to investigate the effect of heat shock protein 90 (Hsp90)-specific inhibitor geldanamycin (GA) on the proliferation and apoptosis induced by vascular endothelial growth factor-C (VEGF-C) in cervical cancer cells.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
25289059-1	2014	The aim of the present study was to investigate the effect of heat shock protein 90 (Hsp90)-specific inhibitor geldanamycin (GA) on the proliferation and apoptosis induced by vascular endothelial growth factor-C (VEGF-C) in cervical cancer cells.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
25289059-1	2014	The aim of the present study was to investigate the effect of heat shock protein 90 (Hsp90)-specific inhibitor geldanamycin (GA) on the proliferation and apoptosis induced by vascular endothelial growth factor-C (VEGF-C) in cervical cancer cells.	geldanamycin	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
25289059-1	2014	The aim of the present study was to investigate the effect of heat shock protein 90 (Hsp90)-specific inhibitor geldanamycin (GA) on the proliferation and apoptosis induced by vascular endothelial growth factor-C (VEGF-C) in cervical cancer cells.	geldanamycin	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
25289059-4	2014	Hsp90 expression was increased 3.31-fold in VEGF-C treated HeLa cells, and this increase was attenuated in the treatment groups (2.17-, 1.69-, 1.82-fold in VEGF-C + KDR-Ab, VEGF-C + PD98059 and VEGF-C + LY294002, respectively).	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	203-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25289059-7	2014	Therefore, the results indicate that the Hsp90-specific inhibitor GA has a critical role in the proliferation and apoptosis induced by VEGF-C in cervical cancer cells.	geldanamycin	66-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
25107562-8	2014	Further experiments demonstrate that resveratrol relieved As2O3-caused endoplasmic reticulum (ER) stress by restoring the function of hERG-Hsp70/Hsp90 chaperone complexes and downregulating the protein expression of ER chaperone proteins (calnexin and calreticulin) and activating transcription factor 6.	Resveratrol	37-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
25107562-8	2014	Further experiments demonstrate that resveratrol relieved As2O3-caused endoplasmic reticulum (ER) stress by restoring the function of hERG-Hsp70/Hsp90 chaperone complexes and downregulating the protein expression of ER chaperone proteins (calnexin and calreticulin) and activating transcription factor 6.	Arsenic Trioxide	58-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
25296971-3	2014	We tested the hypothesis that HSP90 transcriptional and functional inhibition can inhibit cell cycle progression, downregulate TS levels and sensitize colorectal cancer (CRC) cell lines to the effects of 5FU.	Fluorouracil	204-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
25320090-8	2014	In vitro reconstitution of the CTA1 translocation event likewise required ATP hydrolysis by Hsp90.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
25296971-0	2014	HSP90 inhibition downregulates thymidylate synthase and sensitizes colorectal cancer cell lines to the effect of 5FU-based chemotherapy.	Fluorouracil	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25347845-6	2014	Treatment with membrane permeated and impermeable Hsp90 inhibitors 17-AAG and FITC-GA respectively, lead to intracellular accumulation of rNadA, strongly suggesting that the extracellular secreted pool of the chaperone is involved in rNadA intracellular trafficking.	tanespimycin	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25347845-6	2014	Treatment with membrane permeated and impermeable Hsp90 inhibitors 17-AAG and FITC-GA respectively, lead to intracellular accumulation of rNadA, strongly suggesting that the extracellular secreted pool of the chaperone is involved in rNadA intracellular trafficking.	fitc-ga	78-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25347845-8	2014	Interestingly, cell treatment with Hsp90 inhibitors, including the membrane-impermeable FITC-GA, abolished Rab11-rNadA colocalization but do not interfere with Rab11-TfR colocalization.	fitc-ga	88-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
25202009-11	2014	In contrast, SERT-R607A/I608A and SERT-P601A/G602A were only rendered susceptible to inhibition of HSP70 and HSP90 by concomitant pharmacochaperoning with noribogaine.	noribogaine	155-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
25389454-2	2014	We wanted to compare the effects of the benzoquinone 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) and the novel isoxazole resorcinol-based Hsp90 inhibitor NVP-AUY922 in a panel of pancreatic and colorectal carcinoma cell lines and in colorectal primary cultures derived from tumors excised to patients.	isoxazole resorcinol	129-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
25196717-2	2014	In this work, we describe the use of LLS for competitive binding experiments to measure accurate dissociation constants of fragments that bind weakly to the ATP binding site of the N-terminal ATPase domain of heat shock protein 90 (Hsp90), a therapeutic target for cancer treatment.	lls	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-230
25196717-2	2014	In this work, we describe the use of LLS for competitive binding experiments to measure accurate dissociation constants of fragments that bind weakly to the ATP binding site of the N-terminal ATPase domain of heat shock protein 90 (Hsp90), a therapeutic target for cancer treatment.	lls	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
25196717-2	2014	In this work, we describe the use of LLS for competitive binding experiments to measure accurate dissociation constants of fragments that bind weakly to the ATP binding site of the N-terminal ATPase domain of heat shock protein 90 (Hsp90), a therapeutic target for cancer treatment.	Adenosine Triphosphate	157-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-230
25196717-2	2014	In this work, we describe the use of LLS for competitive binding experiments to measure accurate dissociation constants of fragments that bind weakly to the ATP binding site of the N-terminal ATPase domain of heat shock protein 90 (Hsp90), a therapeutic target for cancer treatment.	Adenosine Triphosphate	157-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
25239533-7	2014	Furthermore, the low expression of HSP90 significantly increased levels of lactic dehydrogenase and malondialdehyde and GR protein expression in the cytoplasm under heat stress (P &lt; 0.01), and significantly decreased nuclear GR protein expression (P &lt; 0.01).	Malondialdehyde	100-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
25239533-8	2014	Heat shock protein 90 was positively correlated with corticosterone and superoxide dismutase activities (P &lt; 0.01), and HSP90 mRNA was negatively correlated with pH after chilling for 24 h. The results demonstrated that HSP90 plays a pivotal role in protecting cells from oxidation.	Corticosterone	53-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
25239533-8	2014	Heat shock protein 90 was positively correlated with corticosterone and superoxide dismutase activities (P &lt; 0.01), and HSP90 mRNA was negatively correlated with pH after chilling for 24 h. The results demonstrated that HSP90 plays a pivotal role in protecting cells from oxidation.	Corticosterone	53-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
24166505-0	2014	HSP-90 inhibitor ganetespib is synergistic with doxorubicin in small cell lung cancer.	STA 9090	17-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-6
25117641-3	2014	Despite preclinical efficacy of geldanamycin-anasamycin (GA)-derivatives containing benzoquinone moiety as Hsp90 inhibitors, the hepatotoxicity of these GA-derivatives restricts their therapeutic benefit.	geldanamycin-anasamycin	32-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
25153785-9	2014	Indeed, we showed that coadministration of the Hsp90 inhibitor 17-demethoxygeldanamycin (17-DMAG) and proteasome inhibitor (velcade) induced ER stress evidenced by increased unfolded protein response markers.	17-demethoxygeldanamycin	63-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
25153785-9	2014	Indeed, we showed that coadministration of the Hsp90 inhibitor 17-demethoxygeldanamycin (17-DMAG) and proteasome inhibitor (velcade) induced ER stress evidenced by increased unfolded protein response markers.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	89-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
25153785-9	2014	Indeed, we showed that coadministration of the Hsp90 inhibitor 17-demethoxygeldanamycin (17-DMAG) and proteasome inhibitor (velcade) induced ER stress evidenced by increased unfolded protein response markers.	Bortezomib	124-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
24954307-0	2014	The effect of celastrol, a triterpene with antitumorigenic activity, on conformational and functional aspects of the human 90kDa heat shock protein Hsp90alpha, a chaperone implicated in the stabilization of the tumor phenotype.	celastrol	14-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-158
24954307-3	2014	RESULTS: In this work, we investigated the effect of celastrol on the conformational and functional aspects of Hsp90alpha.	celastrol	53-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-121
24954307-4	2014	Interestingly, celastrol appeared to target Hsp90alpha directly as the compound induced the oligomerization of the chaperone via the C-terminal domain as demonstrated by experiments using a deletion mutant.	celastrol	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-54
24954307-5	2014	The nature of the oligomers was investigated by biophysical tools demonstrating that a two-fold excess of celastrol induced the formation of a decameric Hsp90alpha bound throughout the C-terminal domain.	celastrol	106-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-163
24954307-8	2014	CONCLUSION: Celastrol interferes with specific biological functions of Hsp90alpha.	celastrol	12-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-81
24954307-9	2014	Our results suggest a model in which celastrol binds directly to the C-terminal domain of Hsp90alpha causing oligomerization.	celastrol	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-100
24954307-11	2014	Therefore celastrol may act primarily by inducing specific oligomerization that affects some, but not all, of the functions of Hsp90alpha.	celastrol	10-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-137
24954307-12	2014	GENERAL SIGNIFICANCE: To the best of our knowledge, this study is the first work to use multiple probes to investigate the effect that celastrol has on the stability and oligomerization of Hsp90alpha and on the binding of this chaperone to Tom70.	celastrol	135-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-199
24954307-13	2014	This work provides a novel mechanism by which celastrol binds Hsp90alpha.	celastrol	46-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-72
25117641-3	2014	Despite preclinical efficacy of geldanamycin-anasamycin (GA)-derivatives containing benzoquinone moiety as Hsp90 inhibitors, the hepatotoxicity of these GA-derivatives restricts their therapeutic benefit.	Gallium	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
25117641-3	2014	Despite preclinical efficacy of geldanamycin-anasamycin (GA)-derivatives containing benzoquinone moiety as Hsp90 inhibitors, the hepatotoxicity of these GA-derivatives restricts their therapeutic benefit.	quinone	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
26461378-0	2014	The role of HSP90 in Quercetin-induced apoptosis in human papillary thyroid (B-CPAP) cancer cells.	Quercetin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
25106706-14	2014	Reactive cysteines within the structure of HSP90 are known to modulate its ATPase-dependent chaperone activity through disulfide formation and S-nitrosylation.	reactive cysteines	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
25106706-14	2014	Reactive cysteines within the structure of HSP90 are known to modulate its ATPase-dependent chaperone activity through disulfide formation and S-nitrosylation.	Disulfides	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
26461378-9	2014	Finally, we used Western blotting to compare HSP90 and Cleaved-PARP levels in cells treated with Quercetin and the control group.	Quercetin	97-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
24976418-0	2014	Glutamine suppresses Hsp72 not Hsp90alpha and is not inducing Th1, Th2, or Th17 cytokine responses in human septic PBMCs.	Glutamine	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-41
24859453-11	2014	Hsp90 inhibition decreased fatty acid synthesis genes via reduced nuclear SREBP-1 and favoured fatty acid oxidation genes via PPARalpha.	Fatty Acids	27-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24859453-11	2014	Hsp90 inhibition decreased fatty acid synthesis genes via reduced nuclear SREBP-1 and favoured fatty acid oxidation genes via PPARalpha.	Fatty Acids	95-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25308700-0	2014	HSP90 inhibitor CH5164840 induces micronuclei in TK6 cells via an aneugenic mechanism.	CH5164840	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25308700-3	2014	We have examined the mode of action of micronucleus formation in TK6 cells by a novel and highly specific HSP90 inhibitor, CH5164840, by means of an in vitro micronucleus test with fluorescence in situ hybridization (FISH), gammaH2AX staining to detect DNA damage, and microscopic observation of chromosomal alignment in mitotic cells.	CH5164840	123-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
25349783-3	2014	It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or beta-naphthoflavone (beta-NF), the AhR dissociates from HSP90 and translocates to the nucleus.	Polychlorinated Dibenzodioxins	96-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
25349783-3	2014	It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or beta-naphthoflavone (beta-NF), the AhR dissociates from HSP90 and translocates to the nucleus.	Polychlorinated Dibenzodioxins	59-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
25161239-8	2014	The novel observations include: previously unknown similarities in the effects induced by 15-delta prostaglandin J2 and HSP90 inhibitors, which are linked to the 3D descriptors of the drugs; and the induction by simvastatin of leukemia-specific response, resembling the effects of corticosteroids.	Simvastatin	212-223	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
25167922-0	2014	A selenosemicarbazone complex with copper efficiently down-regulates the 90-kDa heat shock protein HSP90AA1 and its client proteins in cancer cells.	selenosemicarbazone	2-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-107
25167922-0	2014	A selenosemicarbazone complex with copper efficiently down-regulates the 90-kDa heat shock protein HSP90AA1 and its client proteins in cancer cells.	Copper	35-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-107
25167922-8	2014	Interestingly, although RNA-seq revealed that the transcription of HSP90AA1 was increased in 2-24a/Cu-treated cells, western blotting showed that the expression of HSP90AA1 protein was significantly decreased in these cells.	Copper	99-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-75
25167922-8	2014	Interestingly, although RNA-seq revealed that the transcription of HSP90AA1 was increased in 2-24a/Cu-treated cells, western blotting showed that the expression of HSP90AA1 protein was significantly decreased in these cells.	Copper	99-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-172
25210794-2	2014	The HSP90-inhibitor ganetespib showed benefit in advanced clinical trials.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
25210794-10	2014	When the most ganetespib-resistant cell line, HT29, was treated with ganetespib, the levels of HSP90 clients were unaffected.	STA 9090	69-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
25210794-11	2014	However, HT29 cells became sensitized to the drug, and HSP90 client proteins were destabilized by ganetespib upon siRNA-mediated UGT1A knockdown.	STA 9090	98-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
25202064-1	2014	BACKGROUND/AIM: The aim of the present study was to evaluate the effect of radicicol, an inhibitor of heat shock protein (hsp) 90, alone or in combination with hsp70 inhibition on survival of anaplastic thyroid carcinoma (ATC) cells.	monorden	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-129
25202064-6	2014	CONCLUSION: Our results suggest that radicicol induces cell death mediated through PI3K/Akt signaling with modulation of hsp90 client proteins and hsp70 inhibition enhances radicicol-induced cell death with suppression of survivin in ATC cells.	monorden	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
25059319-0	2014	Phase I dose-escalation study of the HSP90 inhibitor AUY922 in Japanese patients with advanced solid tumors.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	53-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24887036-8	2014	Simvastatin therapy partially reduced HDL inflammation index, improved the capacity of HDL to stimulate eNOS and Akt phosphorylation at S1177, eNOS associated with HSP90, NO production, reduced eNOS phosphorylation at T495 and superoxide generation, and improved endothelium-dependent vasodilation.	Simvastatin	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
25140900-4	2014	The goal of the present work was to investigate if Rose Bengal Acetate (RBAc), a powerful PS able to trigger apoptosis and autophagy, enables photosensitized HeLa cells to expose and/or release pivotal DAMPs, i.e. ATP, HSP70, HSP90, HMGB1, and calreticulin (CRT), that characterize ICD.	Rose Bengal acetate	51-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
25140900-4	2014	The goal of the present work was to investigate if Rose Bengal Acetate (RBAc), a powerful PS able to trigger apoptosis and autophagy, enables photosensitized HeLa cells to expose and/or release pivotal DAMPs, i.e. ATP, HSP70, HSP90, HMGB1, and calreticulin (CRT), that characterize ICD.	Rose Bengal acetate	72-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
25140900-4	2014	The goal of the present work was to investigate if Rose Bengal Acetate (RBAc), a powerful PS able to trigger apoptosis and autophagy, enables photosensitized HeLa cells to expose and/or release pivotal DAMPs, i.e. ATP, HSP70, HSP90, HMGB1, and calreticulin (CRT), that characterize ICD.	Adenosine Triphosphate	214-217	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
24992077-0	2014	Synthesis and antiproliferative activity of novobiocin analogues as potential hsp90 inhibitors.	Novobiocin	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24980703-0	2014	Fragment-based hit discovery and structure-based optimization of aminotriazoloquinazolines as novel Hsp90 inhibitors.	aminotriazoloquinazolines	65-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
24961936-3	2014	In this study, the Hsp90 blocker 17-DMAG inhibited proliferation of activated total B cells and their IgG secretion in cultures of human peripheral B cells from healthy subjects, but IgG production was no longer affected when these activated B cells were allowed to differentiate prior to a deferred application of the inhibitor.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	33-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
25349783-3	2014	It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or beta-naphthoflavone (beta-NF), the AhR dissociates from HSP90 and translocates to the nucleus.	Methylcholanthrene	103-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
25349783-3	2014	It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or beta-naphthoflavone (beta-NF), the AhR dissociates from HSP90 and translocates to the nucleus.	Methylcholanthrene	124-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
25349783-3	2014	It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or beta-naphthoflavone (beta-NF), the AhR dissociates from HSP90 and translocates to the nucleus.	beta-Naphthoflavone	134-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
25349783-9	2014	The ligand 17-DMAG inhibited binding of HSP90 to GST-PAS.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	11-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
24682747-0	2014	The HSP90 inhibitor ganetespib has chemosensitizer and radiosensitizer activity in colorectal cancer.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24682747-3	2014	Here we evaluated the activity of ganetespib, a second-generation HSP90 inhibitor, in models of CRC.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
24682747-9	2014	This demonstration of combinatorial benefit afforded by an HSP90 inhibitor to a standard CRC adjuvant regimen provides an attractive new framework for the potential application of ganetespib as an investigational agent in this disease.	STA 9090	180-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
24934933-5	2014	Here, we report that AR-42 induces NF-kappaB inhibition, disrupts the ability of Hsp90 to stabilize its oncogenic clients, and causes potent and specific cell death of LSCs but not normal hematopoietic stem and progenitor cells.	HDAC-42	21-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
27486036-0	2014	Hybrids of the Benzofuran Core from Natural Products and the 2,4-Dihydroxy-5-isopropylbenzene Fragment as Potent Hsp90 Inhibitors: Design, Synthesis and Bioevaluation.	benzofuran	15-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
27486036-0	2014	Hybrids of the Benzofuran Core from Natural Products and the 2,4-Dihydroxy-5-isopropylbenzene Fragment as Potent Hsp90 Inhibitors: Design, Synthesis and Bioevaluation.	2,4-dihydroxy-5-isopropylbenzene	61-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
27486036-3	2014	In this study, a novel class of hybrids of benzofuran, a privileged core from natural products, and 2,4-dihydroxy-5-isopropyl phenyl, an efficient fragment in Hsp90 inhibitors, were designed and synthesized.	benzofuran	43-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
27486036-3	2014	In this study, a novel class of hybrids of benzofuran, a privileged core from natural products, and 2,4-dihydroxy-5-isopropyl phenyl, an efficient fragment in Hsp90 inhibitors, were designed and synthesized.	2,4-dihydroxy-5-isopropyl phenyl	100-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
27486036-6	2014	The methods reported here may expand the range of known structural types accommodated by the ATP binding site of Hsp90.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
24850175-0	2014	Potent antitumor activity of HSP90 inhibitor AUY922 in adrenocortical carcinoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
24850175-8	2014	AUY922 inhibited the proliferation of ACC cells in a time- and concentration-dependent manner, and increasing apoptosis was observed in tumor cells treated with the HSP90 inhibitor.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
24850175-10	2014	Our data suggest that the specific HSP90 inhibitor AUY922 can play a therapeutic role in treatment of ACC and, thus, HSP90 could qualify as a promising new target in ACC.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	51-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
24850175-10	2014	Our data suggest that the specific HSP90 inhibitor AUY922 can play a therapeutic role in treatment of ACC and, thus, HSP90 could qualify as a promising new target in ACC.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	51-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
24945998-9	2014	CONCLUSIONS: The addition of simvastatin at a dose used in patients with cardiovascular diseases (40-80 mg once daily) may potentiate the anti-angiogenic effects of bevacizumab on CRC by suppressing angiopoietin2, BiP, and Hsp90alpha in cancer cells.	Simvastatin	29-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-233
24879994-0	2014	SNX-25a, a novel Hsp90 inhibitor, inhibited human cancer growth more potently than 17-AAG.	snx-25a	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
25806308-7	2014	The inhibition of the molecular chaperone, HSP90, represents another promising strategy to overcome crizotinib resistance in ALK-rearranged NSCLC.	Crizotinib	100-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
24879994-1	2014	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a typical Hsp90 inhibitor derived from geldanamycin (GA), has entered Phase III clinical trials for cancer therapy.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
24879994-1	2014	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a typical Hsp90 inhibitor derived from geldanamycin (GA), has entered Phase III clinical trials for cancer therapy.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
24879994-1	2014	17-Allylamino-17-demethoxygeldanamycin (17-AAG), a typical Hsp90 inhibitor derived from geldanamycin (GA), has entered Phase III clinical trials for cancer therapy.	geldanamycin	102-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
24879994-3	2014	In this study, the anticancer activity and mechanism of SNX-25a, a novel Hsp90 inhibitor, was investigated comparing with that of 17-AAG.	snx-25a	56-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
24879994-6	2014	Compared with 17-AAG, SNX-25a was more potent in arresting the cell cycle at G2 phase, and displayed more potent effects on human cancer cell apoptosis and Hsp90 client proteins.	snx-25a	22-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
24952482-0	2014	Receptor ligand-triggered resistance to alectinib and its circumvention by Hsp90 inhibition in EML4-ALK lung cancer cells.	alectinib	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
25020117-10	2014	Both hsp90 and caveolin-1 have been shown to influence eNOS uncoupling and a peptide mimicking the scaffolding domain of caveolin-1 blocked the ability of PKCalpha to stimulate eNOS-derived superoxide.	Superoxides	190-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
24874477-11	2014	Heat-shock protein 90-specific inhibitors inhibit EDP-stimulated HT-1080 cell-invasive capacity and restrained EDP-stimulated pro-MMP-2 and uPA secretions.	2-ethyl-3,5-dimethylpyrazine	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
24874477-11	2014	Heat-shock protein 90-specific inhibitors inhibit EDP-stimulated HT-1080 cell-invasive capacity and restrained EDP-stimulated pro-MMP-2 and uPA secretions.	2-ethyl-3,5-dimethylpyrazine	111-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
24903226-2	2014	Vorinostat is a panHDAC inhibitor that sensitizes breast cancer cells to taxanes and trastuzumab by suppressing HDAC6 and Hsp90 client proteins.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
24903226-2	2014	Vorinostat is a panHDAC inhibitor that sensitizes breast cancer cells to taxanes and trastuzumab by suppressing HDAC6 and Hsp90 client proteins.	Taxoids	73-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
24903226-8	2014	Vorinostat increased acetylation of Hsp90 and alpha tubulin, and reduced expression of Hsp90 client proteins and HDAC6 in the primary tumor.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24903226-8	2014	Vorinostat increased acetylation of Hsp90 and alpha tubulin, and reduced expression of Hsp90 client proteins and HDAC6 in the primary tumor.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
24903226-10	2014	Consistent with cell line and xenograft data, vorinostat increased acetylation of Hsp90 and alpha tubulin, and decreased Hsp90 client protein and HDAC6 expression in human breast cancers in vivo.	Vorinostat	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
24903226-10	2014	Consistent with cell line and xenograft data, vorinostat increased acetylation of Hsp90 and alpha tubulin, and decreased Hsp90 client protein and HDAC6 expression in human breast cancers in vivo.	Vorinostat	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
24753447-0	2014	Chiral resolution and pharmacological characterization of the enantiomers of the Hsp90 inhibitor 2-amino-7-[4-fluoro-2-(3-pyridyl)phenyl]-4-methyl-7,8-dihydro-6H-quinazolin-5-one oxime.	2-amino-7-[4-fluoro-2-(3-pyridyl)phenyl]-4-methyl-7,8-dihydro-6h-quinazolin-5-one oxime	97-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
24753447-2	2014	2-Amino-7-[4-fluoro-2-(3-pyridyl)phenyl]-4-methyl-7,8-dihydro-6H-quinazolin-5-one oxime is a racemic Hsp90 inhibitor that targets the N-terminal adenosine triphosphatase site.	2-amino-7-[4-fluoro-2-(3-pyridyl)phenyl]-4-methyl-7,8-dihydro-6h-quinazolin-5-one oxime	0-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
24671949-2	2014	In this paper, we used in vivo fluorescence lifetime imaging with HER2-targeted fluorescent probes as an alternative imaging method to investigate the efficacy of targeted therapy with 17-DMAG (an HSP90 inhibitor) on tumors with high expression of HER2 receptors.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	185-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	197-202
24411988-9	2014	In vitro, OGX-427 synergistically enhanced Hsp90 inhibitor-induced suppression of cell growth and induced apoptosis by 60% as measured by increased sub-G1 fraction and poly(ADP-ribose) polymerase cleavage.	apatorsen	10-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
24411988-11	2014	In vivo, OGX-427 potentiated the anticancer effects of Hsp90 inhibitor PF-04929113 (orally, 25mg/kg) to inhibit tumor growth and prolong survival in CRPC LNCaP xenografts.	apatorsen	9-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
24411988-11	2014	In vivo, OGX-427 potentiated the anticancer effects of Hsp90 inhibitor PF-04929113 (orally, 25mg/kg) to inhibit tumor growth and prolong survival in CRPC LNCaP xenografts.	SNX-5422	71-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
24411988-12	2014	CONCLUSIONS: HSP90 inhibitor-mediated induction of Hsp27 expression can be attenuated by OGX-427, resulting in increased ER stress and apoptosis, and synergistic inhibition of CRPC tumor growth.	apatorsen	89-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
24785461-3	2014	Inhibition of Hsp90alpha by C-Terminal domain (CTD) ATP binding-site blockage might be used as an effective treatment strategy against the disease via degradation of tau proteins that are involved in the progression of the disease.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-24
24785461-4	2014	Till date, a variety of drugs have been identified as Hsp90alpha inhibitors, which include Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone.	Novobiocin	91-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-64
24785461-4	2014	Till date, a variety of drugs have been identified as Hsp90alpha inhibitors, which include Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone.	clorobiocin	103-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-64
24785461-4	2014	Till date, a variety of drugs have been identified as Hsp90alpha inhibitors, which include Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone.	epigallocatechin gallate	116-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-64
24785461-4	2014	Till date, a variety of drugs have been identified as Hsp90alpha inhibitors, which include Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone.	epigallocatechin gallate	141-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-64
24785461-6	2014	HYPOTHESIS: We hypothesize that binding site for ATP of Hsp90alpha CTD contains multiple ATP binding sites.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
24785461-6	2014	HYPOTHESIS: We hypothesize that binding site for ATP of Hsp90alpha CTD contains multiple ATP binding sites.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
24785461-7	2014	We also hypothesize that a drug which can bind to the ATP binding site of CTD strongly can inhibit Hsp90alpha function which is in turn redirects towards the proteasomal degradation of diseased client protein like tau in AD.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-109
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	Novobiocin	82-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	clorobiocin	94-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	epigallocatechin gallate	107-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	epigallocatechin gallate	132-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	Adenosine Triphosphate	183-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	Leucine	216-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	Leucine	225-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-13	2014	Furthermore, docking studies were performed of various Hsp90alpha inhibitors like Novobiocin, Clorobiocin, Epigallocatechingallate (EGCG) and Derrubone with the previously recognized ATP binding residues of CTD i.e. Leu 665, Leu 666 and Leu 694.	Leucine	225-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-65
24785461-16	2014	CONCLUSION: Based on our findings, we propose that the recognized sites i.e. Leu665, Leu 666 and Leu694 could possibly be the binding sites of Hsp90alpha CTD for ATP and the Hsp90 inhibitors.	Leucine	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-153
24785461-16	2014	CONCLUSION: Based on our findings, we propose that the recognized sites i.e. Leu665, Leu 666 and Leu694 could possibly be the binding sites of Hsp90alpha CTD for ATP and the Hsp90 inhibitors.	Adenosine Triphosphate	162-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-153
24784839-3	2014	Here, a selective HSP90 inhibitor, ganetespib, induced loss of FGFR3-TACC3 fusion protein expression and depletion of multiple oncogenic signaling proteins in RT112 bladder cells, resulting in potent cytotoxicity comparable with the pan-FGFR tyrosine kinase inhibitor BGJ398.	STA 9090	35-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
24784839-3	2014	Here, a selective HSP90 inhibitor, ganetespib, induced loss of FGFR3-TACC3 fusion protein expression and depletion of multiple oncogenic signaling proteins in RT112 bladder cells, resulting in potent cytotoxicity comparable with the pan-FGFR tyrosine kinase inhibitor BGJ398.	infigratinib	268-274	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
24784839-6	2014	Interestingly, two additional FGFR3 fusion-positive lines (RT4 and SW480) retained sensitivity to HSP90 inhibitor treatment by the ansamycins 17-AAG and 17-DMAG yet displayed intrinsic resistance to ganetespib or AUY922, both second-generation resorcinol-based compounds.	Lactams, Macrocyclic	131-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
24784839-6	2014	Interestingly, two additional FGFR3 fusion-positive lines (RT4 and SW480) retained sensitivity to HSP90 inhibitor treatment by the ansamycins 17-AAG and 17-DMAG yet displayed intrinsic resistance to ganetespib or AUY922, both second-generation resorcinol-based compounds.	tanespimycin	142-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
24784839-6	2014	Interestingly, two additional FGFR3 fusion-positive lines (RT4 and SW480) retained sensitivity to HSP90 inhibitor treatment by the ansamycins 17-AAG and 17-DMAG yet displayed intrinsic resistance to ganetespib or AUY922, both second-generation resorcinol-based compounds.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	153-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
24784839-9	2014	Furthermore, UDP-glucuronosyltransferase enzyme expression may serve as a predictive factor for clinical response to resorcinol-based HSP90 inhibitors.	resorcinol	117-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
24959709-3	2014	Our results showed that Hsp90 is required at a very early stage of viral replication and Hsp90 inhibitor Geldanamycin (GA) can abrogate new virus particle formation more effectively in the case of S 27 than that of DRDE-06.	geldanamycin	105-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
24959709-3	2014	Our results showed that Hsp90 is required at a very early stage of viral replication and Hsp90 inhibitor Geldanamycin (GA) can abrogate new virus particle formation more effectively in the case of S 27 than that of DRDE-06.	geldanamycin	119-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
24927996-9	2014	CONCLUSIONS: As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.	conglobatin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
24927996-9	2014	CONCLUSIONS: As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.	conglobatin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24927996-9	2014	CONCLUSIONS: As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.	conglobatin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24927996-9	2014	CONCLUSIONS: As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.	conglobatin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24927996-9	2014	CONCLUSIONS: As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.	conglobatin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24835034-9	2014	This study also revealed that short-term exposure of tumour cells with ONO4140 is sufficient to inhibit the catalytic activity of Hsp90, evaluated through disruption of Hsp90-p23 association by immunoprecipitation.	ONO4140	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
24835034-9	2014	This study also revealed that short-term exposure of tumour cells with ONO4140 is sufficient to inhibit the catalytic activity of Hsp90, evaluated through disruption of Hsp90-p23 association by immunoprecipitation.	ONO4140	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
24835034-11	2014	The study also reveals that apoptosis following Hsp90 inhibition with ONO4140 occurs via Caspase9-Caspase3 intrinsic apoptotic pathway, a process that is likely triggered by inactivation of Akt.	ONO4140	70-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
24789751-10	2014	Furthermore, the miR-27a mimic oligonucleotide suppressed the elevation of the expression of Hsp90 and Hsp110 in HSC-4 cells, suggesting that these HSPs may be involved in a mechanism of thermal resistance.	Oligonucleotides	31-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
24705874-0	2014	Anticancer effects of the Hsp90 inhibitor 17-demethoxy-reblastatin in human breast cancer MDA-MB-231 cells.	17-demethoxy-reblastatin	42-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
24705874-3	2014	17-Demethoxy-reblastatin (17-DR), a novel nonbenzoquinone- type geldanamycin analog, exhibited potent Hsp90 ATPase inhibition activity.	17-demethoxy-reblastatin	0-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
24705874-3	2014	17-Demethoxy-reblastatin (17-DR), a novel nonbenzoquinone- type geldanamycin analog, exhibited potent Hsp90 ATPase inhibition activity.	17-dr	26-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
24760959-5	2014	LC-MRM analysis showed HSP90 inhibition to be associated with decreased expression of multiple receptor tyrosine kinases, modules in the PI3K/AKT/mammalian target of rapamycin pathway, and the MAPK/CDK4 signaling axis in NRAS mutant melanoma cell lines and the inhibition of PI3K/AKT signaling in BRAF mutant melanoma xenografts with acquired vemurafenib resistance.	Vemurafenib	343-354	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24947016-3	2014	Many molecular machines, like Hsp90, work far from equilibrium by utilizing the energy of ATP hydrolysis.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
24947016-7	2014	This reveals a previously undescribed mechanism on how cochaperones can modify Hsp90, namely by strengthening of the coupling between ATP hydrolysis and a kinetic step involved in the Hsp90 system resulting in a stronger directionality.	Adenosine Triphosphate	134-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
24947016-7	2014	This reveals a previously undescribed mechanism on how cochaperones can modify Hsp90, namely by strengthening of the coupling between ATP hydrolysis and a kinetic step involved in the Hsp90 system resulting in a stronger directionality.	Adenosine Triphosphate	134-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
24949977-4	2014	Full recovery of ligand binding requires ATP hydrolysis on Hsp90 and the Hop and p23 cochaperones.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
24949977-5	2014	Surprisingly, Hsp90 ATP hydrolysis appears to regulate client transfer from Hsp70, likely through a coupling of the two chaperone"s ATP cycles.	Adenosine Triphosphate	20-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
24949977-5	2014	Surprisingly, Hsp90 ATP hydrolysis appears to regulate client transfer from Hsp70, likely through a coupling of the two chaperone"s ATP cycles.	Adenosine Triphosphate	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
24927938-2	2014	In this regard, we examined the efficacy of combination treatment with the widely-used genotoxic drug doxorubicin and the mitochondriotoxic Hsp90 inhibitor gamitrinib to exploit disparate stress signaling pathways for cancer therapy.	Gamitrinib	156-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
24927996-0	2014	FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation.	phenylalanyltryptophan	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
24927996-0	2014	FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation.	phenylalanyltryptophan	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
24927996-4	2014	RESULTS: We have verified the direct binding of FW-04-806 to the N-terminal domain of Hsp90 and found that FW-04-806 inhibits Hsp90/cell division cycle protein 37 (Cdc37) chaperone/co-chaperone interactions, but does not affect ATP-binding capability of Hsp90, thereby leading to the degradation of multiple Hsp90 client proteins via the proteasome pathway.	Adenosine Triphosphate	228-231	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
24927996-4	2014	RESULTS: We have verified the direct binding of FW-04-806 to the N-terminal domain of Hsp90 and found that FW-04-806 inhibits Hsp90/cell division cycle protein 37 (Cdc37) chaperone/co-chaperone interactions, but does not affect ATP-binding capability of Hsp90, thereby leading to the degradation of multiple Hsp90 client proteins via the proteasome pathway.	Adenosine Triphosphate	228-231	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
24927996-4	2014	RESULTS: We have verified the direct binding of FW-04-806 to the N-terminal domain of Hsp90 and found that FW-04-806 inhibits Hsp90/cell division cycle protein 37 (Cdc37) chaperone/co-chaperone interactions, but does not affect ATP-binding capability of Hsp90, thereby leading to the degradation of multiple Hsp90 client proteins via the proteasome pathway.	Adenosine Triphosphate	228-231	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
24927996-4	2014	RESULTS: We have verified the direct binding of FW-04-806 to the N-terminal domain of Hsp90 and found that FW-04-806 inhibits Hsp90/cell division cycle protein 37 (Cdc37) chaperone/co-chaperone interactions, but does not affect ATP-binding capability of Hsp90, thereby leading to the degradation of multiple Hsp90 client proteins via the proteasome pathway.	Adenosine Triphosphate	228-231	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
24726918-2	2014	ATP-dependent client activation by Hsp90 is tightly regulated by a host of co-chaperone proteins that control progression through the activation cycle.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
24726919-7	2014	Moreover, native-state hydrogen exchange indicates that Hsp90 can also interact with partially folded states only transiently populated from within a thermodynamically stable, native-state ensemble.	Hydrogen	23-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
25988145-10	2014	The cochaperones Sba1 was found previously in the crystal structure bound to the ATP hydrolysis-competent conformation of Hsp90, which did not allow to distinguish the mode of Sba1-mediated inhibition of Hsp90"s ATPase activity by stabilizing the pre- or post-hydrolysis step.	Adenosine Triphosphate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
25988145-11	2014	Our HX-MS experiments now show that Sba1 binding leads to a protection of the ATP binding lid, suggesting that it inhibits Hsp90"s ATPase activity by slowing down product release.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
24618845-9	2014	Combined treatments with heat shock, HSP90 inhibition by 17-AAG, proteasome inhibition by bortezomib, or DNA-damaging agents did not result in significant synergistic effects.	tanespimycin	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24512858-1	2014	BACKGROUND: Ganetespib is a small molecule, nongeldanamycin HSP90 inhibitor with potent inhibitory effects on HSP90-dependent oncoproteins of relevance to breast cancer pathogenesis.	STA 9090	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
24736433-1	2014	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (Hsp90), is a ligand-activated transcription factor that plays a role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	152-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
24736433-1	2014	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (Hsp90), is a ligand-activated transcription factor that plays a role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	152-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
24736433-1	2014	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (Hsp90), is a ligand-activated transcription factor that plays a role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	185-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
24736433-1	2014	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (Hsp90), is a ligand-activated transcription factor that plays a role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	185-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
25594042-3	2014	The HSP90 inhibitor, 17AAG, has shown promise against various solid tumors, including prostate cancer (PC).	tanespimycin	21-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24512858-1	2014	BACKGROUND: Ganetespib is a small molecule, nongeldanamycin HSP90 inhibitor with potent inhibitory effects on HSP90-dependent oncoproteins of relevance to breast cancer pathogenesis.	STA 9090	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
24512858-1	2014	BACKGROUND: Ganetespib is a small molecule, nongeldanamycin HSP90 inhibitor with potent inhibitory effects on HSP90-dependent oncoproteins of relevance to breast cancer pathogenesis.	nongeldanamycin	44-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
24512858-1	2014	BACKGROUND: Ganetespib is a small molecule, nongeldanamycin HSP90 inhibitor with potent inhibitory effects on HSP90-dependent oncoproteins of relevance to breast cancer pathogenesis.	nongeldanamycin	44-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
24512858-14	2014	Ganetespib was well tolerated and responses in more targeted populations harboring specific HSP90-dependent oncoproteins justifies its further study, particularly as part of rational combinations.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
24789511-0	2014	Hsp90 inhibition by WK88-1 potently suppresses the growth of gefitinib-resistant H1975 cells harboring the T790M mutation in EGFR.	Gefitinib	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24682466-1	2014	UNLABELLED: The benzoquinone ansamycins (BQAs) are a valuable class of antitumor agents that serve as inhibitors of heat shock protein (Hsp)-90.	benzoquinone ansamycins	16-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-143
24682466-1	2014	UNLABELLED: The benzoquinone ansamycins (BQAs) are a valuable class of antitumor agents that serve as inhibitors of heat shock protein (Hsp)-90.	bqas	41-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-143
24682466-8	2014	19-Phenyl BQAs inhibited purified Hsp90 in a NAD(P)H: quinone oxidoreductase 1 (NQO1)-dependent manner, demonstrating increased efficacy of the hydroquinone ansamycin relative to its parent quinone.	19-phenyl bqas	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24682466-8	2014	19-Phenyl BQAs inhibited purified Hsp90 in a NAD(P)H: quinone oxidoreductase 1 (NQO1)-dependent manner, demonstrating increased efficacy of the hydroquinone ansamycin relative to its parent quinone.	hydroquinone ansamycin	144-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24682466-8	2014	19-Phenyl BQAs inhibited purified Hsp90 in a NAD(P)H: quinone oxidoreductase 1 (NQO1)-dependent manner, demonstrating increased efficacy of the hydroquinone ansamycin relative to its parent quinone.	quinone	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24682466-9	2014	Molecular modeling supported increased stability of the hydroquinone form of 19-phenyl-DMAG in the active site of human Hsp90.	hydroquinone	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
24682466-9	2014	Molecular modeling supported increased stability of the hydroquinone form of 19-phenyl-DMAG in the active site of human Hsp90.	19-phenyl-dmag	77-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
24718854-3	2014	The expression of HSP90 and the anticancer effect of the HSP90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin (17-AAG) coupled with cisplatin, docetaxel, or gemcitabine were examined using immunohistochemistry, quantitative real-time PCR, cell growth, flow cytometry, immunoblots and caspase-3/7 assays.	tanespimycin	73-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
24789511-5	2014	Our data revealed that inhibition of Hsp90 by WK88-1 induced overall degradation of multiple oncogenic signaling molecules including EGFR, ErbB2 and ErbB3, leading to subsequent growth arrest and apoptosis in the gefitinib-resistant H1975 cell line.	Gefitinib	213-222	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24733395-0	2014	Nitric oxide and heat shock protein 90 activate soluble guanylate cyclase by driving rapid change in its subunit interactions and heme content.	Heme	130-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-38
24874742-3	2014	In a previous report, we have identified heat shock protein 90 (Hsp90) as a critical modulator of the balance between autophagy and apoptosis in selenite-treated leukemia cells.	Selenious Acid	145-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
24874742-3	2014	In a previous report, we have identified heat shock protein 90 (Hsp90) as a critical modulator of the balance between autophagy and apoptosis in selenite-treated leukemia cells.	Selenious Acid	145-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
24733395-2	2014	hsp90 associates with the heme-free (apo) sGC-beta1 subunit and helps to drive heme insertion during maturation of sGC to its NO-responsive active form.	Heme	26-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24733395-2	2014	hsp90 associates with the heme-free (apo) sGC-beta1 subunit and helps to drive heme insertion during maturation of sGC to its NO-responsive active form.	Heme	79-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24733395-5	2014	Thus, NO promoted a rapid, transient, and hsp90-dependent heme insertion into the apo-sGC-beta1 subpopulation in cells, which enabled it to combine with the sGC-alpha1 subunit to form the mature enzyme.	Heme	58-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
24733395-7	2014	Such dynamic interplay between hsp90, apo-sGC-beta1, and sGC-alpha1 in response to NO is unprecedented and represent new steps by which cells can modulate the heme content and activity of sGC for signaling cascades.	Heme	159-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
24852575-7	2014	Interestingly, following 1 or 6 h of MeHg exposure, Hsp90 binding to PGES/p23 or nNOS was significantly increased, resulting in increased prostaglandin E2 (PGE2) synthesis from MeHg-treated astrocytes.	Dinoprostone	138-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
24885082-7	2014	Combination therapy of nutlin-3 and Hsp90 inhibitor geldanamycin demonstrated synergistic induction of apoptosis in AML cell lines and primary AML cells.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24852575-7	2014	Interestingly, following 1 or 6 h of MeHg exposure, Hsp90 binding to PGES/p23 or nNOS was significantly increased, resulting in increased prostaglandin E2 (PGE2) synthesis from MeHg-treated astrocytes.	Dinoprostone	156-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
24852575-7	2014	Interestingly, following 1 or 6 h of MeHg exposure, Hsp90 binding to PGES/p23 or nNOS was significantly increased, resulting in increased prostaglandin E2 (PGE2) synthesis from MeHg-treated astrocytes.	mehg	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
24852575-8	2014	These effects were attenuated by the Hsp90 antagonist, geldanmycin.	geldanmycin	55-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24745965-0	2014	Towards the discovery of drug-like epigallocatechin gallate analogs as Hsp90 inhibitors.	epigallocatechin gallate	35-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
24745965-8	2014	Selected analogs in this series are more potent than EGCG in a luciferase refolding assay for Hsp90 activity.	epigallocatechin gallate	53-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
24886060-2	2014	The heat shock protein 90 (HSP90) inhibitor 17-N-allylamino-17-demethoxygeldanamycin (17-AAG) has previously been proposed as a possible candidate drug.	tanespimycin	44-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
24886060-2	2014	The heat shock protein 90 (HSP90) inhibitor 17-N-allylamino-17-demethoxygeldanamycin (17-AAG) has previously been proposed as a possible candidate drug.	tanespimycin	44-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
24796583-6	2014	The combination of the HSP90 inhibitor NVP-AUY922 and the PI3K/mTOR inhibitor NVP-BEZ235 was synergistic in inducing cell death in CCA cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
25050163-4	2014	We describe the synthesis and biological evaluation of a new hsp90 inhibitor, SM253.	SM253	78-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
24810052-5	2014	Our studies indicate that celastrol promotes proteotoxic stress, supported by two feedback mechanisms: (i) impairment of protein quality control as revealed by accumulation of polyubiquitinated aggregates and the canonical autophagy substrate, p62, and (ii) the induction of heat-shock proteins, HSP72 and HSP90.	celastrol	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	306-311
24810052-9	2014	This study further emphasizes that targeting proteotoxic stress responses by inhibiting HSP90 with 17-N-Allylamino-17-demethoxygeldanamycin sensitizes human glioblastoma to celastrol treatment, thereby serving as a novel synergism to overcome drug resistance.	tanespimycin	99-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
24810052-9	2014	This study further emphasizes that targeting proteotoxic stress responses by inhibiting HSP90 with 17-N-Allylamino-17-demethoxygeldanamycin sensitizes human glioblastoma to celastrol treatment, thereby serving as a novel synergism to overcome drug resistance.	celastrol	173-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
24760825-5	2014	Through a focused siRNA screen of 28 Cullin-RING ligase family members, we found that CUL5 and RBX2 were required for degradation of several HSP90 clients upon treatment of human cancer cells with the clinical HSP90 inhibitor 17-AAG.	tanespimycin	226-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
24760825-5	2014	Through a focused siRNA screen of 28 Cullin-RING ligase family members, we found that CUL5 and RBX2 were required for degradation of several HSP90 clients upon treatment of human cancer cells with the clinical HSP90 inhibitor 17-AAG.	tanespimycin	226-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-215
24303801-3	2014	We investigated the mechanisms of hsp90 inhibition by 17-N-allylamino-17-demethoxygeldanamycin (17-AAG) on NF-kappaB activation by LPS in primary human lung microvascular endothelial cells.	tanespimycin	54-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24887242-1	2014	BACKGROUND: Novobiocin is a coumarin antibiotic, which affects also eukaryotic cells inhibiting activity of Heat shock protein 90 (Hsp90).	Novobiocin	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-129
24887242-1	2014	BACKGROUND: Novobiocin is a coumarin antibiotic, which affects also eukaryotic cells inhibiting activity of Heat shock protein 90 (Hsp90).	Novobiocin	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
24887242-1	2014	BACKGROUND: Novobiocin is a coumarin antibiotic, which affects also eukaryotic cells inhibiting activity of Heat shock protein 90 (Hsp90).	coumarin	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-129
24887242-1	2014	BACKGROUND: Novobiocin is a coumarin antibiotic, which affects also eukaryotic cells inhibiting activity of Heat shock protein 90 (Hsp90).	coumarin	28-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
24690674-0	2014	Synthesis of potential allosteric modulators of Hsp90 by chemical glycosylation of Eupomatenoid-6.	eupomatenoid	83-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
24690674-12	2014	The glycosides obtained are currently under investigation as modulators of Hsp90 chaperone activity.	Glycosides	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
24669860-3	2014	In fact, since the initial serendipitous discovery that geldanamycin (GM) inhibits HSP90, the field has rapidly moved from proof-of-concept clinical studies with GM derivatives to novel second-generation inhibitors.	geldanamycin	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
24669860-3	2014	In fact, since the initial serendipitous discovery that geldanamycin (GM) inhibits HSP90, the field has rapidly moved from proof-of-concept clinical studies with GM derivatives to novel second-generation inhibitors.	geldanamycin	70-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
24676905-11	2014	In addition, 17-AAD, an inhibitor of HSP90, exerts a potent synergistic effect on NSCLC proliferation with VER-155008.	17-aad	13-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24676905-11	2014	In addition, 17-AAD, an inhibitor of HSP90, exerts a potent synergistic effect on NSCLC proliferation with VER-155008.	VER 155008	107-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24742089-5	2014	EXPERT OPINION: For Hsp90, there has been considerable creativity in the discovery of novel pharmacophores that fall outside the three initially discovered scaffolds (i.e., ansamycins, resorcinols and purines).	Resorcinols	185-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
24798692-4	2014	Analysis of publicly available gene expression data showed that exposure of HR-proficient breast cancer cell lines to HSP90i 17-AAG(17-allylamino-17-demethoxygeldanamycin) downregulated HR, ATM and Fanconi Anemia pathways.	tanespimycin	132-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
24483157-3	2014	HSP90 is a molecular target for the HIV protease inhibitor nelfinavir (NFV).	Nelfinavir	59-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24742089-5	2014	EXPERT OPINION: For Hsp90, there has been considerable creativity in the discovery of novel pharmacophores that fall outside the three initially discovered scaffolds (i.e., ansamycins, resorcinols and purines).	Purines	201-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
24664541-5	2014	OLA-NO2 decreased protein expression of eNOS and caveolin-1 (Cav-1) but increased heat shock protein 90 (Hsp90) expression.	ola-no2	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-103
24664541-5	2014	OLA-NO2 decreased protein expression of eNOS and caveolin-1 (Cav-1) but increased heat shock protein 90 (Hsp90) expression.	ola-no2	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
24664541-6	2014	Immunoprecipitation analysis confirmed that OLA-NO2 replaced eNOS/Cav-1 with eNOS/Hsp90 interaction, resulting in increasing eNOS activity.	ola-no2	44-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
24664541-9	2014	Collectively, these results substantiate a new functional role for nitrated fatty acid, demonstrating that OLA-NO2 exerts vascular protective effects by increasing NO bioavailability through eNOS phosphorylation/dephosphorylation and interaction with associated proteins such as Hsp90 and Cav-1.	nitrated fatty acid	67-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	279-284
24664541-9	2014	Collectively, these results substantiate a new functional role for nitrated fatty acid, demonstrating that OLA-NO2 exerts vascular protective effects by increasing NO bioavailability through eNOS phosphorylation/dephosphorylation and interaction with associated proteins such as Hsp90 and Cav-1.	ola-no2	107-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	279-284
24502926-6	2014	BKT140 induced apoptotic cell death, decreasing the levels of HSP70 and HSP90 chaperones and antiapoptotic proteins BCL-2 and BCL-XL, subsequently promoting the release of mitochondrial factors cytochrome c and SMAC/Diablo.	BKT140	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24706778-3	2014	Here we report that specific inhibitors of Hsp90 such as 17-(N-allylamino)-17-demethoxygeldanamycin and AUY922 prevent HIV-1 reactivation in CD4+ T cells.	tanespimycin	57-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
24554781-3	2014	To overcome this limitation, a clinically feasible method was sought to block HSP synthesis induced by the potent HSP90 inhibitor ganetespib.	STA 9090	130-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
24191862-0	2014	Metabolite elucidation of the Hsp90 inhibitor SNX-2112 using ultraperformance liquid chromatography/quadrupole time-of-flight mass spectrometry (UPLC-QTOF/MS).	SNX 2112	46-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
23506739-8	2014	SDS-PAGE results showed that there was substantial diversity in 90 kDa proteins in the frozen-thawed sperm and HSP90 was confirmed as one of the 90 kDa proteins by western blot.	Sodium Dodecyl Sulfate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
24785146-5	2014	We introduce a novel impermeant Hsp90 inhibitor STA-12-7191 derived from ganetespib and show that it is markedly less toxic to cells and can inhibit cancer cell migration in a dose dependent manner.	sta-12	48-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
24785146-5	2014	We introduce a novel impermeant Hsp90 inhibitor STA-12-7191 derived from ganetespib and show that it is markedly less toxic to cells and can inhibit cancer cell migration in a dose dependent manner.	STA 9090	73-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
24760083-5	2014	Mutation of these residues to alanine caused a significant decrease in the melting temperature according to differential scanning fluorimetry experiments, indicating a reduced stability of the mutant hHsp90 complexes.	Alanine	30-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-206
24660900-1	2014	Heat shock protein 90 (Hsp90) is a highly conserved ATP-driven machine involved in client protein maturation, folding, and activation.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
24660900-1	2014	Heat shock protein 90 (Hsp90) is a highly conserved ATP-driven machine involved in client protein maturation, folding, and activation.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24660900-6	2014	We observe that the Caenorhabditis elegans Sgt1 homologue D1054.3 binds to Hsp90 in the absence of nucleotides but much stronger in the presence of ATP and ATPgammaS.	Adenosine Triphosphate	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
24660900-7	2014	The latter binding mode is similar to p23, another CS-domain containing Hsp90 cofactor, even though binding is not observable for p23 in the absence of nucleotides.	Cesium	51-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24706778-3	2014	Here we report that specific inhibitors of Hsp90 such as 17-(N-allylamino)-17-demethoxygeldanamycin and AUY922 prevent HIV-1 reactivation in CD4+ T cells.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
24565573-0	2014	4,5,6,7-Tetrahydro-isoxazolo-[4,5-c]-pyridines as a new class of cytotoxic Hsp90 inhibitors.	4,5,6,7-tetrahydro-isoxazolo-[4,5-c]-pyridines	0-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
24706829-10	2014	We found that the heat shock protein 90 (Hsp90) inhibitor ganetespib induced degradation of these variants whereas others lacking a partial TAPE domain were resistant in both overexpression models and patient-derived cell lines.	STA 9090	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
24706829-10	2014	We found that the heat shock protein 90 (Hsp90) inhibitor ganetespib induced degradation of these variants whereas others lacking a partial TAPE domain were resistant in both overexpression models and patient-derived cell lines.	STA 9090	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
24565573-6	2014	Moreover, a derivative bearing a hydroxamic acid residue bound to C-3 amide portion was found to inhibit both Hsp90 and HDAC6.	Hydroxamic Acids	33-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
24565573-6	2014	Moreover, a derivative bearing a hydroxamic acid residue bound to C-3 amide portion was found to inhibit both Hsp90 and HDAC6.	Amides	70-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
24535459-3	2014	We show here that HOP has ATP-binding activity comparable to that of HSP70/HSP90, and that HOP slowly hydrolyzes ATP.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
24567332-3	2014	Critical to these interactions are TPR domains that target co-chaperone binding to the EEVD-COOH motif that terminates Hsp70/Hsp90.	Carbonic Acid	92-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
24694060-3	2014	FINDINGS: Using anti-CD3 antibody-stimulated human peripheral blood mononuclear cell cultures, we observed that Hsp90 inhibition by non-toxic concentrations of the geldanamycin derivative 17-DMAG significantly blocked T cell proliferation, reduced IFN-gamma and IL-17 expression on CD4+ T lymphocytes, and arrested secretion of proinflammatory IFN-gamma, TNF-alpha, and IL-17, cytokines characteristic of Th1 and Th17 cells, respectively.	geldanamycin	164-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
24694060-3	2014	FINDINGS: Using anti-CD3 antibody-stimulated human peripheral blood mononuclear cell cultures, we observed that Hsp90 inhibition by non-toxic concentrations of the geldanamycin derivative 17-DMAG significantly blocked T cell proliferation, reduced IFN-gamma and IL-17 expression on CD4+ T lymphocytes, and arrested secretion of proinflammatory IFN-gamma, TNF-alpha, and IL-17, cytokines characteristic of Th1 and Th17 cells, respectively.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	188-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
24265268-3	2014	We found that IP-FCM could effectively detect HSP70, p23, Cdc37, and Cdk6 components in the HSP90 complex naturally formed in U937 cells when this complex was captured by anti-HSP90 antibody-coated polystyrene microspheres.	Polystyrenes	198-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
24265268-3	2014	We found that IP-FCM could effectively detect HSP70, p23, Cdc37, and Cdk6 components in the HSP90 complex naturally formed in U937 cells when this complex was captured by anti-HSP90 antibody-coated polystyrene microspheres.	Polystyrenes	198-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
24265268-5	2014	In a cell-free environment, IP-FCM could detect the direct effects of ATP and/or HSP90 inhibitors (17-N-allylamino-17-demethoxygeldanamycin or celastrol) in causing component dissociation and the time- and dose-effects of inhibitor-caused dissociation.	ip-fcm	28-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
24265268-5	2014	In a cell-free environment, IP-FCM could detect the direct effects of ATP and/or HSP90 inhibitors (17-N-allylamino-17-demethoxygeldanamycin or celastrol) in causing component dissociation and the time- and dose-effects of inhibitor-caused dissociation.	tanespimycin	99-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
24407159-4	2014	The combination treatment with JSI-124 and bortezomib resulted in the highest expression of heat shock protein (HSP) 90 and the lowest expression of p-STAT3 in dying myeloma cells.	cucurbitacin I	31-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-119
24265268-5	2014	In a cell-free environment, IP-FCM could detect the direct effects of ATP and/or HSP90 inhibitors (17-N-allylamino-17-demethoxygeldanamycin or celastrol) in causing component dissociation and the time- and dose-effects of inhibitor-caused dissociation.	celastrol	143-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
24530475-0	2014	Down-regulation of MSH2 expression by an Hsp90 inhibitor enhances pemetrexed-induced cytotoxicity in human non-small-cell lung cancer cells.	Pemetrexed	66-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
24530475-7	2014	Combining the drug treatment with an Hsp90 inhibitor resulted in an enhanced pemetrexed-induced cytotoxic effect, accompanied with the reduction of MSH2 protein and mRNA levels.	Pemetrexed	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24258787-5	2014	On the contrary, low concentrations of melatonin turn on the production of anti-apoptotic heat shock proteins: HSP27, HSP70, and HSP90, which prevents the activation of caspase-3.	Melatonin	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
24682203-3	2014	Heat shock protein 90 (HSP90), an adenosine triphosphate (ATP)-dependent molecular chaperone, has important functions in many cellular regulatory pathways by controlling the activity and stability of its various client proteins.	Adenosine Triphosphate	34-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
24682203-3	2014	Heat shock protein 90 (HSP90), an adenosine triphosphate (ATP)-dependent molecular chaperone, has important functions in many cellular regulatory pathways by controlling the activity and stability of its various client proteins.	Adenosine Triphosphate	34-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24682203-3	2014	Heat shock protein 90 (HSP90), an adenosine triphosphate (ATP)-dependent molecular chaperone, has important functions in many cellular regulatory pathways by controlling the activity and stability of its various client proteins.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
24682203-3	2014	Heat shock protein 90 (HSP90), an adenosine triphosphate (ATP)-dependent molecular chaperone, has important functions in many cellular regulatory pathways by controlling the activity and stability of its various client proteins.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24407159-4	2014	The combination treatment with JSI-124 and bortezomib resulted in the highest expression of heat shock protein (HSP) 90 and the lowest expression of p-STAT3 in dying myeloma cells.	Bortezomib	43-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-119
24407159-8	2014	The data suggest that pretreatment of myeloma cells with JSI-124 and bortezomib can recover DC function through the up-regulation of HSP90 and the down-regulation of p-STAT3 and inhibitory cytokines, and that these DCs can potently generate myeloma-specific CTLs.	cucurbitacin I	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
24407159-8	2014	The data suggest that pretreatment of myeloma cells with JSI-124 and bortezomib can recover DC function through the up-regulation of HSP90 and the down-regulation of p-STAT3 and inhibitory cytokines, and that these DCs can potently generate myeloma-specific CTLs.	Bortezomib	69-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
27485776-0	2014	Discovery and Bioevaluation of Novel Pyrazolopyrimidine Analogs as Competitive Hsp90 Inhibitors Through Shape-Based Similarity Screening.	1H-pyrazolo[4,3-d]pyrimidine	37-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
27485776-2	2014	Many Hsp90 inhibitors such as BIIB021 and CUDC-305 have been in clinical.	CUDC 305	42-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
27485776-3	2014	In this paper shape-based similarity screening through ROCS overlays on the basis of CUDC-305, BIIB021, PU-H71 and PU-3 were performed to discover HSP90 inhibitors.	CUDC 305	85-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
27485776-4	2014	A set of 19 novel pyrazolopyrimidine analogues was identified and evaluated on enzyme level and cell-based level as Hsp90 inhibitors.	1H-pyrazolo[4,3-d]pyrimidine	18-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
27485776-5	2014	The compound HDI4-04 with IC50 0.35 microM in the Hsp90 ATP hydrolysis assay exhibited potent cytotoxicity against five human cancer cell lines.	Adenosine Triphosphate	56-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
24555544-4	2014	The mixed LB/SB protocol was applied to virtually screen potential Hsp90 inhibitors from the NCI Diversity Set composed of 1785 compounds.	lb	10-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
24435554-6	2014	Corresponding mutants of Galpha13 exhibited robust SRE activation, suggesting a Galpha12-specific mechanism, and inhibition of Hsp90 by geldanamycin or small interfering RNA-mediated lowering of Hsp90 levels resulted in greater downregulation of Galpha12 than Galpha13 signaling in SRE activation experiments.	geldanamycin	136-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
24293393-6	2014	Here, we showed that 17-DMAG, a well-known HSP-90 inhibitor, significantly inhibits NB cell growth, arrests cell cycle, and strongly induces NB cell apoptosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-49
24582562-0	2014	The Hsp90 inhibitor SNX-2112 induces apoptosis of human hepatocellular carcinoma cells: the role of ER stress.	SNX 2112	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24582562-2	2014	SNX-2112 is an Hsp90 inhibitor showing broad antitumor activity.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
24582562-8	2014	We found that SNX-2112 showed stronger inhibition on cell growth than 17-AAG, a classical Hsp90 inhibitor.	SNX 2112	14-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
24582562-8	2014	We found that SNX-2112 showed stronger inhibition on cell growth than 17-AAG, a classical Hsp90 inhibitor.	tanespimycin	70-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
24470592-7	2014	Combination therapy with the heat shock protein 90 (HSP90) inhibitor PU-H71 and ruxolitinib reduced total and phospho-JAK2 and achieved more potent inhibition of downstream signaling than ruxolitinib monotherapy.	ruxolitinib	80-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
24470592-7	2014	Combination therapy with the heat shock protein 90 (HSP90) inhibitor PU-H71 and ruxolitinib reduced total and phospho-JAK2 and achieved more potent inhibition of downstream signaling than ruxolitinib monotherapy.	ruxolitinib	80-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
24470592-7	2014	Combination therapy with the heat shock protein 90 (HSP90) inhibitor PU-H71 and ruxolitinib reduced total and phospho-JAK2 and achieved more potent inhibition of downstream signaling than ruxolitinib monotherapy.	ruxolitinib	188-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
24470592-7	2014	Combination therapy with the heat shock protein 90 (HSP90) inhibitor PU-H71 and ruxolitinib reduced total and phospho-JAK2 and achieved more potent inhibition of downstream signaling than ruxolitinib monotherapy.	ruxolitinib	188-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
24580531-4	2014	We found that the ATP-binding pocket has a Pf-specific extension, whose sequence lining is identical in human Hsp90 but which differs by tertiary structure and dynamics.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
24580531-5	2014	Using these insights for a structure-based drug screen, we discovered novel 7-azaindole compounds that exclusively bind the recombinant N-terminal domain of PfHsp90 but not of human Hsp90 nor of a PfHsp90 mutant with "human-like" dynamics.	7-azaindole dimer	76-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
24588105-0	2014	Synthesis and evaluation of new Hsp90 inhibitors based on a 1,4,5-trisubstituted 1,2,3-triazole scaffold.	1,4,5-trisubstituted 1,2,3-triazole	60-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
24588105-1	2014	Ruthenium catalyzed 1,3-cycloaddition (click chemistry) of an azido moiety installed on dihydroxycumene scaffold with differently substituted aryl propiolates gave a new family of 1,4,5-trisubstituted triazole carboxylic acid derivatives that showed high affinity toward Hsp90 associated with cell proliferation inhibition, both in nanomolar range.	Ruthenium	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
24588105-1	2014	Ruthenium catalyzed 1,3-cycloaddition (click chemistry) of an azido moiety installed on dihydroxycumene scaffold with differently substituted aryl propiolates gave a new family of 1,4,5-trisubstituted triazole carboxylic acid derivatives that showed high affinity toward Hsp90 associated with cell proliferation inhibition, both in nanomolar range.	3',5-diazido-2',3'-dideoxyuridine	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
24588105-1	2014	Ruthenium catalyzed 1,3-cycloaddition (click chemistry) of an azido moiety installed on dihydroxycumene scaffold with differently substituted aryl propiolates gave a new family of 1,4,5-trisubstituted triazole carboxylic acid derivatives that showed high affinity toward Hsp90 associated with cell proliferation inhibition, both in nanomolar range.	dihydroxycumene	88-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
24588105-1	2014	Ruthenium catalyzed 1,3-cycloaddition (click chemistry) of an azido moiety installed on dihydroxycumene scaffold with differently substituted aryl propiolates gave a new family of 1,4,5-trisubstituted triazole carboxylic acid derivatives that showed high affinity toward Hsp90 associated with cell proliferation inhibition, both in nanomolar range.	aryl propiolates	142-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
24588105-1	2014	Ruthenium catalyzed 1,3-cycloaddition (click chemistry) of an azido moiety installed on dihydroxycumene scaffold with differently substituted aryl propiolates gave a new family of 1,4,5-trisubstituted triazole carboxylic acid derivatives that showed high affinity toward Hsp90 associated with cell proliferation inhibition, both in nanomolar range.	1,4,5-trisubstituted triazole carboxylic acid	180-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	271-276
24588105-3	2014	Docking simulations suggested that the triazoles penetrate the Hsp90 ATP binding site.	Triazoles	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
24588105-3	2014	Docking simulations suggested that the triazoles penetrate the Hsp90 ATP binding site.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
24588105-5	2014	In vitro metabolic stability and in vivo preliminary studies on selected compounds have shown promising results comparable to the potent Hsp90 inhibitor NVP-AUY922.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	157-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
24658058-6	2014	Moreover, the glucose analog 2-DG and the Hsp90 inhibitor 17-AAG, which destabilizes the HIF-1alpha protein, synergized with IMQ to induce tumor cell apoptosis in vitro and significantly inhibited tumor growth in vivo.	tanespimycin	58-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
24658058-6	2014	Moreover, the glucose analog 2-DG and the Hsp90 inhibitor 17-AAG, which destabilizes the HIF-1alpha protein, synergized with IMQ to induce tumor cell apoptosis in vitro and significantly inhibited tumor growth in vivo.	Imiquimod	125-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
24447628-12	2014	Dobutamine induced DNA-binding of HSF-1 and mRNA-expression of hsp70 and hsp90.	Dobutamine	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
24618430-6	2014	A heat shock protein 90 (HSP90) inhibitor (ganetespib) showed modest effects but was well tolerated making it available for use with conventional chemotherapy (Abstract #297).	STA 9090	43-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	2-23
24618430-6	2014	A heat shock protein 90 (HSP90) inhibitor (ganetespib) showed modest effects but was well tolerated making it available for use with conventional chemotherapy (Abstract #297).	STA 9090	43-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
24451373-10	2014	Pharmacologic intervention with CP-31398, a p53 rescue agent, inhibited recruitment of Aha1 to Hsp90 and suppressed Wnt-mediated gene expression in colon cancer cells.	CP 31398	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
24608665-5	2014	The ability of DBC2 to bind GTP was modulated by the Hsp90 ATPase cycle, as demonstrated through the use of the Hsp90 chemical inhibitors, geldanamycin and molybdate.	Guanosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
24608665-5	2014	The ability of DBC2 to bind GTP was modulated by the Hsp90 ATPase cycle, as demonstrated through the use of the Hsp90 chemical inhibitors, geldanamycin and molybdate.	Guanosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
24608665-5	2014	The ability of DBC2 to bind GTP was modulated by the Hsp90 ATPase cycle, as demonstrated through the use of the Hsp90 chemical inhibitors, geldanamycin and molybdate.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
24608665-5	2014	The ability of DBC2 to bind GTP was modulated by the Hsp90 ATPase cycle, as demonstrated through the use of the Hsp90 chemical inhibitors, geldanamycin and molybdate.	molybdate	156-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
24556722-5	2014	This review focuses on the preclinical activity profile of ganetespib, a potent small-molecule inhibitor of HSP90, the characterization of which has provided important frameworks for the optimal design and application of HSP90 inhibitor-based strategies in a variety of cancer types.	STA 9090	59-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
24556722-5	2014	This review focuses on the preclinical activity profile of ganetespib, a potent small-molecule inhibitor of HSP90, the characterization of which has provided important frameworks for the optimal design and application of HSP90 inhibitor-based strategies in a variety of cancer types.	STA 9090	59-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	221-226
24556722-6	2014	Beyond client protein-driven tumors, ganetespib can also potentiate the effects of other molecularly targeted and standard-of-care therapeutics while simultaneously overcoming drug resistance in multiple tumor types, thereby positioning this compound as the leading HSP90 inhibitor currently under clinical development.	STA 9090	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	266-271
23686707-0	2014	Targeted inhibition of Hsp90 by ganetespib is effective across a broad spectrum of breast cancer subtypes.	STA 9090	32-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24296245-9	2014	We observed that NAC pretreatment upregulated heat-shock protein 90 (Hsp90) expression and increased the interaction of Hsp90 with HIF-1alpha in ischemic brains.	Acetylcysteine	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
24296245-9	2014	We observed that NAC pretreatment upregulated heat-shock protein 90 (Hsp90) expression and increased the interaction of Hsp90 with HIF-1alpha in ischemic brains.	Acetylcysteine	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
24296245-9	2014	We observed that NAC pretreatment upregulated heat-shock protein 90 (Hsp90) expression and increased the interaction of Hsp90 with HIF-1alpha in ischemic brains.	Acetylcysteine	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
24296245-11	2014	Moreover, Hsp90 inhibition attenuated NAC-induced HIF-1alpha protein accumulation and diminished NAC-induced neuroprotection in the MCAO model.	Acetylcysteine	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
24296245-11	2014	Moreover, Hsp90 inhibition attenuated NAC-induced HIF-1alpha protein accumulation and diminished NAC-induced neuroprotection in the MCAO model.	Acetylcysteine	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
24366006-0	2014	Radiosensitization of human lung cancer cells by the novel purine-scaffold Hsp90 inhibitor, PU-H71.	purine	59-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
24366006-0	2014	Radiosensitization of human lung cancer cells by the novel purine-scaffold Hsp90 inhibitor, PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	92-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
24366006-2	2014	PU-H71 is a purine-scaffold Hsp90 inhibitor with less toxicity in normal cells than in cancer cells.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
24366006-2	2014	PU-H71 is a purine-scaffold Hsp90 inhibitor with less toxicity in normal cells than in cancer cells.	purine	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
24415765-1	2014	In eukaryotes, heat shock protein 90 (Hsp90) is an essential ATP-dependent molecular chaperone that associates with numerous client proteins.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36
24415765-1	2014	In eukaryotes, heat shock protein 90 (Hsp90) is an essential ATP-dependent molecular chaperone that associates with numerous client proteins.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
24556685-10	2014	Accordingly, S100A2-deficient cells are more sensitive to the HSP-90 inhibitor, 17-N-allylamino-17-demethoxygeldanamycin, potentially representing a novel therapeutic strategy for S100A2- and BRCA1-deficient cancers.	tanespimycin	80-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-68
24461493-0	2014	Synthesis and biological evaluation of coumarin replacements of novobiocin as Hsp90 inhibitors.	coumarin	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24461493-0	2014	Synthesis and biological evaluation of coumarin replacements of novobiocin as Hsp90 inhibitors.	Novobiocin	64-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24461493-2	2014	In an effort to develop more efficacious compounds for Hsp90 inhibition, novobiocin analogues were prepared by replacing the central coumarin core with naphthalene, quinolinone, and quinoline surrogates.	Novobiocin	73-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
24524692-0	2014	Geldanamycin-mediated inhibition of heat shock protein 90 partially activates dendritic cells, but interferes with their full maturation, accompanied by impaired upregulation of RelB.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-57
24524692-4	2014	METHODS: Unstimulated human monocyte-derived DCs (MO-DCs) were treated with the prototypical HSP90 inhibitor geldanamycin (GA).	geldanamycin	109-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
24524692-5	2014	Based on dose titration studies performed to assess cytotoxic effects, GA was applied at a rather low concentration, comparable to serum levels of clinically used HSP90 inhibitors.	geldanamycin	71-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
24490822-10	2014	METHODS: We inhibit the function of HSP90 with two inhibitors, geldanamycin (GA) and 17- allylamono-demethoxygeldanamycin (17-AAG), and down-regulated the expression of endogenous HSP90 with specific small-interfering RNAs (siRNAs).	geldanamycin	63-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24490822-10	2014	METHODS: We inhibit the function of HSP90 with two inhibitors, geldanamycin (GA) and 17- allylamono-demethoxygeldanamycin (17-AAG), and down-regulated the expression of endogenous HSP90 with specific small-interfering RNAs (siRNAs).	geldanamycin	77-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24490822-10	2014	METHODS: We inhibit the function of HSP90 with two inhibitors, geldanamycin (GA) and 17- allylamono-demethoxygeldanamycin (17-AAG), and down-regulated the expression of endogenous HSP90 with specific small-interfering RNAs (siRNAs).	geldanamycin	77-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
24490822-10	2014	METHODS: We inhibit the function of HSP90 with two inhibitors, geldanamycin (GA) and 17- allylamono-demethoxygeldanamycin (17-AAG), and down-regulated the expression of endogenous HSP90 with specific small-interfering RNAs (siRNAs).	17- allylamono-demethoxygeldanamycin	85-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24490822-10	2014	METHODS: We inhibit the function of HSP90 with two inhibitors, geldanamycin (GA) and 17- allylamono-demethoxygeldanamycin (17-AAG), and down-regulated the expression of endogenous HSP90 with specific small-interfering RNAs (siRNAs).	tanespimycin	123-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24490822-10	2014	METHODS: We inhibit the function of HSP90 with two inhibitors, geldanamycin (GA) and 17- allylamono-demethoxygeldanamycin (17-AAG), and down-regulated the expression of endogenous HSP90 with specific small-interfering RNAs (siRNAs).	tanespimycin	123-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
24493589-7	2014	Our findings define a novel cooperative mechanism in which a GPCR (DP1) promotes the activity of the enzyme (L-PGDS) that produces its agonist (PGD2) and in which this enzyme in turn acts as a cofactor (of Hsp90) to promote export and agonist-dependent activity of the receptor.	Prostaglandin D2	144-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
24286867-6	2014	Thus, we studied the role of Hsp90 activity in a well established model of cultured hippocampal neurons using an Hsp90 specific inhibitor, 17-AAG.	tanespimycin	139-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
24286867-8	2014	Hsp90 inhibition during the first 3h in culture promotes multiple axon morphology, while this inhibition after 3h slows down axonal elongation.	Tritium	34-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24291777-4	2014	We report a mechanism by which HSF1 activation diminishes the effect of Hsp90 inhibitors geldanamycin and 17-allylaminogeldanamycin (17-AAG, tanespimycin).	geldanamycin	89-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24291777-4	2014	We report a mechanism by which HSF1 activation diminishes the effect of Hsp90 inhibitors geldanamycin and 17-allylaminogeldanamycin (17-AAG, tanespimycin).	tanespimycin	106-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24291777-4	2014	We report a mechanism by which HSF1 activation diminishes the effect of Hsp90 inhibitors geldanamycin and 17-allylaminogeldanamycin (17-AAG, tanespimycin).	tanespimycin	133-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24291777-4	2014	We report a mechanism by which HSF1 activation diminishes the effect of Hsp90 inhibitors geldanamycin and 17-allylaminogeldanamycin (17-AAG, tanespimycin).	tanespimycin	141-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
23686707-2	2014	Here we undertook a comprehensive evaluation of the activity of ganetespib, a selective Hsp90 inhibitor, in this malignancy.	STA 9090	64-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
23686707-8	2014	Thus, ganetespib potently inhibits Hsp90 leading to the degradation of multiple clinically-validated oncogenic client proteins in breast cancer cells, encompassing the broad spectrum of molecularly-defined subtypes.	STA 9090	6-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
23887853-0	2014	Structure-activity relationship (SAR) of withanolides to inhibit Hsp90 for its activity in pancreatic cancer cells.	Withanolides	41-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
23887853-1	2014	Withaferin A (WA), a naturally occurring steroidal lactone, directly binds to Hsp90 and leads to the degradation of Hsp90 client protein.	withaferin A	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
23887853-1	2014	Withaferin A (WA), a naturally occurring steroidal lactone, directly binds to Hsp90 and leads to the degradation of Hsp90 client protein.	withaferin A	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
23887853-1	2014	Withaferin A (WA), a naturally occurring steroidal lactone, directly binds to Hsp90 and leads to the degradation of Hsp90 client protein.	Lactones	51-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
23887853-2	2014	The purpose of this study is to investigate the structure activity relationship (SAR) of withanolides for their inhibition of Hsp90 and anti-proliferative activities in pancreatic cancer cells.	Withanolides	89-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
23887853-7	2014	SAR study suggested that the C-5(6)-epoxy functional group contributes considerably for withanolide to bind to Hsp90, inhibit Hsp90 chaperone activity, and result in Hsp90 client protein depletion.	Withanolides	88-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
23887853-7	2014	SAR study suggested that the C-5(6)-epoxy functional group contributes considerably for withanolide to bind to Hsp90, inhibit Hsp90 chaperone activity, and result in Hsp90 client protein depletion.	Withanolides	88-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
23887853-7	2014	SAR study suggested that the C-5(6)-epoxy functional group contributes considerably for withanolide to bind to Hsp90, inhibit Hsp90 chaperone activity, and result in Hsp90 client protein depletion.	Withanolides	88-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
23887853-8	2014	Meanwhile, the hydroxyl group at C-4 of ring A may enhance withanolide to inhibit Hsp90 activity and disrupt Hsp90-Cdc37 interaction.	Withanolides	59-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23887853-8	2014	Meanwhile, the hydroxyl group at C-4 of ring A may enhance withanolide to inhibit Hsp90 activity and disrupt Hsp90-Cdc37 interaction.	Withanolides	59-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
24252723-0	2014	HPLC method development, validation and impurity characterization for an antitumor Hsp90 inhibitor-PU-H71 (NSC 750424).	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	99-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
24100579-6	2014	Here for the first time we compare three recently-identified HSP70 inhibitors, PES-Cl, MKT-077, and Ver-155008, for their ability to impact some of the known and reported functions of this chaperone; specifically, the ability to inhibit autophagy, to influence the level of HSP90 client proteins, to induce cell cycle arrest, and to inhibit the enzymatic activity of the anaphase-promoting complex/cyclosome (APC/C).	pes-cl	79-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	274-279
24398428-0	2014	Overcoming acquired BRAF inhibitor resistance in melanoma via targeted inhibition of Hsp90 with ganetespib.	STA 9090	96-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
24398428-3	2014	Here, we examined the activity of ganetespib, a small-molecule inhibitor of Hsp90, in melanoma lines harboring the BRAF(V600E) mutation.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
24398428-5	2014	Dual targeting of Hsp90 and BRAF(V600E) provided combinatorial benefit in vemurafenib-sensitive melanoma cells in vitro and in vivo.	Vemurafenib	74-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
24171710-4	2014	This study aims to evaluate the effect of leflunomide on HSPN adults with nephrotic proteinuria.	Leflunomide	42-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-61
24171710-11	2014	CONCLUSION: Leflunomide combined with steroids is effective for treating adult HSPN with nephrotic proteinuria.	Leflunomide	12-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-83
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
24317439-0	2014	The HSP90 inhibitor 17-N-allylamino-17-demethoxy geldanamycin (17-AAG) synergizes with cisplatin and induces apoptosis in cisplatin-resistant esophageal squamous cell carcinoma cell lines via the Akt/XIAP pathway.	tanespimycin	20-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24317439-0	2014	The HSP90 inhibitor 17-N-allylamino-17-demethoxy geldanamycin (17-AAG) synergizes with cisplatin and induces apoptosis in cisplatin-resistant esophageal squamous cell carcinoma cell lines via the Akt/XIAP pathway.	Cisplatin	87-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24317439-0	2014	The HSP90 inhibitor 17-N-allylamino-17-demethoxy geldanamycin (17-AAG) synergizes with cisplatin and induces apoptosis in cisplatin-resistant esophageal squamous cell carcinoma cell lines via the Akt/XIAP pathway.	Cisplatin	122-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24317439-4	2014	In the present study, we evaluated the synergistic effects of combining CDDP with the HSP90 inhibitor 17-N-allylamino-17-demethoxy geldanamycin (17-AAG) on two CDDP-resistant human esophageal squamous cancer cell lines, KYSE30 and KYSE150.	tanespimycin	102-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
24317439-4	2014	In the present study, we evaluated the synergistic effects of combining CDDP with the HSP90 inhibitor 17-N-allylamino-17-demethoxy geldanamycin (17-AAG) on two CDDP-resistant human esophageal squamous cancer cell lines, KYSE30 and KYSE150.	Cisplatin	160-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
24317439-10	2014	Combination therapy with CDDP and an HSP90 inhibitor may represent a promising strategy to overcome CDDP resistance in ESCC.	Cisplatin	100-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
24369839-0	2014	Design and synthesis of 2-amino-6-(1H,3H-benzo[de]isochromen-6-yl)-1,3,5-triazines as novel Hsp90 inhibitors.	2-amino-6-(1h,3h-benzo[de]isochromen-6-yl)-1,3,5-triazines	24-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
24462205-0	2014	Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.	Adenosine Triphosphate	56-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-18
24462205-2	2014	Hsp90"s function is coupled to ATP binding and hydrolysis and requires a series of conformational changes that are regulated by cochaperones and numerous posttranslational modifications (PTMs).	Adenosine Triphosphate	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24462205-4	2014	Here, we show that asymmetric SUMOylation of a conserved lysine residue in the N domain of both yeast (K178) and human (K191) Hsp90 facilitates both recruitment of the adenosine triphosphatase (ATPase)-activating cochaperone Aha1 and, unexpectedly, the binding of Hsp90 inhibitors, suggesting that these drugs associate preferentially with Hsp90 proteins that are actively engaged in the chaperone cycle.	Lysine	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
24462205-4	2014	Here, we show that asymmetric SUMOylation of a conserved lysine residue in the N domain of both yeast (K178) and human (K191) Hsp90 facilitates both recruitment of the adenosine triphosphatase (ATPase)-activating cochaperone Aha1 and, unexpectedly, the binding of Hsp90 inhibitors, suggesting that these drugs associate preferentially with Hsp90 proteins that are actively engaged in the chaperone cycle.	Lysine	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	264-269
24462205-4	2014	Here, we show that asymmetric SUMOylation of a conserved lysine residue in the N domain of both yeast (K178) and human (K191) Hsp90 facilitates both recruitment of the adenosine triphosphatase (ATPase)-activating cochaperone Aha1 and, unexpectedly, the binding of Hsp90 inhibitors, suggesting that these drugs associate preferentially with Hsp90 proteins that are actively engaged in the chaperone cycle.	Lysine	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	264-269
24462206-0	2014	Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.	Adenosine Triphosphate	92-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
24465863-9	2014	Although still limited by potential toxicity, Hsp90 inhibitors tested herein demonstrate oral efficacy and possible beneficial effects on dopamine production in a vertebrate model of parkinsonism that warrant further study.	Dopamine	138-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
24466147-10	2014	We have found that cochaperone-induced conformational changes in Hsp90 may be determined by specific interaction networks that can inhibit or promote progression of the ATPase cycle and thus control the recruitment of client proteins.	cochaperone	19-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
24097863-1	2014	PURPOSE: BIIB021 is the first oral, synthetic, non-geldanamycin-based HSP90 inhibitor that showed activity in preclinical models at low nanomolar concentrations.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
24161787-0	2014	Andrographolide downregulates the v-Src and Bcr-Abl oncoproteins and induces Hsp90 cleavage in the ROS-dependent suppression of cancer malignancy.	andrographolide	0-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
24161787-0	2014	Andrographolide downregulates the v-Src and Bcr-Abl oncoproteins and induces Hsp90 cleavage in the ROS-dependent suppression of cancer malignancy.	ros	99-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
24161787-3	2014	In the present study, we demonstrated the involvement of Hsp90 in the andrographolide-mediated inhibition of Src oncogenic activity.	andrographolide	70-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
24161787-4	2014	Using a proteomics approach, a cleavage fragment of Hsp90alpha was identified in andrographolide-treated cells.	andrographolide	81-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-62
24161787-6	2014	In cancer cells, the induction of Hsp90 cleavage by andrographolide and its structural derivatives correlated well with decreased Src levels, the suppression of transformation, and the induction of apoptosis.	andrographolide	52-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24161787-7	2014	Moreover, the andrographolide-induced Hsp90 cleavage, Src degradation, inhibition of transformation, and induction of apoptosis were abolished by a ROS inhibitor, N-acetyl-cysteine.	andrographolide	14-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
24161787-7	2014	Moreover, the andrographolide-induced Hsp90 cleavage, Src degradation, inhibition of transformation, and induction of apoptosis were abolished by a ROS inhibitor, N-acetyl-cysteine.	ros	148-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
24161787-7	2014	Moreover, the andrographolide-induced Hsp90 cleavage, Src degradation, inhibition of transformation, and induction of apoptosis were abolished by a ROS inhibitor, N-acetyl-cysteine.	Acetylcysteine	163-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
24161787-8	2014	Notably, Hsp90 cleavage, decreased levels of Bcr-Abl (another known Hsp90 client protein), and the induction of apoptosis were also observed in human K562 leukemia cells treated with andrographolide or its active derivatives.	andrographolide	183-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
24161787-8	2014	Notably, Hsp90 cleavage, decreased levels of Bcr-Abl (another known Hsp90 client protein), and the induction of apoptosis were also observed in human K562 leukemia cells treated with andrographolide or its active derivatives.	andrographolide	183-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
24161787-9	2014	Together, we demonstrated a novel mechanism by which andrographolide suppressed cancer malignancy that involved inhibiting Hsp90 function and reducing the levels of Hsp90 client proteins.	andrographolide	53-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
24161787-9	2014	Together, we demonstrated a novel mechanism by which andrographolide suppressed cancer malignancy that involved inhibiting Hsp90 function and reducing the levels of Hsp90 client proteins.	andrographolide	53-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
24173541-0	2014	Preclinical activity profile and therapeutic efficacy of the HSP90 inhibitor ganetespib in triple-negative breast cancer.	STA 9090	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
24173541-2	2014	Here, we undertook a comprehensive evaluation of the activity of ganetespib, a potent inhibitor of HSP90, in this malignancy.	STA 9090	65-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
24369839-1	2014	A novel series of 2-amino-1,3,5-triazines bearing a tricyclic moiety as heat shock protein 90 (Hsp90) inhibitors is described.	2-amino-1,3,5-triazines	18-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-93
24369839-1	2014	A novel series of 2-amino-1,3,5-triazines bearing a tricyclic moiety as heat shock protein 90 (Hsp90) inhibitors is described.	2-amino-1,3,5-triazines	18-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
24369839-2	2014	Molecular design was performed using X-ray cocrystal structures of the lead compound CH5015765 and natural Hsp90 inhibitor geldanamycin with Hsp90.	geldanamycin	123-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
24369839-2	2014	Molecular design was performed using X-ray cocrystal structures of the lead compound CH5015765 and natural Hsp90 inhibitor geldanamycin with Hsp90.	geldanamycin	123-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
24418474-0	2014	Enhanced cytotoxic effect of radiation and temozolomide in malignant glioma cells: targeting PI3K-AKT-mTOR signaling, HSP90 and histone deacetylases.	Temozolomide	43-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
24418474-6	2014	Treatment with a dual inhibitor of Class I PI3K/mTOR, PI103; a HSP90 inhibitor, 17-DMAG; or a HDAC inhibitor, LBH589, further increased the cytotoxic effect of radiation therapy plus TMZ in U251 cells than in T98G cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	80-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
24322890-0	2014	Sulphoxythiocarbamates modify cysteine residues in HSP90 causing degradation of client proteins and inhibition of cancer cell proliferation.	sulphoxythiocarbamates	0-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
24322890-0	2014	Sulphoxythiocarbamates modify cysteine residues in HSP90 causing degradation of client proteins and inhibition of cancer cell proliferation.	Cysteine	30-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
24322890-4	2014	This study aimed to test the hypothesis that targeting cysteine residues of HSP90 will lead to degradation of client proteins and inhibition of cancer cell proliferation.	Cysteine	55-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
24322890-7	2014	RESULTS: The mildly electrophilic sulphoxythiocarbamate alkyne (STCA) selectively targets cysteine residues of HSP90, forming stable thiocarbamate adducts.	sulphoxythiocarbamate alkyne	34-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
24322890-7	2014	RESULTS: The mildly electrophilic sulphoxythiocarbamate alkyne (STCA) selectively targets cysteine residues of HSP90, forming stable thiocarbamate adducts.	SODIUM TRICHLOROACETATE	64-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
24322890-7	2014	RESULTS: The mildly electrophilic sulphoxythiocarbamate alkyne (STCA) selectively targets cysteine residues of HSP90, forming stable thiocarbamate adducts.	Cysteine	90-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
24322890-7	2014	RESULTS: The mildly electrophilic sulphoxythiocarbamate alkyne (STCA) selectively targets cysteine residues of HSP90, forming stable thiocarbamate adducts.	Thiocarbamates	42-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
24322890-11	2014	CONCLUSION: By virtue of their cysteine reactivity, sulphoxythiocarbamates target HSP90, causing destabilisation of its client oncoproteins and inhibiting cell proliferation.	Cysteine	31-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
24351928-4	2014	Celastrol interfered with the establishment of the heat-shock protein 90/Hsp90 cochaperone Cdc37/Hsp90-Hsp70-organizing protein chaperone complex with mutant GCase and reduced heat-shock protein 90-associated protein degradation.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
24360559-4	2014	We define the unique molecular profile of a compound (SM145) that regulates hormone receptor protein levels through hsp90 inhibition without inducing the heat shock response.	sm145	54-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
24351928-4	2014	Celastrol interfered with the establishment of the heat-shock protein 90/Hsp90 cochaperone Cdc37/Hsp90-Hsp70-organizing protein chaperone complex with mutant GCase and reduced heat-shock protein 90-associated protein degradation.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
24952196-6	2014	Our mass-spectrometry data and subsequent biochemical validation shows that Thiostrepton (and MG-132 proteasome inhibitor) trigger upregulation of heat shock proteins HspA1A, Hsp70, Hsp90alpha, or Hsp105 in various human cancer cells.	Thiostrepton	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-192
23972231-6	2014	RhoA nitration and activity were increased by LPS in HLMVECs and suppressed when pretreated with the Hsp90 inhibitor, 17-allylamino-17 demethoxy-geldanamycin (17-AAG).	tanespimycin	118-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
23972231-6	2014	RhoA nitration and activity were increased by LPS in HLMVECs and suppressed when pretreated with the Hsp90 inhibitor, 17-allylamino-17 demethoxy-geldanamycin (17-AAG).	tanespimycin	159-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
23972231-9	2014	MLC phosphorylation induced by constitutively active RhoA was also suppressed by 17-AAG, suggesting a role for Hsp90 downstream of RhoA.	tanespimycin	81-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
25227788-0	2014	Hsp90 inhibitor geldanamycin enhances the antitumor efficacy of enediyne lidamycin in association with reduced DNA damage repair.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25227788-0	2014	Hsp90 inhibitor geldanamycin enhances the antitumor efficacy of enediyne lidamycin in association with reduced DNA damage repair.	enediyne lidamycin	64-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
25227788-2	2014	To investigate the potentiation of antitumor efficacy of lidamycin (LDM), an enediyne agent by the Hsp90 inhibitor geldanamycin (GDM), and possible mechanisms, we have determined effects on ovarian cancer SKOV- 3, hepatoma Bel-7402 and HepG2 cells by MTT assay, apoptosis assay, and cell cycle analysis.	C 1027	57-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
25227799-2	2014	Geldanamycin derivative 17 allylamino-17-demethoxygeldanamycin (17-AAG) inhibits the function and expression of HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
25227799-2	2014	Geldanamycin derivative 17 allylamino-17-demethoxygeldanamycin (17-AAG) inhibits the function and expression of HSP90.	tanespimycin	24-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
25227799-8	2014	The level of Hsp90 gene expression in cells treated with beta-cyclodextrin- 17AAG complex was lower than that of cells treated with free 17AAG (P=0.001).	beta-cyclodextrin- 17aag	57-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
25227799-8	2014	The level of Hsp90 gene expression in cells treated with beta-cyclodextrin- 17AAG complex was lower than that of cells treated with free 17AAG (P=0.001).	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
25227799-9	2014	CONCLUSIONS: The results demonstrated that beta-cyclodextrin- 17AAG complexes are more effective than free 17AAG in down-regulating HSP90 expression due to enhanced beta-cyclodextrin-17AAG uptake by cells.	betadex	43-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
25227799-9	2014	CONCLUSIONS: The results demonstrated that beta-cyclodextrin- 17AAG complexes are more effective than free 17AAG in down-regulating HSP90 expression due to enhanced beta-cyclodextrin-17AAG uptake by cells.	tanespimycin	62-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
25227799-9	2014	CONCLUSIONS: The results demonstrated that beta-cyclodextrin- 17AAG complexes are more effective than free 17AAG in down-regulating HSP90 expression due to enhanced beta-cyclodextrin-17AAG uptake by cells.	betadex	165-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
25227799-9	2014	CONCLUSIONS: The results demonstrated that beta-cyclodextrin- 17AAG complexes are more effective than free 17AAG in down-regulating HSP90 expression due to enhanced beta-cyclodextrin-17AAG uptake by cells.	tanespimycin	107-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
25374192-0	2014	Comparison of inhibitory effect of 17-DMAG nanoparticles and free 17-DMAG in HSP90 gene expression in lung cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	35-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	2-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	2-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-214
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
25374192-0	2014	Comparison of inhibitory effect of 17-DMAG nanoparticles and free 17-DMAG in HSP90 gene expression in lung cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	66-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
25374192-12	2014	CONCLUSIONS: The results demonstrated that PLGA-PEG-17DMAG complexes can be more effective than free 17DMAG in down-regulating of hsp90 expression by enhancing uptake by cells.	Polyethylene Glycols	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
25374192-12	2014	CONCLUSIONS: The results demonstrated that PLGA-PEG-17DMAG complexes can be more effective than free 17DMAG in down-regulating of hsp90 expression by enhancing uptake by cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	52-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
25374192-12	2014	CONCLUSIONS: The results demonstrated that PLGA-PEG-17DMAG complexes can be more effective than free 17DMAG in down-regulating of hsp90 expression by enhancing uptake by cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	101-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
24120917-6	2014	DHA not only displaced several raft-associated onco-proteins, including EGFR, Hsp90, Akt, and Src, from the rafts but also decreased total levels of those proteins via multiple pathways, including the proteasomal and lysosomal pathways, thereby decreasing their activities.	dehydroacetic acid	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
24120917-7	2014	Hsp90 overexpression maintained its client proteins, EGFR and Akt, and attenuated DHA-induced cell death.	dehydroacetic acid	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24120917-9	2014	All these data indicate that the anti-proliferative effect of DHA is mediated by targeting of lipid rafts via decreasing cell surface lipid rafts by their internalization, thereby decreasing raft-associated onco-proteins via proteasomal and lysosomal pathways and decreasing Hsp90 chaperone function.	dehydroacetic acid	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	275-280
25243120-4	2014	We show that chronic exposure of cells to rapamycin can inhibit mTORC2 pathway, and AKT will be destabilized by administration of the HSP90 inhibitor 17-allylamino-geldanamycin (17-AAG).	tanespimycin	150-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
25243120-4	2014	We show that chronic exposure of cells to rapamycin can inhibit mTORC2 pathway, and AKT will be destabilized by administration of the HSP90 inhibitor 17-allylamino-geldanamycin (17-AAG).	tanespimycin	178-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
24345447-0	2014	Discovery of hybrid Hsp90 inhibitors and their anti-neoplastic effects against gefitinib-resistant non-small cell lung cancer (NSCLC).	Gefitinib	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-214
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-214
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-214
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	141-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
24117238-5	2014	A threonine residue set, Thr(115)/Thr(425)/Thr(603), of Hsp90alpha is specifically phosphorylated by PKCgamma, and, more interestingly, this threonine residue set serves as a "phosphorylation switch" for Hsp90alpha binding or release of PKCgamma.	Threonine	141-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-214
24117238-6	2014	Moreover, phosphorylation of Hsp90alpha by PKCgamma decreases the binding affinity of Hsp90alpha towards ATP and co-chaperones such as Cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-39
24117238-6	2014	Moreover, phosphorylation of Hsp90alpha by PKCgamma decreases the binding affinity of Hsp90alpha towards ATP and co-chaperones such as Cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-96
24925400-9	2014	Release of heat shock protein 90 (HSP-90) from endothelial cells can convert prekallikrein to kallikrein (stoichiometrically) within the prekallikrein-HK complex, even in the absence of factor XII, and the prekallikrein-HK complex can autoactivate to generate kallikrein if phosphate is the buffering ion.	Phosphates	274-283	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-32
24925400-9	2014	Release of heat shock protein 90 (HSP-90) from endothelial cells can convert prekallikrein to kallikrein (stoichiometrically) within the prekallikrein-HK complex, even in the absence of factor XII, and the prekallikrein-HK complex can autoactivate to generate kallikrein if phosphate is the buffering ion.	Phosphates	274-283	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-40
25219422-0	2014	Antiproliferative effect of HSP90 inhibitor Y306zh against pancreatic cancer is mediated by interruption of AKT and MAPK signaling pathways.	y306zh	44-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
25219422-7	2014	RESULTS: Y306zh binds tightly to the NH2-terminus of HSP90 with an IC50 of 85 nM, and this causes ATP incapable to attach to the same binding site, and disrupts HSP90-p23 association.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
25219422-11	2014	CONCLUSIONS: Y306zh, a novel HSP90 inhibitor, interrupts ATP binding to HSP90 and disrupts HSP90-p23 interaction, and eventually inhibits the growth of PC cells.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
25219422-11	2014	CONCLUSIONS: Y306zh, a novel HSP90 inhibitor, interrupts ATP binding to HSP90 and disrupts HSP90-p23 interaction, and eventually inhibits the growth of PC cells.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
25219422-11	2014	CONCLUSIONS: Y306zh, a novel HSP90 inhibitor, interrupts ATP binding to HSP90 and disrupts HSP90-p23 interaction, and eventually inhibits the growth of PC cells.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24758428-1	2014	(+)-Lentiginosine, a natural trans-1,2-dihydroxyindolizidine belonging to the class of iminosugars, is a potent inhibitor of amyloglucosidase, and a good inhibitor of Hsp90.	lentiginosine	0-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
24126359-1	2014	The purpose of this study is to assess the impact of human epidermal growth factor receptor 2 (HER2) status on the antitumor activity of CH5164840, an orally available heat shock protein 90 (HSP90) inhibitor, using pharmacokinetic-pharmacodynamic modeling.	CH5164840	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-189
24126359-1	2014	The purpose of this study is to assess the impact of human epidermal growth factor receptor 2 (HER2) status on the antitumor activity of CH5164840, an orally available heat shock protein 90 (HSP90) inhibitor, using pharmacokinetic-pharmacodynamic modeling.	CH5164840	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
25272063-7	2014	Overexpression of HSPs (27, 70, 90), HSF1, and HDAC6 in leukemia cells were down-regulated by curcumin, and the effects on HSPs 27and 70 were less than that on HSP 90.	Curcumin	94-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-166
25185500-5	2014	As a novel microtubule and heat shock protein 90 (HSP90) dual targeting inhibitor, CDBT causes the destabilization of microtubules and degradation of HSP90 client proteins CRAF-1 and ERBB2, resulting in cell cycle arrest at the G2/M phase and apoptosis.	GNF-PF-62	83-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-48
25185500-5	2014	As a novel microtubule and heat shock protein 90 (HSP90) dual targeting inhibitor, CDBT causes the destabilization of microtubules and degradation of HSP90 client proteins CRAF-1 and ERBB2, resulting in cell cycle arrest at the G2/M phase and apoptosis.	GNF-PF-62	83-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
25185500-5	2014	As a novel microtubule and heat shock protein 90 (HSP90) dual targeting inhibitor, CDBT causes the destabilization of microtubules and degradation of HSP90 client proteins CRAF-1 and ERBB2, resulting in cell cycle arrest at the G2/M phase and apoptosis.	GNF-PF-62	83-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
24345447-2	2014	We have designed a series of hybrid Hsp90 inhibitors by connecting the resorcinol ring of VER-49009 (2) and the trimethoxyphenyl ring of PU3 (3) using structure-based approach.	resorcinol	71-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24345447-2	2014	We have designed a series of hybrid Hsp90 inhibitors by connecting the resorcinol ring of VER-49009 (2) and the trimethoxyphenyl ring of PU3 (3) using structure-based approach.	9-BUTYL-8-(3,4,5-TRIMETHOXYBENZYL)-9H-PURIN-6-AMINE	137-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24217247-6	2013	Geldanamycin, a HSP90alpha inhibitor, dissociated AKR1B10-HSP90alpha complexes and significantly reduced AKR1B10 secretion in a dose-dependent manner.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-26
24711448-4	2014	These amino acids reside in a region of PHD2 that harbors a zinc finger, which we have previously discovered binds to a Pro-Xaa-Leu-Glu (PXLE) motif in the HSP90 cochaperone p23, thereby recruiting PHD2 to the HSP90 pathway to facilitate HIF-alpha hydroxylation.	pro-xaa-leu-glu	120-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
24711448-4	2014	These amino acids reside in a region of PHD2 that harbors a zinc finger, which we have previously discovered binds to a Pro-Xaa-Leu-Glu (PXLE) motif in the HSP90 cochaperone p23, thereby recruiting PHD2 to the HSP90 pathway to facilitate HIF-alpha hydroxylation.	pro-xaa-leu-glu	120-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-215
24713615-7	2014	An exception was the marked response to celastrol which reduced the steady-state levels of cytoplasmic HSP90 transcripts and protein.	celastrol	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
24713615-8	2014	As Hsp90 participates in the targeting of misfolded proteins to the proteasome pathway, its down-modulation in response to celastrol may partly account for the mechanism of improved homeostasis of L444P GCase mediated by this triterpene.	celastrol	123-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
24713615-8	2014	As Hsp90 participates in the targeting of misfolded proteins to the proteasome pathway, its down-modulation in response to celastrol may partly account for the mechanism of improved homeostasis of L444P GCase mediated by this triterpene.	Triterpenes	226-236	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
24211270-6	2014	These results were similar to those of cells treated with geldanamycin (a heat shock protein (HSP)90 inhibitor), suggesting that RuCO might affect HSP90 activity.	geldanamycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-100
24211270-6	2014	These results were similar to those of cells treated with geldanamycin (a heat shock protein (HSP)90 inhibitor), suggesting that RuCO might affect HSP90 activity.	geldanamycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
24211270-10	2014	Additionally, treatment with a chemopreventive compound, curcumin, induced HO-1 expression accompanied with reduction of HSP90 client protein expression.	Curcumin	57-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
24217247-6	2013	Geldanamycin, a HSP90alpha inhibitor, dissociated AKR1B10-HSP90alpha complexes and significantly reduced AKR1B10 secretion in a dose-dependent manner.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-68
24217247-8	2013	Targeted point mutations recognized that amino acids Lys-233, Glu-236, and Lys-240 in helix 10 mediate the interaction of AKR1B10 with HSP90alpha.	Lysine	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-145
24217247-8	2013	Targeted point mutations recognized that amino acids Lys-233, Glu-236, and Lys-240 in helix 10 mediate the interaction of AKR1B10 with HSP90alpha.	Glutamic Acid	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-145
24217247-8	2013	Targeted point mutations recognized that amino acids Lys-233, Glu-236, and Lys-240 in helix 10 mediate the interaction of AKR1B10 with HSP90alpha.	Lysine	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-145
24380020-3	2013	To fulfill this task Hsp90 performs conformational changes driven by the hydrolysis of ATP.	Adenosine Triphosphate	87-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
24241349-0	2013	Hsp90 inhibitor BIIB021 enhances triptolide-induced apoptosis of human T-cell acute lymphoblastic leukemia cells in vitro mainly by disrupting p53-MDM2 balance.	triptolide	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23955554-0	2013	Ethoxyquin prevents chemotherapy-induced neurotoxicity via Hsp90 modulation.	Ethoxyquin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
23911537-5	2013	Pretreatment with geldanamycin, which binds to the ATP pocket of HSP90, significantly decreased the interaction of rpS3 with HSP90 and stimulated the accumulation of rpS3 in the mitochondria.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
23911537-5	2013	Pretreatment with geldanamycin, which binds to the ATP pocket of HSP90, significantly decreased the interaction of rpS3 with HSP90 and stimulated the accumulation of rpS3 in the mitochondria.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
23911537-5	2013	Pretreatment with geldanamycin, which binds to the ATP pocket of HSP90, significantly decreased the interaction of rpS3 with HSP90 and stimulated the accumulation of rpS3 in the mitochondria.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
23911537-7	2013	Therefore, we concluded that when mitochondrial DNA damages accumulate due to increased levels of ROS, rpS3 accumulates in the mitochondria to repair damaged DNA due to the decreased interaction between rpS3 and HSP90 in the cytosol.	ros	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
23955554-5	2013	Furthermore, we demonstrated that ethoxyquin acts by modulating the chaperone activity of heat shock protein 90 (Hsp90) and blocking the binding of 2 of its client proteins, ataxin-2 and Sf3b2.	Ethoxyquin	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-111
23955554-5	2013	Furthermore, we demonstrated that ethoxyquin acts by modulating the chaperone activity of heat shock protein 90 (Hsp90) and blocking the binding of 2 of its client proteins, ataxin-2 and Sf3b2.	Ethoxyquin	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
23955554-7	2013	INTERPRETATION: Ethoxyquin and its novel derivatives as well as other classes of small molecules that act as Hsp90 modulators may offer a new opportunity for development of drugs to prevent chemotherapy-induced axonal degeneration.	Ethoxyquin	16-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
24125885-0	2013	Targeting the hydrophobic region of Hsp90"s ATP binding pocket with novel 1,3,5-triazines.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
23933177-6	2013	EF31 and UBS109 inhibited HSP-90 and NF-kappaB leading to downregulation of DNA methyltransferase-1 (DNMT-1) expression.	UBS109	9-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-32
24125885-0	2013	Targeting the hydrophobic region of Hsp90"s ATP binding pocket with novel 1,3,5-triazines.	1,3,5-triazines	74-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24125885-2	2013	In an attempt to discover a new class of Hsp90 inhibitors, a series of 1,3,5-triazine compounds were rationally designed, synthesized, and their biological activities were evaluated.	1,3,5-TRIAZINE	71-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
24125885-4	2013	The binding mode of 3b in the ATP-binding site of Hsp90 was predicted by the molecular docking.	Adenosine Triphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
24263157-3	2013	Ad-mda-7 and an Hsp90 inhibitor, geldanamycin (GA), produced cytotoxic effects, and a combinatory use of Ad-mda-7 and GA further achieved synergistic effects.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
24263157-3	2013	Ad-mda-7 and an Hsp90 inhibitor, geldanamycin (GA), produced cytotoxic effects, and a combinatory use of Ad-mda-7 and GA further achieved synergistic effects.	geldanamycin	47-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
24012704-2	2013	17-Allylamino-17-demethoxy geldanamycin (17-AAG) is an inhibitor of heat shock protein 90 (HSP90).	tanespimycin	0-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
24012704-2	2013	17-Allylamino-17-demethoxy geldanamycin (17-AAG) is an inhibitor of heat shock protein 90 (HSP90).	tanespimycin	0-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
24046333-1	2013	6-Chloro-9-(4-methoxy-3,5-dimethyl-pyridin-2-ylmethyl)-9H-purin-2-ylamine (BIIB021), a synthetic HSP90 inhibitor, exhibited promising antitumor activity in preclinical models and was in development for the treatment of breast cancer.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	0-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
24121490-0	2013	The HSP90 inhibitor ganetespib synergizes with the MET kinase inhibitor crizotinib in both crizotinib-sensitive and -resistant MET-driven tumor models.	STA 9090	20-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24121490-0	2013	The HSP90 inhibitor ganetespib synergizes with the MET kinase inhibitor crizotinib in both crizotinib-sensitive and -resistant MET-driven tumor models.	Crizotinib	72-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24121490-0	2013	The HSP90 inhibitor ganetespib synergizes with the MET kinase inhibitor crizotinib in both crizotinib-sensitive and -resistant MET-driven tumor models.	Crizotinib	91-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24121490-6	2013	Combining the HSP90 inhibitor ganetespib with the MET-TKI crizotinib achieves synergistic inhibition of MET, its downstream signaling pathways, and tumor growth in both TKI-sensitive and -resistant MET-driven tumor models.	STA 9090	30-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
24046333-1	2013	6-Chloro-9-(4-methoxy-3,5-dimethyl-pyridin-2-ylmethyl)-9H-purin-2-ylamine (BIIB021), a synthetic HSP90 inhibitor, exhibited promising antitumor activity in preclinical models and was in development for the treatment of breast cancer.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
24109220-7	2013	Treatment of HTLV-1-transformed cells with the HSP90 inhibitor 17-DMAG elicited proteasomal degradation of Tax in the nuclear matrix with concomitant inhibition of NF-kappaB and HTLV-1 long terminal repeat (LTR) activation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	63-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
24090817-1	2013	In human trials certain heat shock protein 90 (Hsp90) inhibitors, including 17-DMAG and NVP-AUY922, have caused visual disorders indicative of retinal dysfunction; others such as 17-AAG and ganetespib have not.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	76-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
24090817-1	2013	In human trials certain heat shock protein 90 (Hsp90) inhibitors, including 17-DMAG and NVP-AUY922, have caused visual disorders indicative of retinal dysfunction; others such as 17-AAG and ganetespib have not.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	76-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
24090817-1	2013	In human trials certain heat shock protein 90 (Hsp90) inhibitors, including 17-DMAG and NVP-AUY922, have caused visual disorders indicative of retinal dysfunction; others such as 17-AAG and ganetespib have not.	tanespimycin	179-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
24090817-1	2013	In human trials certain heat shock protein 90 (Hsp90) inhibitors, including 17-DMAG and NVP-AUY922, have caused visual disorders indicative of retinal dysfunction; others such as 17-AAG and ganetespib have not.	tanespimycin	179-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
24090817-1	2013	In human trials certain heat shock protein 90 (Hsp90) inhibitors, including 17-DMAG and NVP-AUY922, have caused visual disorders indicative of retinal dysfunction; others such as 17-AAG and ganetespib have not.	STA 9090	190-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
24090817-1	2013	In human trials certain heat shock protein 90 (Hsp90) inhibitors, including 17-DMAG and NVP-AUY922, have caused visual disorders indicative of retinal dysfunction; others such as 17-AAG and ganetespib have not.	STA 9090	190-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
23873112-2	2013	The expression of HSP90 was investigated in 38 paraffin-embedded samples of PHEO patients using immunohistochemistry.	Paraffin	47-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
24689233-13	2013	The decreased levels of RAF-1, EGFR, AKT, CDK4 and HER-2 showed that CDG possessed HSP90 inhibitory effect.	cdg	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
24158444-7	2013	Finally, knockdown renders cells more susceptible to the Hsp90 inhibitor 17-AAG, suggesting that UBE3C protects against the harmful accumulation of protein fragments arising from incompletely degraded proteasome substrates.	tanespimycin	73-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
24900777-2	2014	Currently, the majority of Hsp90 C-terminal inhibitors are derived from novobiocin, a natural product traditionally used as an antibiotic.	Novobiocin	72-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
24900777-3	2014	Assisted by molecular docking studies, a scaffold containing a biphenyl moiety in lieu of the coumarin ring system found in novobiocin was identified for development of new Hsp90 C-terminal inhibitors.	coumarin	94-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
24900777-3	2014	Assisted by molecular docking studies, a scaffold containing a biphenyl moiety in lieu of the coumarin ring system found in novobiocin was identified for development of new Hsp90 C-terminal inhibitors.	Novobiocin	124-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
24114842-3	2013	CQ accumulated the acetylation levels of several key proteins including histone H3 (H3), p53, HSP90, and alpha-tubulin.	Clioquinol	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
24278192-1	2013	(-)-Epigallocatechin 3-O-gallate (EGCG) a molecule found in green tea and known for a plethora of bioactive properties is an inhibitor of heat shock protein 90 (HSP90), a protein of interest as a target for cancer and neuroprotection.	epigallocatechin gallate	0-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-159
24278192-1	2013	(-)-Epigallocatechin 3-O-gallate (EGCG) a molecule found in green tea and known for a plethora of bioactive properties is an inhibitor of heat shock protein 90 (HSP90), a protein of interest as a target for cancer and neuroprotection.	epigallocatechin gallate	0-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
24278192-1	2013	(-)-Epigallocatechin 3-O-gallate (EGCG) a molecule found in green tea and known for a plethora of bioactive properties is an inhibitor of heat shock protein 90 (HSP90), a protein of interest as a target for cancer and neuroprotection.	epigallocatechin gallate	34-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-159
24278192-1	2013	(-)-Epigallocatechin 3-O-gallate (EGCG) a molecule found in green tea and known for a plethora of bioactive properties is an inhibitor of heat shock protein 90 (HSP90), a protein of interest as a target for cancer and neuroprotection.	epigallocatechin gallate	34-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
23948507-5	2013	A detailed study using many biophysical methods has revealed that Hsp90 prevents alpha-synuclein from aggregating in an ATP-independent manner and that it forms a strong complex with the transiently populated toxic oligomeric alpha-synuclein species formed along the aggregation pathway.	Adenosine Triphosphate	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
23948708-7	2013	Moreover, by double affinity chromatography and subsequent analysis with mass spectrometry, we identified in the heat shock protein 90-alpha (HSP90alpha) a good candidate as carrier of the Galbeta1-3GalNAc epitope at low oxygen tension.	Oxygen	221-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-152
24070451-6	2013	In this study, we employed IFST to study the displacement of water molecules from the ATP binding site of Hsp90, using a test set of 103 ligands.	Adenosine Triphosphate	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
23580156-5	2013	We demonstrated that CPS induces pre- and early apoptotic cell surface exposure of calreticulin (CRT), HSP90, and HSP70 as well as ATP release.	Capsaicin	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
24045182-0	2013	A phase I study of the HSP90 inhibitor retaspimycin hydrochloride (IPI-504) in patients with gastrointestinal stromal tumors or soft-tissue sarcomas.	tanespimycin	39-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24045182-0	2013	A phase I study of the HSP90 inhibitor retaspimycin hydrochloride (IPI-504) in patients with gastrointestinal stromal tumors or soft-tissue sarcomas.	tanespimycin	67-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24045182-2	2013	This phase I study investigated the safety and maximum tolerated dose (MTD) of retaspimycin hydrochloride (IPI-504), a novel potent and selective HSP90 inhibitor, in patients with metastatic and/or unresectable GIST or other soft-tissue sarcomas (STS).	tanespimycin	79-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
24185264-0	2013	Mode of cell death induced by the HSP90 inhibitor 17-AAG (tanespimycin) is dependent on the expression of pro-apoptotic BAX.	tanespimycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24317089-6	2013	The HSP90 inhibitor 17-AAG abrogated the effects of the IBP inhibitors on intracellular monoclonal protein levels and localization as well as induction of the UPR in myeloma cells.	tanespimycin	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
24045182-13	2013	CONCLUSIONS: In this study of advanced GIST or other STS, IPI-504 was generally well-tolerated with some evidence of antitumor activity, serving as a clinical proof-of-concept that HSP90 inhibition remains a promising strategy.	tanespimycin	58-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
22955701-1	2013	The aim of this study was to investigate the effects of 17-Allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor, on the proliferation, cell cycle, and apoptosis of human cholangiocarcinoma (CCA) cells.	tanespimycin	56-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-128
22955701-1	2013	The aim of this study was to investigate the effects of 17-Allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor, on the proliferation, cell cycle, and apoptosis of human cholangiocarcinoma (CCA) cells.	tanespimycin	56-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
23886587-0	2013	The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin modulates radiosensitivity by downregulating serine/threonine kinase 38 via Sp1 inhibition.	tanespimycin	20-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23886587-1	2013	The ansamycin-based HSP90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) combats tumors and has been shown to modulate cellular sensitivity to radiation, prompting researchers to use 17-AAG as a radiosensitizer.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
23886587-1	2013	The ansamycin-based HSP90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) combats tumors and has been shown to modulate cellular sensitivity to radiation, prompting researchers to use 17-AAG as a radiosensitizer.	tanespimycin	44-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
24018284-5	2013	However, Hsp90alpha inhibitors both natural and chemical, reported so far are plagued with problems related to toxicity, bioavailability and solubility including geldanamycin, the most common Hsp90alpha inhibitor.	geldanamycin	162-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-19
24018284-5	2013	However, Hsp90alpha inhibitors both natural and chemical, reported so far are plagued with problems related to toxicity, bioavailability and solubility including geldanamycin, the most common Hsp90alpha inhibitor.	geldanamycin	162-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	192-202
23995768-3	2013	Here we combine compound library screening with structural and computational analyses to identify purine-based chemical tools that are specific for Hsp90 paralogs.	purine	98-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
24056254-10	2013	Very interestingly, Sulforaphane, Withaferin A, Celastrol and EGCG all decreased the complemented NRL-Hsp90alpha/Cdc37-CRL activities in the concentration-dependent manner.	celastrol	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-112
24056254-10	2013	Very interestingly, Sulforaphane, Withaferin A, Celastrol and EGCG all decreased the complemented NRL-Hsp90alpha/Cdc37-CRL activities in the concentration-dependent manner.	epigallocatechin gallate	62-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-112
24070451-0	2013	Combining solvent thermodynamic profiles with functionality maps of the Hsp90 binding site to predict the displacement of water molecules.	Water	122-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
24070451-6	2013	In this study, we employed IFST to study the displacement of water molecules from the ATP binding site of Hsp90, using a test set of 103 ligands.	Water	61-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
24070451-10	2013	The results show that IFST alone can be used to reliably predict the observed displacement of water molecules in Hsp90.	Water	94-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
23943653-1	2013	PU-H71 is a purine-scaffold Hsp90 inhibitor that, in contrast to other Hsp90 inhibitors, displays unique selectivity for binding the fraction of Hsp90 that is preferentially associated with oncogenic client proteins and enriched in tumor cells (teHsp90).	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
24156782-0	2013	A novel Hsp90 inhibitor AT13387 induces senescence in EBV-positive nasopharyngeal carcinoma cells and suppresses tumor formation.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	24-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
24156782-2	2013	AT13387 is a novel heat shock protein 90 (Hsp90) inhibitor, which inhibits the chaperone function of Hsp90 and reduces expression of Hsp90-dependent client oncoproteins.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-40
24156782-2	2013	AT13387 is a novel heat shock protein 90 (Hsp90) inhibitor, which inhibits the chaperone function of Hsp90 and reduces expression of Hsp90-dependent client oncoproteins.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
24156782-2	2013	AT13387 is a novel heat shock protein 90 (Hsp90) inhibitor, which inhibits the chaperone function of Hsp90 and reduces expression of Hsp90-dependent client oncoproteins.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
24156782-2	2013	AT13387 is a novel heat shock protein 90 (Hsp90) inhibitor, which inhibits the chaperone function of Hsp90 and reduces expression of Hsp90-dependent client oncoproteins.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
24156782-4	2013	RESULTS: Our results showed that AT13387 inhibited C666-1 cell growth and induced cellular senescence with the downregulation of multiple Hsp90 client oncoproteins EGFR, AKT, CDK4, and restored the protein expression of negative cell cycle regulator p27.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	33-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
23943653-1	2013	PU-H71 is a purine-scaffold Hsp90 inhibitor that, in contrast to other Hsp90 inhibitors, displays unique selectivity for binding the fraction of Hsp90 that is preferentially associated with oncogenic client proteins and enriched in tumor cells (teHsp90).	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
23943653-1	2013	PU-H71 is a purine-scaffold Hsp90 inhibitor that, in contrast to other Hsp90 inhibitors, displays unique selectivity for binding the fraction of Hsp90 that is preferentially associated with oncogenic client proteins and enriched in tumor cells (teHsp90).	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
23943653-1	2013	PU-H71 is a purine-scaffold Hsp90 inhibitor that, in contrast to other Hsp90 inhibitors, displays unique selectivity for binding the fraction of Hsp90 that is preferentially associated with oncogenic client proteins and enriched in tumor cells (teHsp90).	purine	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
23934201-0	2013	Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.	geldanamycin	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-31
23934201-0	2013	Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.	geldanamycin	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
23934201-5	2013	Competition for ATP by geldanamycin and related compounds abrogate the chaperone function of Hsp90.	Adenosine Triphosphate	16-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
23934201-5	2013	Competition for ATP by geldanamycin and related compounds abrogate the chaperone function of Hsp90.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
23934201-6	2013	In this context, this account pursues three topics in detail: a) Hsp90 and its biochemistry, b) Hsp90 and its role in oncogenesis and c) strategies to create compound libraries of structurally complex inhibitors like geldanamycin on which SAR studies and the development of drugs that are currently in different stages of clinical testing rely.	geldanamycin	217-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
23934201-6	2013	In this context, this account pursues three topics in detail: a) Hsp90 and its biochemistry, b) Hsp90 and its role in oncogenesis and c) strategies to create compound libraries of structurally complex inhibitors like geldanamycin on which SAR studies and the development of drugs that are currently in different stages of clinical testing rely.	geldanamycin	217-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
24127661-9	2013	Novobiocin analogues that revealed activity in this assay were examined via western blot experiments for client protein degradation, a hallmark of Hsp90 inhibition.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
23770604-0	2013	An improved route to 19-substituted geldanamycins as novel Hsp90 inhibitors--potential therapeutics in cancer and neurodegeneration.	19-substituted geldanamycins	21-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
23770604-1	2013	19-Substituted geldanamycin derivatives are efficient Hsp90 inhibitors, without the toxicity associated with the other benzoquinone ansamycins, thus giving them potential for use as molecular therapeutics in cancer and neurodegeneration.	geldanamycin	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
23838996-3	2013	We hypothesized that ganetespib, a potent HSP90 inhibitor, would disrupt angiogenesis in colorectal cancer (CRC) through inhibition of HIF-1alpha and STAT-3.	STA 9090	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23863134-0	2013	Enhanced antitumor activity of erlotinib in combination with the Hsp90 inhibitor CH5164840 against non-small-cell lung cancer.	CH5164840	81-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
23863134-5	2013	In the present study, we investigated the effect of the novel Hsp90 inhibitor CH5164840 on the antitumor activity of erlotinib.	CH5164840	78-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
23863134-5	2013	In the present study, we investigated the effect of the novel Hsp90 inhibitor CH5164840 on the antitumor activity of erlotinib.	Erlotinib Hydrochloride	117-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
23863134-9	2013	Phosphorylation of Stat3 increased with erlotinib treatment in NCI-H292 cells, which was abrogated by Hsp90 inhibition.	Erlotinib Hydrochloride	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
23863134-13	2013	Our results support the therapeutic potential of CH5164840 as a Hsp90 inhibitor for combination therapy with EGFR-targeting agents against EGFR-addicted NSCLC.	CH5164840	49-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
24056254-10	2013	Very interestingly, Sulforaphane, Withaferin A, Celastrol and EGCG all decreased the complemented NRL-Hsp90alpha/Cdc37-CRL activities in the concentration-dependent manner.	sulforaphane	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-112
24056254-10	2013	Very interestingly, Sulforaphane, Withaferin A, Celastrol and EGCG all decreased the complemented NRL-Hsp90alpha/Cdc37-CRL activities in the concentration-dependent manner.	withaferin A	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-112
24518700-1	2013	Heat shock protein 90 (Hsp90) a member of the heat shock proteins (HSPs) family, is an adenosine triphosphate dependent molecular chaperone protein, which integrates multiple oncogenic pathways.	Adenosine Triphosphate	87-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
24518700-1	2013	Heat shock protein 90 (Hsp90) a member of the heat shock proteins (HSPs) family, is an adenosine triphosphate dependent molecular chaperone protein, which integrates multiple oncogenic pathways.	Adenosine Triphosphate	87-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
24518700-3	2013	Hsp90 as the target of anticancer activity of geldanamycin sparked much interest in the inhibition of Hsp90 as a strategy for the treatment of cancer.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24518700-3	2013	Hsp90 as the target of anticancer activity of geldanamycin sparked much interest in the inhibition of Hsp90 as a strategy for the treatment of cancer.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
24014883-10	2013	TAS-116, a new class of Hsp-90alpha/beta inhibitor, is one of the products.	TAS-116	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-35
24066128-0	2013	Identification of the plant compound geraniin as a novel Hsp90 inhibitor.	Geraniin	37-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
24066128-2	2013	In an effort to discover new small molecules able to inhibit the Hsp90 ATPase and chaperoning activities, we screened, by a surface plasmon resonance assay, a small library including different plant polyphenols.	Polyphenols	199-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
24066128-4	2013	Geraniin was able to inhibit in vitro the Hsp90alpha ATPase activity in a dose-dependent manner, with an inhibitory efficiency comparable to that measured for 17-AAG.	Geraniin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-52
23881928-0	2013	A purine scaffold HSP90 inhibitor BIIB021 has selective activity against KSHV-associated primary effusion lymphoma and blocks vFLIP K13-induced NF-kappaB.	purine	2-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
23881928-5	2013	RESULTS: We show that BIIB021, a purine scaffold-based orally administrable HSP90 inhibitor, shows preferential cytotoxicity toward PEL cells as compared with non-PEL cells.	purine	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
23900136-7	2013	We therefore assessed ganetespib, a clinically promising second-generation small-molecule HSP90 inhibitor, for activity against EOC, both as a single agent and in combination with cytotoxic and targeted therapeutic agents.	STA 9090	22-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
23897823-1	2013	An eight-amino acid segment is known to be responsible for the marked difference in the rates of degradation of the EGF receptor (ErbB1) and ErbB2 upon treatment of cells with the Hsp90 inhibitor geldanamycin.	geldanamycin	196-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
24066060-5	2013	We focused on the redox perylene-quinone Hypericin (HYP) and showed that HYP targets Hsp90 for polyubiquitination, degradation and inactivation.	perylenequinone	24-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
24066060-5	2013	We focused on the redox perylene-quinone Hypericin (HYP) and showed that HYP targets Hsp90 for polyubiquitination, degradation and inactivation.	hypericin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
23777986-0	2013	The Hsp90 inhibitor SNX-2112, induces apoptosis in multidrug resistant K562/ADR cells through suppression of Akt/NF-kappaB and disruption of mitochondria-dependent pathways.	SNX 2112	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23777986-1	2013	Heat shock protein 90 (Hsp90) serves as an ATP-dependent molecular chaperone for numerous cell signaling proteins, including many oncogenes and clinically validated cancer targets that are involved in cell proliferation and survival.	Adenosine Triphosphate	43-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
23777986-1	2013	Heat shock protein 90 (Hsp90) serves as an ATP-dependent molecular chaperone for numerous cell signaling proteins, including many oncogenes and clinically validated cancer targets that are involved in cell proliferation and survival.	Adenosine Triphosphate	43-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23777986-2	2013	Recent studies have shown that the Hsp90 inhibitor, SNX-2112, effectively inhibits tumor cell growth and angiogenesis in hematological and solid tumors.	SNX 2112	52-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
24019877-2	2013	Nitric oxide (NO) is synthesised by nitric oxide synthase (NOS), which is a client protein of the molecular chaperon heat shock protein 90 (HSP90).	Nitric Oxide	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
23859777-0	2013	Synthesis and biological evaluation of novobiocin analogues as potential heat shock protein 90 inhibitors.	Novobiocin	39-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-94
23859777-1	2013	Recent studies have shown that novobiocin (NB), a member of the coumermycin (CA) family of antibiotics with demonstrated DNA gyrase inhibitory activity, inhibits Heat shock protein 90 (HSP90) by binding weakly to a putative ATP-binding site within its C-terminus.	Novobiocin	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-183
23859777-1	2013	Recent studies have shown that novobiocin (NB), a member of the coumermycin (CA) family of antibiotics with demonstrated DNA gyrase inhibitory activity, inhibits Heat shock protein 90 (HSP90) by binding weakly to a putative ATP-binding site within its C-terminus.	Novobiocin	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
23859777-1	2013	Recent studies have shown that novobiocin (NB), a member of the coumermycin (CA) family of antibiotics with demonstrated DNA gyrase inhibitory activity, inhibits Heat shock protein 90 (HSP90) by binding weakly to a putative ATP-binding site within its C-terminus.	coumermycin	64-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-183
23859777-1	2013	Recent studies have shown that novobiocin (NB), a member of the coumermycin (CA) family of antibiotics with demonstrated DNA gyrase inhibitory activity, inhibits Heat shock protein 90 (HSP90) by binding weakly to a putative ATP-binding site within its C-terminus.	coumermycin	64-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
23859777-1	2013	Recent studies have shown that novobiocin (NB), a member of the coumermycin (CA) family of antibiotics with demonstrated DNA gyrase inhibitory activity, inhibits Heat shock protein 90 (HSP90) by binding weakly to a putative ATP-binding site within its C-terminus.	Adenosine Triphosphate	224-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-183
23859777-1	2013	Recent studies have shown that novobiocin (NB), a member of the coumermycin (CA) family of antibiotics with demonstrated DNA gyrase inhibitory activity, inhibits Heat shock protein 90 (HSP90) by binding weakly to a putative ATP-binding site within its C-terminus.	Adenosine Triphosphate	224-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
23873691-2	2013	We conducted a phase I dose-finding and pharmacokinetic/pharmacodynamic study of BIIB028, a prodrug designed to inhibit Hsp90 activity.	KD4GWWK597	81-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
23843639-0	2013	Hsp90 inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	16-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23706562-3	2013	We hypothesize that chloroquine (CQ), an antimalarial drug that inhibits autophagosome function, in combination with either echinomycin, a HIF-1alpha inhibitor, or 17-dimethylaminoethylamino-17-dimethoxygeldanamycin (17-DMAG), an Hsp 90 inhibitor, will result in cytotoxicity in melanoma.	Chloroquine	20-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-236
23706562-3	2013	We hypothesize that chloroquine (CQ), an antimalarial drug that inhibits autophagosome function, in combination with either echinomycin, a HIF-1alpha inhibitor, or 17-dimethylaminoethylamino-17-dimethoxygeldanamycin (17-DMAG), an Hsp 90 inhibitor, will result in cytotoxicity in melanoma.	Chloroquine	33-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-236
23256542-1	2013	Abstract This phase I study was conducted to determine the maximum tolerated dose (MTD) and dose limiting toxicities (DLTs) of the heat shock protein 90 (HSP90) inhibitor 17-allyamino-17-demethoxygeldanamycin (17-AAG) in combination with bortezomib, and to provide pharmacokinetic data in relapsed or refractory acute myeloid leukemia (AML).	17-allyamino-17-demethoxygeldanamycin	171-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-152
23256542-1	2013	Abstract This phase I study was conducted to determine the maximum tolerated dose (MTD) and dose limiting toxicities (DLTs) of the heat shock protein 90 (HSP90) inhibitor 17-allyamino-17-demethoxygeldanamycin (17-AAG) in combination with bortezomib, and to provide pharmacokinetic data in relapsed or refractory acute myeloid leukemia (AML).	17-allyamino-17-demethoxygeldanamycin	171-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
23256542-1	2013	Abstract This phase I study was conducted to determine the maximum tolerated dose (MTD) and dose limiting toxicities (DLTs) of the heat shock protein 90 (HSP90) inhibitor 17-allyamino-17-demethoxygeldanamycin (17-AAG) in combination with bortezomib, and to provide pharmacokinetic data in relapsed or refractory acute myeloid leukemia (AML).	tanespimycin	210-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
23256542-1	2013	Abstract This phase I study was conducted to determine the maximum tolerated dose (MTD) and dose limiting toxicities (DLTs) of the heat shock protein 90 (HSP90) inhibitor 17-allyamino-17-demethoxygeldanamycin (17-AAG) in combination with bortezomib, and to provide pharmacokinetic data in relapsed or refractory acute myeloid leukemia (AML).	Bortezomib	238-248	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
23843639-2	2013	In this study, we show that heat shock protein 90 (Hsp90) interacts directly with each of the eight CHPKs, and we demonstrate that an Hsp90 inhibitor drug, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), decreases expression of all eight CHPKs in transfected HeLa cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	156-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
23843639-2	2013	In this study, we show that heat shock protein 90 (Hsp90) interacts directly with each of the eight CHPKs, and we demonstrate that an Hsp90 inhibitor drug, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), decreases expression of all eight CHPKs in transfected HeLa cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	156-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
23843639-2	2013	In this study, we show that heat shock protein 90 (Hsp90) interacts directly with each of the eight CHPKs, and we demonstrate that an Hsp90 inhibitor drug, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), decreases expression of all eight CHPKs in transfected HeLa cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	156-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
23843639-2	2013	In this study, we show that heat shock protein 90 (Hsp90) interacts directly with each of the eight CHPKs, and we demonstrate that an Hsp90 inhibitor drug, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), decreases expression of all eight CHPKs in transfected HeLa cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	209-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
23843639-2	2013	In this study, we show that heat shock protein 90 (Hsp90) interacts directly with each of the eight CHPKs, and we demonstrate that an Hsp90 inhibitor drug, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), decreases expression of all eight CHPKs in transfected HeLa cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	209-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
23843639-2	2013	In this study, we show that heat shock protein 90 (Hsp90) interacts directly with each of the eight CHPKs, and we demonstrate that an Hsp90 inhibitor drug, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), decreases expression of all eight CHPKs in transfected HeLa cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	209-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
23843639-7	2013	These results suggest that Hsp90 inhibitors, including 17-DMAG, may be a promising group of drugs that could have profound antiviral effects on herpesviruses.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	55-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
23860250-0	2013	Design of novel Geldanamycin analogue hsp90 alpha-inhibitor in silico for breast cancer therapy.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-49
23860250-1	2013	BACKGROUND: Geldanamycin, which is one of the most potent and effective hsp90 alpha inhibitor until date, is normally used to target breast cancer.	geldanamycin	12-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-83
23860250-9	2013	We further hypothesize that the higher binding affinity of the novel Geldanamycin analogue for hsp90 alpha triggers the degradation of nonfunctional mutant p53 by cellular proteasomes.	geldanamycin	69-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-106
23828170-8	2013	ACTB, HSP90AA1, HSPA5 and HSPA8, which are key mediators of pathways related to apoptosis, proliferation and neoplastic processes, were key mediators of the same pathways in low-dose nickel and cadmium exposure in particular.	Nickel	183-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-14
23828170-8	2013	ACTB, HSP90AA1, HSPA5 and HSPA8, which are key mediators of pathways related to apoptosis, proliferation and neoplastic processes, were key mediators of the same pathways in low-dose nickel and cadmium exposure in particular.	Cadmium	194-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-14
23828170-10	2013	We found that HSP90AA1, one of the main modulators, interacted with HIF1A, AR and BCL2 in nickel-exposed cells.	Nickel	90-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-22
23828170-11	2013	Interestingly, we found that HSP90AA1 was involved in the BCL2-associated apoptotic pathway in the nickel-only data, whereas this gene interacted with several genes functioning in CASP-associated apoptotic signaling in the cadmium-only data.	Nickel	99-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-37
24015183-5	2013	We demonstrated that the treatment of 143B cells with geldanamycin caused a subsequent upregulation of cytoplasmic Hsp90 and Hsp70 whose activity is at least partly responsible for cancer development and drug resistance.	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
23955587-3	2013	The antibiotic geldanamycin (GA) inhibits HSP90"s ATP binding for its proper interaction with client proteins.	geldanamycin	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23955587-3	2013	The antibiotic geldanamycin (GA) inhibits HSP90"s ATP binding for its proper interaction with client proteins.	geldanamycin	29-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23955587-3	2013	The antibiotic geldanamycin (GA) inhibits HSP90"s ATP binding for its proper interaction with client proteins.	Adenosine Triphosphate	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23834230-0	2013	Synthesis and structure-activity relationships of EGCG analogues, a recently identified Hsp90 inhibitor.	epigallocatechin gallate	50-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
23834230-1	2013	Epigallocatechin-3-gallate (EGCG), the principal polyphenol isolated from green tea, was recently shown to inhibit Hsp90; however, structure-activity relationships for this natural product have not yet been produced.	epigallocatechin gallate	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
23834230-1	2013	Epigallocatechin-3-gallate (EGCG), the principal polyphenol isolated from green tea, was recently shown to inhibit Hsp90; however, structure-activity relationships for this natural product have not yet been produced.	epigallocatechin gallate	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
23834230-2	2013	Herein, we report the synthesis and biological evaluation of EGCG analogues to establish structure-activity relationships between EGCG and Hsp90.	epigallocatechin gallate	61-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
23834230-5	2013	The prenyl-substituted aryl ester of 3,5-dihydroxychroman-3-ol ring system was identified as a novel scaffold that exhibits Hsp90 inhibitory activity.	prenyl-substituted aryl ester	4-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
23834230-5	2013	The prenyl-substituted aryl ester of 3,5-dihydroxychroman-3-ol ring system was identified as a novel scaffold that exhibits Hsp90 inhibitory activity.	3,5-dihydroxychroman-3-ol	37-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
23951259-3	2013	Hsp90 undergoes an ATP hydrolysis dependent conformational cycle to assist folding of the client protein.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23951259-8	2013	However, the extra domain reduces the ATP hydrolysis rate to about half when compared to Hsp90 thereby acting as a negative regulator of the molecular chaperones intrinsic ATPase activity.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
23841533-7	2013	For example, our profiling results revealed K356 as a new ATP-binding site in HSP90.	potassium iodate	44-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
23841533-7	2013	For example, our profiling results revealed K356 as a new ATP-binding site in HSP90.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
23763277-0	2013	The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
23829382-0	2013	Alterations in macrophage cellular proteome induced by calcium oxalate crystals: the association of HSP90 and F-actin is important for phagosome formation.	Calcium Oxalate	55-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
23668972-5	2013	Several reports showed that the Hsp90 inhibitor geldanamycin (GA) induces Thr308 and Ser473 phosphorylations of Akt, however, it is still unknown about the significance of GA-induced Akt activation in degradation of the kinase.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
23668972-5	2013	Several reports showed that the Hsp90 inhibitor geldanamycin (GA) induces Thr308 and Ser473 phosphorylations of Akt, however, it is still unknown about the significance of GA-induced Akt activation in degradation of the kinase.	geldanamycin	62-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
23763277-3	2013	We describe a robust and readily assayed proteomics fingerprint that AUY922 shares with the flagship Hsp90 inhibitors 17-DMAG and radicicol.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	118-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
23763277-3	2013	We describe a robust and readily assayed proteomics fingerprint that AUY922 shares with the flagship Hsp90 inhibitors 17-DMAG and radicicol.	monorden	130-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
23674492-8	2013	RESULTS: NMS-E973, representative of a novel isoxazole-derived class of Hsp90 inhibitors, binds Hsp90alpha with subnanomolar affinity and high selectivity towards kinases, as well as other ATPases.	Isoxazoles	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
23763921-0	2013	Phase I trial of the HSP90 inhibitor PF-04929113 (SNX5422) in adult patients with recurrent, refractory hematologic malignancies.	SNX-5422	37-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
23763921-0	2013	Phase I trial of the HSP90 inhibitor PF-04929113 (SNX5422) in adult patients with recurrent, refractory hematologic malignancies.	SNX-5422	50-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
23763921-2	2013	We undertook a phase 1 trial of PF-04929113 (SNX-5422), a novel oral HSP90 inhibitor, to estimate the maximum tolerated dose and describe the pharmacokinetic and toxicity profiles.	SNX-5422	32-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
23641970-0	2013	Discovery and development of heat shock protein 90 inhibitors as anticancer agents: a review of patented potent geldanamycin derivatives.	geldanamycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
23641970-4	2013	Geldanamycin (GM), the first benzoquinone ansamycin, has shown anticancer activity by binding to Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
23641970-4	2013	Geldanamycin (GM), the first benzoquinone ansamycin, has shown anticancer activity by binding to Hsp90.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
23641970-4	2013	Geldanamycin (GM), the first benzoquinone ansamycin, has shown anticancer activity by binding to Hsp90.	benzoquinone ansamycin	29-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
23641970-6	2013	AREAS COVERED: Several research groups have studied GM and its derivatives to develop novel and potent Hsp90 inhibitors for the treatment of cancer.	geldanamycin	52-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
23641970-7	2013	The crystal structure of Hsp90 was utilized to undergo structural optimization of GM derivatives.	geldanamycin	82-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
23896275-5	2013	Here, we review the current status of HSP90 inhibitors in clinical development, including geldanamycin derivatives, resorcinol derivatives, purine analogues, and other synthetic inhibitors.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
23896275-5	2013	Here, we review the current status of HSP90 inhibitors in clinical development, including geldanamycin derivatives, resorcinol derivatives, purine analogues, and other synthetic inhibitors.	resorcinol	116-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
23896275-5	2013	Here, we review the current status of HSP90 inhibitors in clinical development, including geldanamycin derivatives, resorcinol derivatives, purine analogues, and other synthetic inhibitors.	purine	140-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
24379910-0	2013	Effectively delivering a unique hsp90 inhibitor using star polymers.	star polymers	54-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
24379910-1	2013	We report the synthesis of a novel heat shock protein 90 (hsp90) inhibitor conjugated to a star polymer.	star polymer	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-56
24379910-1	2013	We report the synthesis of a novel heat shock protein 90 (hsp90) inhibitor conjugated to a star polymer.	star polymer	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
24379910-3	2013	The stars were cross-linked using disulfide linkers, and a tagged version of our hsp90 inhibitor was conjugated to the polymer core to generate nanoparticles (14 nM).	Polymers	119-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
24379910-7	2013	These studies show that we can deliver our hsp90 inhibitor effectively using star polymers, and induce apoptosis by the same pathway as the parent compound.	star polymers	77-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
23687373-4	2013	We reveal that GSK47867A and GSK47869A specifically alter the GR LBD structure at the HSP90-binding site.	GSK47867A	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
23687373-4	2013	We reveal that GSK47867A and GSK47869A specifically alter the GR LBD structure at the HSP90-binding site.	GSK47869A	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
23687373-5	2013	The alteration in the HSP90-binding site was accompanied by resistance to HSP90 antagonism, with persisting transactivation seen after geldanamycin treatment.	geldanamycin	135-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
23698466-10	2013	Tid1-L inhibited EGFR signaling even more than the HSP90 inhibitor 17-allylamino-demethoxy geldanamycin.	17-allylamino-demethoxy geldanamycin	67-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
23674492-8	2013	RESULTS: NMS-E973, representative of a novel isoxazole-derived class of Hsp90 inhibitors, binds Hsp90alpha with subnanomolar affinity and high selectivity towards kinases, as well as other ATPases.	Isoxazoles	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-106
23757357-0	2013	First-in-human phase I dose-escalation study of the HSP90 inhibitor AUY922 in patients with advanced solid tumors.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
23926110-0	2013	Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis.	pyrimidine	109-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36
22851653-14	2013	Bioinformatic data were confirmed since the expression of HSP90, AhR, ANRT, and beta-tubulin (involved in AhR-signalling transduction) were accordingly modified after IPost-Co. IPost-Co rescued 52% of the left ventricle-at-risk compared with reperfusion alone and resulted in a  30% relative improvement in left ventricular ejection fraction (P &lt;0.05).	ipost-co	167-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
23926110-4	2013	We found that Cpr6 and Hsp90 interacted with Ura2, a protein critical for pyrimidine biosynthesis.	pyrimidine	74-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23729439-5	2013	Importantly, inhibition of HDAC activity by trichostatin A (TSA) enhanced the hyperacetylation of heat shock protein (HSP)90 and suppressed its chaperone activity for IRF-1.	trichostatin A	44-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-124
23770448-0	2013	Dimeric and trimeric triazole based molecules as a new class of Hsp90 molecular chaperone inhibitors.	trimeric triazole	12-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
23770448-4	2013	Surface Plasmon Resonance Binding assay, performed on the synthesized compounds, allow to identify a series of molecules able to potently interact with the target enzyme and to disclose an interesting hit: compound 2b showed to interact with the ATP binding site in the N-terminus domain of Hsp90 and to efficiently inhibit the chaperone activity.	Adenosine Triphosphate	246-249	heat shock protein 90 alpha family class A member 1	Homo sapiens	291-296
23729439-5	2013	Importantly, inhibition of HDAC activity by trichostatin A (TSA) enhanced the hyperacetylation of heat shock protein (HSP)90 and suppressed its chaperone activity for IRF-1.	trichostatin A	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-124
23768697-9	2013	Rosuvastatin reduced the phosphorylation of Y455 in HSP90 protein.	Rosuvastatin Calcium	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
23867252-4	2013	Here we demonstrate that two chemically unrelated Hsp90 inhibitors, the benzoquinone ansamycin geldanamycin and the purine analog PU-H71, select for overlapping but not identical subpopulations of total cellular Hsp90, even though both inhibitors bind to an amino terminal nucleotide pocket and prevent N domain dimerization.	benzoquinone ansamycin geldanamycin	72-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
23867252-4	2013	Here we demonstrate that two chemically unrelated Hsp90 inhibitors, the benzoquinone ansamycin geldanamycin and the purine analog PU-H71, select for overlapping but not identical subpopulations of total cellular Hsp90, even though both inhibitors bind to an amino terminal nucleotide pocket and prevent N domain dimerization.	benzoquinone ansamycin geldanamycin	72-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
23867252-4	2013	Here we demonstrate that two chemically unrelated Hsp90 inhibitors, the benzoquinone ansamycin geldanamycin and the purine analog PU-H71, select for overlapping but not identical subpopulations of total cellular Hsp90, even though both inhibitors bind to an amino terminal nucleotide pocket and prevent N domain dimerization.	purine	116-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
23867252-4	2013	Here we demonstrate that two chemically unrelated Hsp90 inhibitors, the benzoquinone ansamycin geldanamycin and the purine analog PU-H71, select for overlapping but not identical subpopulations of total cellular Hsp90, even though both inhibitors bind to an amino terminal nucleotide pocket and prevent N domain dimerization.	purine	116-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
23303741-0	2013	Initial testing (stage 1) of ganetespib, an Hsp90 inhibitor, by the Pediatric Preclinical Testing Program.	STA 9090	29-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
23303741-1	2013	Ganetespib, an Hsp90 inhibitor, was tested against the PPTP in vitro cell line panel and selected xenografts in vivo, including JAK2- and BRAF-mutated models.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
23303741-5	2013	Administered as single agents, Hsp90 inhibitors examined by the PPTP have shown limited evidence for a therapeutic window against both solid tumor and leukemia pediatric preclinical models.	N-propyl-4-phenyl-1,2,3,6-tetrahydropyridine	64-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
23867252-4	2013	Here we demonstrate that two chemically unrelated Hsp90 inhibitors, the benzoquinone ansamycin geldanamycin and the purine analog PU-H71, select for overlapping but not identical subpopulations of total cellular Hsp90, even though both inhibitors bind to an amino terminal nucleotide pocket and prevent N domain dimerization.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	130-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
23867252-4	2013	Here we demonstrate that two chemically unrelated Hsp90 inhibitors, the benzoquinone ansamycin geldanamycin and the purine analog PU-H71, select for overlapping but not identical subpopulations of total cellular Hsp90, even though both inhibitors bind to an amino terminal nucleotide pocket and prevent N domain dimerization.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	130-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
23624237-0	2013	Structural requirements within protoporphyrin IX in the inhibition of heat shock protein 90.	protoporphyrin IX	31-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-91
23727383-2	2013	As adipocyte differentiation plays a critical role in obesity development, the present study investigated the effect of an Hsp90 inhibitor radicicol on the differentiation of 3T3-L1 preadipocytes and potential mechanisms.	monorden	139-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
23629654-3	2013	HSP90 inhibition by the antibiotic geldanamycin or its derivative 17-allylamino-17-demethoxygeldanamycin (17-AAG) causes destabilization of its client proteins.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23629654-3	2013	HSP90 inhibition by the antibiotic geldanamycin or its derivative 17-allylamino-17-demethoxygeldanamycin (17-AAG) causes destabilization of its client proteins.	tanespimycin	66-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23496136-0	2013	Learning from nature: advances in geldanamycin- and radicicol-based inhibitors of Hsp90.	geldanamycin	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23496136-0	2013	Learning from nature: advances in geldanamycin- and radicicol-based inhibitors of Hsp90.	monorden	52-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23485394-0	2013	Hsp90 inhibition by PU-H71 induces apoptosis through endoplasmic reticulum stress and mitochondrial pathway in cancer cells and overcomes the resistance conferred by Bcl-2.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23485394-2	2013	This study investigated the mechanism of apoptosis induced by the purine-scaffold Hsp90 inhibitor PU-H71 in different human cancer cell lines and examined the role of Bcl-2 and Bax in this process.	purine	66-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23764212-5	2013	In contrast, expression levels of cytosolic chaperones such as HSP90 and HSP71 were down-regulated in azacytidine-treated myeloma cells, concomitant with an increase of these chaperones in the cell culture medium, suggesting that mitochondrial chaperones and cytosolic chaperones behave differently in necrotic myeloma cells; ER- and mitochondrial-chaperones being retained, and cytosolic chaperones being released into the cell culture medium through the ruptured cell membrane.	Azacitidine	102-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
23624237-2	2013	Porphyrins prevent activation of hypoxia inducible factor-1alpha (HIF-1alpha) by inhibiting heat shock protein 90 (HSP90).	Porphyrins	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-113
23624237-2	2013	Porphyrins prevent activation of hypoxia inducible factor-1alpha (HIF-1alpha) by inhibiting heat shock protein 90 (HSP90).	Porphyrins	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
23624237-3	2013	This study investigated the structural requirements within protoporphyrin IX (PPIX) for the inhibition of HSP90 activity.	protoporphyrin IX	59-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
23624237-3	2013	This study investigated the structural requirements within protoporphyrin IX (PPIX) for the inhibition of HSP90 activity.	protoporphyrin IX	78-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
23624237-4	2013	In HCT116, HT29 and DLD-1 cells, PPIX treatment directly hindered the binding between HSP90 and HIF-1alpha; PPIX treatment inhibited the chaperone activity of HSP90, accelerating protein degradation of HIF-1alpha.	protoporphyrin IX	33-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
23624237-4	2013	In HCT116, HT29 and DLD-1 cells, PPIX treatment directly hindered the binding between HSP90 and HIF-1alpha; PPIX treatment inhibited the chaperone activity of HSP90, accelerating protein degradation of HIF-1alpha.	protoporphyrin IX	33-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
23624237-4	2013	In HCT116, HT29 and DLD-1 cells, PPIX treatment directly hindered the binding between HSP90 and HIF-1alpha; PPIX treatment inhibited the chaperone activity of HSP90, accelerating protein degradation of HIF-1alpha.	protoporphyrin IX	108-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
23624237-4	2013	In HCT116, HT29 and DLD-1 cells, PPIX treatment directly hindered the binding between HSP90 and HIF-1alpha; PPIX treatment inhibited the chaperone activity of HSP90, accelerating protein degradation of HIF-1alpha.	protoporphyrin IX	108-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
23624237-6	2013	In silico analysis, molecular docking model indicated that a tetrapyrrole macrocycle and two propionate chains within PPIX are necessary for the binding to the adenosine triphosphate (ATP)-binding pocket of HSP90.	Tetrapyrroles	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
23624237-6	2013	In silico analysis, molecular docking model indicated that a tetrapyrrole macrocycle and two propionate chains within PPIX are necessary for the binding to the adenosine triphosphate (ATP)-binding pocket of HSP90.	Propionates	93-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
23624237-6	2013	In silico analysis, molecular docking model indicated that a tetrapyrrole macrocycle and two propionate chains within PPIX are necessary for the binding to the adenosine triphosphate (ATP)-binding pocket of HSP90.	protoporphyrin IX	118-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
23624237-6	2013	In silico analysis, molecular docking model indicated that a tetrapyrrole macrocycle and two propionate chains within PPIX are necessary for the binding to the adenosine triphosphate (ATP)-binding pocket of HSP90.	Adenosine Triphosphate	160-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
23624237-6	2013	In silico analysis, molecular docking model indicated that a tetrapyrrole macrocycle and two propionate chains within PPIX are necessary for the binding to the adenosine triphosphate (ATP)-binding pocket of HSP90.	Adenosine Triphosphate	184-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
23624237-8	2013	Our results show that a tetrapyrrole macrocycle and two attached propionate chains in PPIX coordinately interact with the ATP-binding pocket of HSP90, offering structural information on the inhibitory effect of porphyrins on angiogenesis.	Tetrapyrroles	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
23624237-8	2013	Our results show that a tetrapyrrole macrocycle and two attached propionate chains in PPIX coordinately interact with the ATP-binding pocket of HSP90, offering structural information on the inhibitory effect of porphyrins on angiogenesis.	protoporphyrin IX	86-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
23624237-8	2013	Our results show that a tetrapyrrole macrocycle and two attached propionate chains in PPIX coordinately interact with the ATP-binding pocket of HSP90, offering structural information on the inhibitory effect of porphyrins on angiogenesis.	Adenosine Triphosphate	122-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
23493311-0	2013	The HSP90 inhibitor NVP-AUY922 potently inhibits non-small cell lung cancer growth.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	24-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23734688-3	2013	Hsp90 chaperone function depends on its ability to bind and hydrolyze ATP and Hsp90 inhibitors have been shown to compete with nucleotides for binding to Hsp90.	Adenosine Triphosphate	70-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23228483-10	2013	In the same experimental conditions, the combined treatment of tamoxifen with the Hsp90 inhibitor 17-AAG completely abrogated leptin-induced anchorage-independent breast cancer cell growth.	Tamoxifen	63-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23538902-0	2013	Inhibition of Wee1, AKT, and CDK4 underlies the efficacy of the HSP90 inhibitor XL888 in an in vivo model of NRAS-mutant melanoma.	XL 888	80-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
23538902-1	2013	The HSP90 inhibitor XL888 is effective at reversing BRAF inhibitor resistance in melanoma, including that mediated through acquired NRAS mutations.	XL 888	20-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23228483-10	2013	In the same experimental conditions, the combined treatment of tamoxifen with the Hsp90 inhibitor 17-AAG completely abrogated leptin-induced anchorage-independent breast cancer cell growth.	tanespimycin	98-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23900261-2	2013	Here we show that the N-terminal domain of pRb interacts with the CD domain of ESR1 to allow for the assembly of intermediate complex chaperone proteins HSP90 and p23.	Cadmium	66-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
23434444-8	2013	METHODS AND RESULTS: Using an in vitro cell line model we demonstrated that 17-DMAG (HSP90 inhibitor) co-administration with PTACH (HDAC inhibitor) caused elevated ER stress (immunoblotting) (more than 110% , p &lt; 0.05) accompanied by apoptotic cell death (Annexin V) (7-21% , p &lt; 0.05).	PTACH	125-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
23434444-8	2013	METHODS AND RESULTS: Using an in vitro cell line model we demonstrated that 17-DMAG (HSP90 inhibitor) co-administration with PTACH (HDAC inhibitor) caused elevated ER stress (immunoblotting) (more than 110% , p &lt; 0.05) accompanied by apoptotic cell death (Annexin V) (7-21% , p &lt; 0.05).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	76-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
23569206-2	2013	In complex with Hsp90, Cdc37 is thought to bind an important lid structure in the ATPase domain of Hsp90 and inhibit ATP turnover by Hsp90.	Adenosine Triphosphate	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
23569206-2	2013	In complex with Hsp90, Cdc37 is thought to bind an important lid structure in the ATPase domain of Hsp90 and inhibit ATP turnover by Hsp90.	Adenosine Triphosphate	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
23569206-2	2013	In complex with Hsp90, Cdc37 is thought to bind an important lid structure in the ATPase domain of Hsp90 and inhibit ATP turnover by Hsp90.	Adenosine Triphosphate	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
23569206-8	2013	Dephosphorylation of CeCdc37 by the Hsp90-associated phosphatase PPH-5, a step required during the kinase activation process, proceeds normally, even if only the new interaction site is used.	cecdc37	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
23569206-9	2013	This shows that the second interaction site is also functionally relevant and highlights that Cdc37, similar to the Hsp90 cofactors Sti1 and Aha1, may utilize two different attachment sites to restrict the conformational freedom and the ATP turnover of Hsp90.	Adenosine Triphosphate	237-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
23569206-9	2013	This shows that the second interaction site is also functionally relevant and highlights that Cdc37, similar to the Hsp90 cofactors Sti1 and Aha1, may utilize two different attachment sites to restrict the conformational freedom and the ATP turnover of Hsp90.	Adenosine Triphosphate	237-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	253-258
23589305-7	2013	We further show that KDM4B is ubiquitinated on lysines 337 and 562; simultaneous substitution of these residues to arginine suppressed the geldanamycin-induced degradation of KDM4B, suggesting that the ubiquitination of Lys-337 and Lys-562 targets KDM4B for proteasomal degradation upon Hsp90 inhibition.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	287-292
23589305-5	2013	Pharmacological inhibition of Hsp90 with geldanamycin resulted in ubiquitin-dependent proteasomal degradation of KDM4B, but not of KDM4C, suggesting that the turnover of these demethylases is regulated by distinct mechanisms.	geldanamycin	41-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
23553849-1	2013	PURPOSE: Ganetespib is a novel inhibitor of the heat shock protein 90 (Hsp90), a chaperone protein critical to tumor growth and proliferation.	STA 9090	9-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
23415900-2	2013	Whereas Hsp90 inhibitors such as 17-AAG exert promising antitumor effects in clinical trials, current efforts focus on developing agents targeting Hsp90 with improved efficacy and lower toxicity.	tanespimycin	33-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
23589305-7	2013	We further show that KDM4B is ubiquitinated on lysines 337 and 562; simultaneous substitution of these residues to arginine suppressed the geldanamycin-induced degradation of KDM4B, suggesting that the ubiquitination of Lys-337 and Lys-562 targets KDM4B for proteasomal degradation upon Hsp90 inhibition.	Arginine	115-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	287-292
23717436-4	2013	A dual stimulation of protein-bound polysaccharides isolated from Coriolus versicolor (TLR2 agonist) and penicillin-inactivated Streptococcus pyogenes (TLR4 agonist) led human monocyte-derived DCs to produce HSP90alpha and multiple cytokines such as IL-12p70 and IL-10.	Polysaccharides	36-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-218
23717436-4	2013	A dual stimulation of protein-bound polysaccharides isolated from Coriolus versicolor (TLR2 agonist) and penicillin-inactivated Streptococcus pyogenes (TLR4 agonist) led human monocyte-derived DCs to produce HSP90alpha and multiple cytokines such as IL-12p70 and IL-10.	Penicillins	105-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-218
23717436-6	2013	Moreover, fusions of ethanol-treated tumor cells and dual TLRs-stimulated DCs (E-tumor/FCs) inhibited the production of multiple immune-suppressive soluble factors including TGF-beta1 and up-regulated the production of IL-12p70 and HSP90alpha.	Ethanol	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-242
23507703-7	2013	In this regard, the HDAC6 silencing or the functional knockdown of hsp90 by 17AAG resulted in the selective downregulation of AR, EGFR, HER2, and Akt expression/activity, while the decreased phosphorylation of GSK-3beta mediated by PXD101 increased the nuclear expression of CRM1, which in turn modified the AR and survivin recycling with increased caspase 3 activity.	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
23658841-3	2013	We here screened small molecule inhibitors and isolated HSP90 inhibitors, Radicicol and 17-AAG, as candidates that suppress LMP1 expression and cell proliferation not only in EBV-positive SNK6 Natural Killer (NK) cell lymphoma cells, but also in B and T cells.	tanespimycin	88-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
23415900-3	2013	Using a fluorescence polarization assay, we screened over a hundred of synthetic small molecules and identified a resorcinol derivative LD053 that bound the Hsp90 ATP-binding pocket.	resorcinol	114-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
23415900-3	2013	Using a fluorescence polarization assay, we screened over a hundred of synthetic small molecules and identified a resorcinol derivative LD053 that bound the Hsp90 ATP-binding pocket.	Adenosine Triphosphate	163-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
23806880-1	2013	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
23806880-1	2013	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23564374-1	2013	BACKGROUND: 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) is a benzoquinone ansamycin that binds to and inhibits the Hsp90 family of molecular chaperones leading to the proteasomal degradation of client proteins critical in malignant cell proliferation and survival.	tanespimycin	12-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
23564374-1	2013	BACKGROUND: 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) is a benzoquinone ansamycin that binds to and inhibits the Hsp90 family of molecular chaperones leading to the proteasomal degradation of client proteins critical in malignant cell proliferation and survival.	benzoquinone ansamycin	67-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
23502424-0	2013	ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
23502424-3	2013	We show here that Cdc37 directly antagonizes ATP binding to client kinases, suggesting a role for the Hsp90-Cdc37 complex in controlling kinase activity.	Adenosine Triphosphate	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
23502424-6	2013	Our results suggest that at least part of the efficacy of ATP-competitive inhibitors of Hsp90-dependent kinases in tumor cells may be due to targeted chaperone deprivation.	Adenosine Triphosphate	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
23193992-4	2013	Upon binding to dioxin, aryl hydrocarbon receptor (AHR) dissociates from HSP90 and subsequently translocates to the nucleus, where it interacts with AHR nuclear translocator (ARNT).	Dioxins	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
23553849-1	2013	PURPOSE: Ganetespib is a novel inhibitor of the heat shock protein 90 (Hsp90), a chaperone protein critical to tumor growth and proliferation.	STA 9090	9-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
23193992-7	2013	Application of 3-methylcholanthrene, the AHR agonist, enhances BRET signals in cells co-expressing AHR-RL, AIP-His, P23-His and ARNT-YFP (AAPA cells), while suppressing BRET signals in cells co-expressing AHR-RL, AIP-His, P23-His and HSP90-YFP (AAPH cells).	Methylcholanthrene	15-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
23396260-9	2013	Knockdowns of DAF-21 (HSP90 ortholog) and HSF-1block the nuclear export of YAP-1 during this recovery.	daf-21	14-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
23750075-0	2013	Chemo-informatic design of antibiotic geldenamycin analogs to target stress proteins HSP90 of pathogenic protozoan parasites.	geldenamycin	38-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
23750075-3	2013	Here, using molecular modeling and docking protocols, antibiotic Geldenamycin and its analog are targeted to the HSP90 homolog proteins of pathogenic protozoans Plasmodium falciparum, Leishmania donovani, Trypanosoma brucei and Entamoeba Histolytica.	geldenamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
23533265-2	2013	Here, we show that the Hsp90 inhibitor ganetespib induced loss of EML4-ALK expression and depletion of multiple oncogenic signaling proteins in ALK-driven NSCLC cells, leading to greater in vitro potency, superior antitumor efficacy, and prolonged animal survival compared with results obtained with crizotinib.	STA 9090	39-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23220021-9	2013	Using SVM, several known HCC inhibitors, such as geldanamycin, alvespimycin (HSP90 inhibitors), and doxorubicin (chemotherapy drug), were predicted.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	63-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
23413029-0	2013	Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.	pro-xaa-leu	51-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-113
23413029-0	2013	Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.	Glutamic Acid	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-113
23413029-3	2013	In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif (where Xaa = any amino acid) in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2.	Leucine	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
23413029-3	2013	In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif (where Xaa = any amino acid) in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2.	Leucine	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
23413029-3	2013	In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif (where Xaa = any amino acid) in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2.	Glutamic Acid	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
23413029-3	2013	In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif (where Xaa = any amino acid) in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2.	Glutamic Acid	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
23458665-0	2013	Hsp90 Inhibitor SNX-7081 dysregulates proteins involved with DNA repair and replication and the cell cycle in human chronic lymphocytic leukemia (CLL) cells.	SNX-7081	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23458665-1	2013	The proteomic effects of the Hsp90 inhibitor, SNX-7081, have been determined on the p53-mutated B-cell chronic lymphocytic leukemia (CLL) cell line, MEC1.	SNX-7081	46-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
23458665-8	2013	These data suggest that SNX-7081 arrests the cell cycle and inhibits DNA replication and r epair and provides evidence for the mechanism of the observed synergy between Hsp90 inhibitors and drugs that induce DNA strand breaks.	SNX-7081	24-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
23201460-8	2013	Disulfiram, used to treat alcoholism for half-a century now, is a potent ALDH inhibitor and the old anti-viral drug ritonavir inhibits HSP90.	Disulfiram	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
23201460-8	2013	Disulfiram, used to treat alcoholism for half-a century now, is a potent ALDH inhibitor and the old anti-viral drug ritonavir inhibits HSP90.	Ritonavir	116-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
23533265-2	2013	Here, we show that the Hsp90 inhibitor ganetespib induced loss of EML4-ALK expression and depletion of multiple oncogenic signaling proteins in ALK-driven NSCLC cells, leading to greater in vitro potency, superior antitumor efficacy, and prolonged animal survival compared with results obtained with crizotinib.	Crizotinib	300-310	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23107115-5	2013	We established that a single amino acid exchange in the Leishmania Hsp90 renders that protein resistant to the inhibitor radicicol (RAD), yet does not interfere with its functionality.	monorden	121-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
23107115-9	2013	The CKC strategy we developed will allow the future analysis of more Hsp90 domains and motifs in parasite viability and infectivity.	CKC	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
23561390-0	2013	Re: potential role of hsp90 inhibitors in overcoming Cisplatin resistance of bladder cancer-initiating cells.	Cisplatin	53-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
23520985-1	2013	The design through energy-based pharmacophore virtual screening has led to aminocyanopyridine derivatives as efficacious new inhibitors of Hsp90.	3-Amino-2-pyridinecarbonitrile	75-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
23520985-2	2013	The synthesized compounds showed a good affinity for the Hsp90 ATP binding site in the competitive binding assay.	Adenosine Triphosphate	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
23306136-5	2013	[(18)F]FBA was used for the synthesis of novel thiol-reactive prosthetic group 4-[(18)F]fluorobenzyl)maleimide [(18)F]FBM and Hsp90 inhibitor 17-(4-[(18)F]fluorobenzylamino)-17-demethoxy-geldanamycin [(18)F] GA.	Sulfhydryl Compounds	47-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
23395886-0	2013	Inhibition of HSP90 with AUY922 induces synergy in HER2-amplified trastuzumab-resistant breast and gastric cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	25-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
23511419-0	2013	Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90.	19-substituted geldanamycins	13-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
23511419-1	2013	The benzoquinone ansamycin geldanamycin and its derivatives are inhibitors of heat shock protein Hsp90, an emerging target for novel therapeutic agents both in cancer and in neurodegeneration.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
23511419-1	2013	The benzoquinone ansamycin geldanamycin and its derivatives are inhibitors of heat shock protein Hsp90, an emerging target for novel therapeutic agents both in cancer and in neurodegeneration.	geldanamycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
23511419-5	2013	Protein crystallography established that the new compounds bind to Hsp90 with, as expected, a cis-amide conformation.	cis-amide	94-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
23306136-5	2013	[(18)F]FBA was used for the synthesis of novel thiol-reactive prosthetic group 4-[(18)F]fluorobenzyl)maleimide [(18)F]FBM and Hsp90 inhibitor 17-(4-[(18)F]fluorobenzylamino)-17-demethoxy-geldanamycin [(18)F] GA.	17-(4-[(18)f]fluorobenzylamino)-17-demethoxy-geldanamycin	142-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
23306136-10	2013	[(18)F]FBA was also used as building block for the syntheses of small molecules as exemplified by the preparation of Hsp90 inhibitor 17-(4-[(18)F]fluorobenzylamino)-17-demethoxy-geldanamycin.	17-(4-[(18)f]fluorobenzylamino)-17-demethoxy-geldanamycin	133-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
23418749-9	2013	Furthermore, the proline-rich domain decreased the affinity of AIPL1 for Hsp90, implying that this domain acts as a negative regulator of the Hsp90 interaction besides being necessary for efficient binding of AIPL1 to non-native proteins.	Proline	17-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
23418749-9	2013	Furthermore, the proline-rich domain decreased the affinity of AIPL1 for Hsp90, implying that this domain acts as a negative regulator of the Hsp90 interaction besides being necessary for efficient binding of AIPL1 to non-native proteins.	Proline	17-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
23530663-0	2013	A first in human, safety, pharmacokinetics, and clinical activity phase I study of once weekly administration of the Hsp90 inhibitor ganetespib (STA-9090) in patients with solid malignancies.	STA 9090	133-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
23487751-3	2013	Here, we show that nitration of a single tyrosine residue on a small proportion of 90-kDa heat-shock protein (Hsp90), is sufficient to induce motor neuron death by the P2X7 receptor-dependent activation of the Fas pathway.	Tyrosine	41-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
23364790-10	2013	Furthermore, the HSP90 inhibitor 17-allylaminogeldanamycin sharply decreased the level of aggregated AR in neurons derived from SBMA-iPSCs, indicating a potential for discovery and validation of candidate drugs.	tanespimycin	33-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
23616796-0	2013	Synthesis and evaluation of cell-permeable biotinylated PU-H71 derivatives as tumor Hsp90 probes.	Plutonium	56-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
23616796-2	2013	Here, we present a systematic approach to identify biotinylated analogues of the Hsp90 inhibitor PU-H71 that are capable of permeating cell membranes so as to enable the investigation of Hsp90 complexes in live cells.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
23616796-2	2013	Here, we present a systematic approach to identify biotinylated analogues of the Hsp90 inhibitor PU-H71 that are capable of permeating cell membranes so as to enable the investigation of Hsp90 complexes in live cells.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	187-192
23356405-0	2013	The HSP90 inhibitor NVP-AUY922-AG inhibits the PI3K and IKK signalling pathways and synergizes with cytarabine in acute myeloid leukaemia cells.	Cytarabine	100-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23356405-11	2013	This study shows that the novel HSP90 inhibitor NVP-AUY922-AG has significant single agent activity in AML cells and is synergistic with Ara-C.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	52-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
23356405-11	2013	This study shows that the novel HSP90 inhibitor NVP-AUY922-AG has significant single agent activity in AML cells and is synergistic with Ara-C.	Cytarabine	137-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
23487751-4	2013	Nitrotyrosine at position 33 or 56 stimulates a toxic gain of function that turns Hsp90 into a toxic protein.	3-nitrotyrosine	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
23123171-1	2013	Ansamycins are very effective HSP90 inhibitors that showed significant beneficial effects in the treatment of EAE.	Lactams, Macrocyclic	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
22543587-9	2013	Inhibition of Hsp90 chaperone activity by 17-N-allylamino-17-demethoxygeldanamycin reduces c-Myc protein level.	tanespimycin	42-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
23229511-3	2013	17-Allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90 inhibitor, is currently under evaluation for its anticancer activity in clinical trials.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
23429201-5	2013	MB sensitized melanoma cells to the apoptogenic activity of geldanamycin, an Hsp90 antagonist known to induce the counter-regulatory upregulation of Hsp70 expression underlying cancer cell resistance to geldanamycin chemotherapy.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
23294827-7	2013	Peptides pulled down from this reaction were sequenced and it was determined that biotinylated curcumin bound hsp70, hsp90, 3-phosphoglycerate dehydrogenase, and a beta-actin variant.	Curcumin	95-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
23459302-0	2013	5-Episinuleptolide acetate, a norcembranoidal diterpene from the formosan soft coral Sinularia sp., induces leukemia cell apoptosis through Hsp90 inhibition.	5-episinuleptolide acetate	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
23459302-5	2013	Additionally, the expression levels of Hsp90 protein and several client proteins were downregulated in response to 5EPA treatment.	5epa	115-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
23219559-0	2013	Interaction of cepharanthine with immobilized heat shock protein 90alpha (Hsp90alpha) and screening of Hsp90alpha inhibitors.	cepharanthine	15-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-84
23219559-1	2013	Heat shock protein 90alpha (Hsp90alpha) immobilized on aminopropyl silica gels was prepared via the N- or C-terminal, which was termed Hsp90alpha-NT or Hsp90alpha-CT, respectively.	aminopropyl silica	55-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-38
23219559-1	2013	Heat shock protein 90alpha (Hsp90alpha) immobilized on aminopropyl silica gels was prepared via the N- or C-terminal, which was termed Hsp90alpha-NT or Hsp90alpha-CT, respectively.	aminopropyl silica	55-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-145
23219559-1	2013	Heat shock protein 90alpha (Hsp90alpha) immobilized on aminopropyl silica gels was prepared via the N- or C-terminal, which was termed Hsp90alpha-NT or Hsp90alpha-CT, respectively.	aminopropyl silica	55-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-145
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	biscoclaurine alkaloids	24-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	cepharanthine	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	berbamine	70-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	berbamine	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	tetrandrine	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	cycleanine	113-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-2	2013	Binding interactions of biscoclaurine alkaloids (cepharanthine (CEP), berbamine (BBM), isotetrandrine (ITD), and cycleanine (CCN)) with Hsp90alpha were examined using the Hsp90alpha-NT or -CT columns by frontal and zonal chromatography studies.	cycleanine	125-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-146
23219559-3	2013	The dissociation constants of CEP, BBM, ITD, and CCN to Hsp90alpha-NT were estimated to be 5.3, 18.6, 46.3, and 159 muM, respectively, by frontal chromatography techniques.	cepharanthine	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
23219559-3	2013	The dissociation constants of CEP, BBM, ITD, and CCN to Hsp90alpha-NT were estimated to be 5.3, 18.6, 46.3, and 159 muM, respectively, by frontal chromatography techniques.	cycleanine	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-66
23219559-5	2013	These data suggest that these biscoclaurine alkaloids interact with the middle domain of Hsp90alpha.	biscoclaurine alkaloids	30-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-99
23015227-5	2013	Further, perifosine inhibits survivin expression probably by disrupting its association with heat shock protein-90 (HSP-90).	perifosine	9-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-114
23015227-5	2013	Further, perifosine inhibits survivin expression probably by disrupting its association with heat shock protein-90 (HSP-90).	perifosine	9-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-122
22934946-7	2013	As an illustration, we describe the results of a cellbased study of the cytotoxicity of 24 analogs of novobiocin, a C-terminal inhibitor of heat shock protein 90 (Hsp90); the compounds were ranked in order of cytotoxicity to a panel of 18 cancer cell lines and 1 normal cell line.	Novobiocin	102-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
22934946-7	2013	As an illustration, we describe the results of a cellbased study of the cytotoxicity of 24 analogs of novobiocin, a C-terminal inhibitor of heat shock protein 90 (Hsp90); the compounds were ranked in order of cytotoxicity to a panel of 18 cancer cell lines and 1 normal cell line.	Novobiocin	102-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
23123171-3	2013	In the present study we have characterized the anti-inflammatory properties of a novel HSP90 inhibitor, PU-H71, and tested its effects in EAE.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
23359685-5	2013	In addition, small molecule inhibitors of Hsp90 and Hsp70 reversibly disrupt purinosomes and are shown to have a synergistic effect with methotrexate, an anticancer agent that targets purine biosynthesis.	Methotrexate	137-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23359685-5	2013	In addition, small molecule inhibitors of Hsp90 and Hsp70 reversibly disrupt purinosomes and are shown to have a synergistic effect with methotrexate, an anticancer agent that targets purine biosynthesis.	purine	184-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23359685-6	2013	These data implicate the Hsp90/Hsp70 chaperone machinery in the assembly of the purinosome and provide a strategy for the development of improved anticancer therapies that disrupt purine biosynthesis.	purine	180-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
23394616-3	2013	METHODS: In this study, we have investigated the effects of geldanamycin on the regulation of Hsp90-dependent oncogenic signaling pathways directly implicated in cell cycle progression, survival and motility of human urinary bladder cancer cells.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
23394616-6	2013	Furthermore, geldanamycin administration proved to induce prominent downregulation of several Hsp90 protein clients and downstream effectors, such as membrane receptors (IGF-IR and c-Met), protein kinases (Akt, IKKalpha, IKKbeta and Erk1/2) and transcription factors (FOXOs and NF-kappaBeta), therefore resulting in the impairment of proliferative -oncogenic- signaling and reduction of cell motility.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
23394616-7	2013	CONCLUSIONS: In toto, we have evinced the dose-dependent and cell line-specific actions of geldanamycin on cell cycle progression, survival and motility of human bladder cancer cells, due to downregulation of critical Hsp90 clients and subsequent disruption of signaling -oncogenic- integrity.	geldanamycin	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	218-223
23196876-5	2013	In this study, we demonstrated that NVP-AUY922 (AUY922), a new class of HSP90AA1 inhibitor, is effective in inhibiting the growth of GIST cells expressing mutant KIT protein, the imatinib-sensitive GIST882 and imatinib-resistant GIST48 cells.	Imatinib Mesylate	179-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-80
23252346-7	2013	Importantly, the apoptotic effects of the HSP90 inhibitor NVP-AUY922 or the proteasome inhibitor bortezomib were strongly enhanced in combination with triptolide, suggesting a salvage role of HSF1-dependent HSP induction in response to drug treatment.	triptolide	151-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	tanespimycin	39-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	tanespimycin	79-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	Arsenic Trioxide	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	Sirolimus	133-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	tanespimycin	192-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	Arsenic Trioxide	202-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23255002-6	2013	We also found that the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) or arsenic trioxide (ATO) in combination with rapamycin markedly inhibited the growth of MCF-7 cells and 17-AAG or ATO suppressed rapamycin-induced phosphorylation of Akt.	Sirolimus	217-226	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23443787-0	2013	[Effects of HSP90 inhibitor 17-AAG on cell cycle and apoptosis of human gastric cancer cell lines SGC-7901].	tanespimycin	28-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
23443787-1	2013	OBJECTIVE: To study the effect of the HSP90 inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), on cell proliferation and apoptosis of human cancer SGC-7901 cells and explore the mechanisms.	tanespimycin	55-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
23443787-1	2013	OBJECTIVE: To study the effect of the HSP90 inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), on cell proliferation and apoptosis of human cancer SGC-7901 cells and explore the mechanisms.	tanespimycin	95-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
22898035-2	2013	BIIB021 is an oral non-ansamycin HSP90 inhibitor.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
23469976-1	2013	UNLABELLED: AIMS, MATERIALS &amp; METHODS: As heat-shock proteins are associated with tumor proliferation, differentiation, invasion and metastasis, we investigated whether targeting Hsp90 with the geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17AAG) can inhibit the viability of hepatocellular carcinoma cell lines with various levels of metastatic potential.	geldanamycin	198-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
23469976-6	2013	CONCLUSION: 17AAG inhibited the viability of hepatocellular carcinoma cells by degrading Hsp90 client proteins.	tanespimycin	12-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22810956-5	2013	RESULTS: Two HSP90 inhibitors, 17-AAG (tanespimycin) and the synthetic diarylisoxazole amide resorcinol NVP-AUY922, demonstrated potent antiproliferative activity in in vitro studies.	tanespimycin	31-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22810956-5	2013	RESULTS: Two HSP90 inhibitors, 17-AAG (tanespimycin) and the synthetic diarylisoxazole amide resorcinol NVP-AUY922, demonstrated potent antiproliferative activity in in vitro studies.	tanespimycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22810956-5	2013	RESULTS: Two HSP90 inhibitors, 17-AAG (tanespimycin) and the synthetic diarylisoxazole amide resorcinol NVP-AUY922, demonstrated potent antiproliferative activity in in vitro studies.	diarylisoxazole amide	71-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22810956-5	2013	RESULTS: Two HSP90 inhibitors, 17-AAG (tanespimycin) and the synthetic diarylisoxazole amide resorcinol NVP-AUY922, demonstrated potent antiproliferative activity in in vitro studies.	resorcinol	93-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
23234644-2	2013	Novobiocin is the first Hsp90 C-terminal inhibitor ever identified and recent structure-activity relationship studies on the noviose sugar identified several commercially available amines as suitable surrogates.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
22982986-10	2013	The HAX-1 regulation was further supported by loss of IRE-1 inhibition in presence of the Hsp90 inhibitor, 17-N-allylamino-17-demethoxygeldanamycin.	tanespimycin	107-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
23878583-5	2013	Mycograb is a human recombinant monoclonal antibody against heat shock protein 90 (Hsp90) that was revealed to have synergy when combined with fluconazole, caspofungin, and amphotericin B against a broad spectrum of Candida species.	Fluconazole	143-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
23878583-5	2013	Mycograb is a human recombinant monoclonal antibody against heat shock protein 90 (Hsp90) that was revealed to have synergy when combined with fluconazole, caspofungin, and amphotericin B against a broad spectrum of Candida species.	Caspofungin	156-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
23878583-5	2013	Mycograb is a human recombinant monoclonal antibody against heat shock protein 90 (Hsp90) that was revealed to have synergy when combined with fluconazole, caspofungin, and amphotericin B against a broad spectrum of Candida species.	Caspofungin	156-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
23878583-5	2013	Mycograb is a human recombinant monoclonal antibody against heat shock protein 90 (Hsp90) that was revealed to have synergy when combined with fluconazole, caspofungin, and amphotericin B against a broad spectrum of Candida species.	Amphotericin B	173-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
23878583-5	2013	Mycograb is a human recombinant monoclonal antibody against heat shock protein 90 (Hsp90) that was revealed to have synergy when combined with fluconazole, caspofungin, and amphotericin B against a broad spectrum of Candida species.	Amphotericin B	173-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
23878583-6	2013	Furthermore, recent studies have established an important role for Hsp90 in mediating Candida resistance to echinocandins, giving to this antibody molecule even more attractive biological properties.	Echinocandins	108-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
23123171-0	2013	The novel HSP90 inhibitor, PU-H71, suppresses glial cell activation but weakly affects clinical signs of EAE.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
23878583-5	2013	Mycograb is a human recombinant monoclonal antibody against heat shock protein 90 (Hsp90) that was revealed to have synergy when combined with fluconazole, caspofungin, and amphotericin B against a broad spectrum of Candida species.	Fluconazole	143-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
23445811-3	2013	Based on studies of the past few years, we argue that the selected sensitivity of cancer cells to Hsp90 inhibitors, such as 17-N-allylamino-17-demethoxygeldanamycin, is due to inhibition of the extracellular Hsp90 (eHsp90) rather than intracellular Hsp90 by these inhibitors.	tanespimycin	124-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
22920900-2	2013	Among the characterized HSPs, the molecular chaperone HSP90 has emerged as an exciting molecular target for cancer therapy since its discovery as the target protein of the antibiotic geldanamycin.	geldanamycin	183-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
22920906-9	2013	Hsp90 and its co-chaperones are required for the function of these tumor-promoting client proteins; therefore, inhibition of Hsp90 by specific inhibitors such as geldanamycin and its derivatives attenuates the tumor progression.	geldanamycin	162-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22920906-9	2013	Hsp90 and its co-chaperones are required for the function of these tumor-promoting client proteins; therefore, inhibition of Hsp90 by specific inhibitors such as geldanamycin and its derivatives attenuates the tumor progression.	geldanamycin	162-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
22920907-1	2013	Heat shock protein (Hsp) 90 is an ATP-dependent molecular chaperone which stabilizes various oncogenic kinases, including HER2, EGFR, BCR-ABL, B-Raf and EML4-ALK, which are essential for tumor growth.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-27
22920907-3	2013	Previous reports have shown that many oncogenic proteins essential for cancer transformation are chaperoned by the Hsp90 complex, and some of these client proteins have been discovered by using Hsp90 inhibitors, such as geldanamycin (GA) and radicicol (RD).Thus far more than 200 client proteins have been identified.	geldanamycin	220-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
22920907-3	2013	Previous reports have shown that many oncogenic proteins essential for cancer transformation are chaperoned by the Hsp90 complex, and some of these client proteins have been discovered by using Hsp90 inhibitors, such as geldanamycin (GA) and radicicol (RD).Thus far more than 200 client proteins have been identified.	geldanamycin	220-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
22920907-3	2013	Previous reports have shown that many oncogenic proteins essential for cancer transformation are chaperoned by the Hsp90 complex, and some of these client proteins have been discovered by using Hsp90 inhibitors, such as geldanamycin (GA) and radicicol (RD).Thus far more than 200 client proteins have been identified.	monorden	242-251	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
22920907-3	2013	Previous reports have shown that many oncogenic proteins essential for cancer transformation are chaperoned by the Hsp90 complex, and some of these client proteins have been discovered by using Hsp90 inhibitors, such as geldanamycin (GA) and radicicol (RD).Thus far more than 200 client proteins have been identified.	monorden	242-251	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
24228063-5	2013	Moreover, CSEE treatments significantly reversed heat shock protein expression in heat-stressed HSP47-transformed cells (42 C, for 90 min) and mRNA expression of HSP27 and HSP90 in H2O2-treated SH-SY5Y.	Hydrogen Peroxide	181-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
23840275-0	2013	HSP90 Inhibitors, Geldanamycin and Radicicol, Enhance Fisetin-Induced Cytotoxicity via Induction of Apoptosis in Human Colonic Cancer Cells.	fisetin	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23445811-3	2013	Based on studies of the past few years, we argue that the selected sensitivity of cancer cells to Hsp90 inhibitors, such as 17-N-allylamino-17-demethoxygeldanamycin, is due to inhibition of the extracellular Hsp90 (eHsp90) rather than intracellular Hsp90 by these inhibitors.	tanespimycin	124-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-213
23445811-3	2013	Based on studies of the past few years, we argue that the selected sensitivity of cancer cells to Hsp90 inhibitors, such as 17-N-allylamino-17-demethoxygeldanamycin, is due to inhibition of the extracellular Hsp90 (eHsp90) rather than intracellular Hsp90 by these inhibitors.	tanespimycin	124-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-213
22936006-6	2013	Interestingly, the activity of the proteasome was enhanced by geldanamycin, a natural inhibitor of Hsp90.	geldanamycin	62-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
23710334-2	2013	Previously, we have demonstrated that a quinone-based mimetic dipeptide, named DTNQ-Pro, induced differentiation of growing Caco-2 cells through inhibition of HSP70 and HSP90.	quinone	40-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
23114515-5	2013	The hsp90 inhibitors 17-AAG and radicicol nevertheless caused a dose-dependent reduction in total human tau levels in transgenic larvae without specifically altering tau hyperphosphorylated at S396/S404.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23114515-5	2013	The hsp90 inhibitors 17-AAG and radicicol nevertheless caused a dose-dependent reduction in total human tau levels in transgenic larvae without specifically altering tau hyperphosphorylated at S396/S404.	monorden	32-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23710334-2	2013	Previously, we have demonstrated that a quinone-based mimetic dipeptide, named DTNQ-Pro, induced differentiation of growing Caco-2 cells through inhibition of HSP70 and HSP90.	Dipeptides	62-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
23710334-2	2013	Previously, we have demonstrated that a quinone-based mimetic dipeptide, named DTNQ-Pro, induced differentiation of growing Caco-2 cells through inhibition of HSP70 and HSP90.	(3,3')spiro((hexahydropyrrolo(1,2-a)pyrazine-1,4-dione)-6,3'-(2',3'-dihydrothieno(2,3-b)naphtho-4',9'-dione))	79-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
24220679-5	2013	The heat-shock protein (HSP)-90 inhibitor 17-AAG prevents ROS-induced TDP-43 aggregation, alters the type of TDP-43 multimers and reduces the severity of pathological TDP-43 inclusions.	Reactive Oxygen Species	58-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-31
23613388-0	2013	Metformin inhibits proliferation and promotes apoptosis of HER2 positive breast cancer cells by downregulating HSP90.	Metformin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
23613388-8	2013	The expression level of HSP90 in the metformin group was significantly lower than that in the control group.	Metformin	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
23613388-9	2013	CONCLUSION: Metformin can inhibit the proliferation and promote apoptosis of HER2 positive breast cancer cells,which is maybe related to inhibition of HSP90.	Metformin	12-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
23475677-3	2013	Noncovalent affinity capture with a biotinyl analog of the HSP90 inhibitor geldanamycin enables detection of the native protein isoforms Hsp90alpha and Hsp90beta and their phosphorylated forms.	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
23475677-3	2013	Noncovalent affinity capture with a biotinyl analog of the HSP90 inhibitor geldanamycin enables detection of the native protein isoforms Hsp90alpha and Hsp90beta and their phosphorylated forms.	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-147
23475677-4	2013	We applied this probe to map and quantify adducts formed on Hsp90 by 4-hydroxynonenal (HNE) in RKO cells.	4-hydroxy-2-nonenal	69-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
23475677-4	2013	We applied this probe to map and quantify adducts formed on Hsp90 by 4-hydroxynonenal (HNE) in RKO cells.	4-hydroxy-2-nonenal	87-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
23154999-0	2013	The HSP90 inhibitor geldanamycin perturbs endosomal structure and drives recycling ErbB2 and transferrin to modified MVBs/lysosomal compartments.	geldanamycin perturbs	20-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23229893-13	2013	SUMO-1 labelling of lysosomes showed a major increase between 24 and 48 h post-incubation of 1321N1 cells with MG132 resulting in an increase in a 90 kDa SUMO-1-positive band that was immunopositive for Hsp90 and immunoprecipitated with an anti-SUMO-1 antibody.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	111-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
23555724-6	2013	In contrast, expression levels of the cytosolic chaperones HSP90 and HSP71 were down-regulated in the azacytidine-treated monocytes, concomitant with an increase in the levels of these chaperones in the cell culture medium.	Azacitidine	102-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	Capsaicin	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	Capsaicin	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	Capsaicin	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	Capsaicin	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	114-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	114-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	114-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	114-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23468922-4	2013	We found in various non-cancerous and cancerous mammalian epithelial cells that the TRPV1 agonists, capsaicin and resiniferatoxin (RTX), upregulated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70 and Hsp90 respectively, while the TRPV1 antagonists, capsazepine and AMG-9810, attenuated the accumulation of Hsp70, Hsp90 and Hsp27 and Hsp70, Hsp90, respectively.	resiniferatoxin	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
23144451-5	2012	Specifically, knockdown of Hsp60 resulted in a decrease in complex IV activity, whereas antagonistic inhibition of Hsp90 by 17-(allylamino) geldanamycin decreased both Hsp60 and complex IV activity.	tanespimycin	124-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
23144451-8	2012	Drug screening identified ginsenoside Re as a compound capable of reversing the deficit in complex IV activity in PINK1 null cells through specific increases of LRPPRC, Hsp90, and Hsp60 levels.	Ginsenosides	26-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
23144451-11	2012	Furthermore, they demonstrate that treatment with ginsenoside Re enhances functioning of the defective PINK1-Hsp90/LRPPRC-Hsp60-complex IV signaling axis in PINK1 null neurons by restoring NO levels, providing potential for new therapeutics targeting mitochondrial dysfunction in Parkinson"s disease.	Ginsenosides	50-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
23152004-0	2013	Potent activity of the Hsp90 inhibitor ganetespib in prostate cancer             cells irrespective of androgen receptor status or variant receptor expression.	STA 9090	39-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
23152004-5	2013	Here, we examined the preclinical activity of ganetespib,             a small molecule inhibitor of Hsp90, in a panel of prostate cancer cell lines.	STA 9090	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
22566192-6	2013	On the basis of these results, we have treated both parental and HSP90-transfected cells with a HSP90 inhibitor geldanamycin (GA).	geldanamycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
22566192-6	2013	On the basis of these results, we have treated both parental and HSP90-transfected cells with a HSP90 inhibitor geldanamycin (GA).	geldanamycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
22566192-6	2013	On the basis of these results, we have treated both parental and HSP90-transfected cells with a HSP90 inhibitor geldanamycin (GA).	geldanamycin	126-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
22566192-6	2013	On the basis of these results, we have treated both parental and HSP90-transfected cells with a HSP90 inhibitor geldanamycin (GA).	geldanamycin	126-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
23135731-5	2013	The chemosensitivity to cisplatin of the cell was also tested by FACS when HSP90AA1 was overexpressed.	Cisplatin	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-83
23135731-7	2013	Furthermore, overexpression of HSP90AA1 decreased the chemosensitivity to cisplatin of SKOV3 cells and overexpression of HSP90AA1 could partially rescue the survival rate of SKOV3 cells which were treated with cisplatin.	Cisplatin	74-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-39
23135731-7	2013	Furthermore, overexpression of HSP90AA1 decreased the chemosensitivity to cisplatin of SKOV3 cells and overexpression of HSP90AA1 could partially rescue the survival rate of SKOV3 cells which were treated with cisplatin.	Cisplatin	210-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-39
23135731-7	2013	Furthermore, overexpression of HSP90AA1 decreased the chemosensitivity to cisplatin of SKOV3 cells and overexpression of HSP90AA1 could partially rescue the survival rate of SKOV3 cells which were treated with cisplatin.	Cisplatin	210-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-129
23135731-9	2013	High level of HSP90AA1 can increase chemoresistance to cisplatin of SKOV3 cells.	Cisplatin	55-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-22
23154999-2	2013	HSP90 inhibitors, such as geldanamycin (GA), have been developed to target the receptor to degradation or to modulate downstream signaling.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23154999-2	2013	HSP90 inhibitors, such as geldanamycin (GA), have been developed to target the receptor to degradation or to modulate downstream signaling.	geldanamycin	40-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23457505-4	2013	Both the first generation, natural product Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin), and the second-generation synthetic Hsp90 inhibitor STA-9090 (ganetespib) demonstrated potent inhibition of proliferation and migration of pheochromocytoma cell lines and induced degradation of key Hsp90 clients.	tanespimycin	59-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
23418523-0	2013	Activity of the heat shock protein 90 inhibitor ganetespib in melanoma.	STA 9090	48-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
23418523-2	2013	Ganetespib is a potent ATP competitive inhibitor of HSP90.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
23418523-2	2013	Ganetespib is a potent ATP competitive inhibitor of HSP90.	Adenosine Triphosphate	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
23418523-8	2013	HSP90 is functionally important for melanoma cells and HSP90 inhibitors such as ganetespib could potentially be effective therapeutics for melanoma with various genetic mutations and acquired resistance to B-RAF inhibition.	STA 9090	80-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23418523-8	2013	HSP90 is functionally important for melanoma cells and HSP90 inhibitors such as ganetespib could potentially be effective therapeutics for melanoma with various genetic mutations and acquired resistance to B-RAF inhibition.	STA 9090	80-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
22955504-5	2013	As with many of the other classes of molecular chaperone, Hsp90 has a critical ATPase activity, and ATP binding and hydrolysis known to modulate the conformational dynamics of the protein.	Adenosine Triphosphate	79-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
23147571-1	2013	Previous studies have reported that a Gamitrinib variant containing triphenylphosphonium (G-TPP) binds to mitochondrial Hsp90 and rapidly inhibits its activity, thus inducing the apoptotic pathway in the cells.	Gamitrinib	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
23147571-1	2013	Previous studies have reported that a Gamitrinib variant containing triphenylphosphonium (G-TPP) binds to mitochondrial Hsp90 and rapidly inhibits its activity, thus inducing the apoptotic pathway in the cells.	3-(bromopropyl)triphenylphosphonium	68-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
23147571-1	2013	Previous studies have reported that a Gamitrinib variant containing triphenylphosphonium (G-TPP) binds to mitochondrial Hsp90 and rapidly inhibits its activity, thus inducing the apoptotic pathway in the cells.	UNII-M6LC47TUG3	90-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	geldanamycin	105-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	geldanamycin	105-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	tanespimycin	118-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	tanespimycin	118-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	Gallium	160-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	Gallium	160-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	tanespimycin	163-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
23256568-4	2012	This study aims to demonstrate that inhibition of the heat shock protein 90 (Hsp90) either by inhibitors geldanamycin/17-N-Allylamino-17-demethoxygeldanamycin (GA/17-AAG) or siRNA technique in human lung cancer cells induces c-FLIPL degradation and cellular apoptosis through C-terminus of Hsp70-interacting protein (CHIP)-mediated mechanisms.	tanespimycin	163-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
23018093-0	2012	Targeting conserved water molecules: design of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine Hsp90 inhibitors using fragment-based screening and structure-based optimization.	Water	20-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
23186287-3	2012	Our initial studies confirmed that deguelin disrupts ATP binding to HSP90 and consequently induces destabilization of its client proteins such as HIF-1alpha.	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
22227828-0	2012	Synergistic activity of the Hsp90 inhibitor ganetespib with taxanes in non-small cell lung cancer models.	STA 9090	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
22227828-0	2012	Synergistic activity of the Hsp90 inhibitor ganetespib with taxanes in non-small cell lung cancer models.	Taxoids	60-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
22227828-4	2012	Ganetespib is a non-ansamycin inhibitor of Hsp90 currently under clinical evaluation in a number of human malignancies, including NSCLC.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
22227828-9	2012	Our data suggest that the improved therapeutic indices are likely to be mechanistically multifactorial, including loss of pro-survival signaling and direct cell cycle effects resulting from Hsp90 modulation by ganetespib.	STA 9090	210-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
23063542-11	2012	The results demonstrated that Tan IIA restored eNOS uncoupling induced by high glucose by targeting NADPH oxidase, HSP90, GTPCH1 and DHFR, and PI3K pathway, which leads to reduced intracellular oxidative stress and increased NO generation.	Glucose	79-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
23023377-5	2012	Elevated reactive oxygen species production in obese (db/db) aorta was suppressed by Hsp90 inhibition.	Reactive Oxygen Species	9-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
23069143-3	2012	This study investigated the role of Rad51 expression in HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG)-induced cytotoxicity in two NSCLC cell lines, A549 and H1975.	tanespimycin	72-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
23069143-3	2012	This study investigated the role of Rad51 expression in HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG)-induced cytotoxicity in two NSCLC cell lines, A549 and H1975.	tanespimycin	112-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
23069143-4	2012	The 17-AAG treatment decreased cellular Rad51 protein and mRNA levels and phosphorylated MKK1/2-ERK1/2 protein levels, and disrupted the HSP90 and Rad51 interaction.	tanespimycin	4-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
23018093-0	2012	Targeting conserved water molecules: design of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine Hsp90 inhibitors using fragment-based screening and structure-based optimization.	4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine	47-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
23018093-2	2012	Here we describe a series of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine ATP competitive Hsp90 inhibitors that were identified following structure-driven optimization of purine hits revealed by NMR based screening of a proprietary fragment library.	4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
23018093-2	2012	Here we describe a series of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine ATP competitive Hsp90 inhibitors that were identified following structure-driven optimization of purine hits revealed by NMR based screening of a proprietary fragment library.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
23018093-2	2012	Here we describe a series of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine ATP competitive Hsp90 inhibitors that were identified following structure-driven optimization of purine hits revealed by NMR based screening of a proprietary fragment library.	purine	165-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
23018093-3	2012	Ligand-Hsp90 X-ray structures combined with molecular modeling led to the rational displacement of a conserved water molecule leading to enhanced affinity for Hsp90 as measured by fluorescence polarization, isothermal titration calorimetry and surface plasmon resonance assays.	Water	111-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	7-12
23018093-3	2012	Ligand-Hsp90 X-ray structures combined with molecular modeling led to the rational displacement of a conserved water molecule leading to enhanced affinity for Hsp90 as measured by fluorescence polarization, isothermal titration calorimetry and surface plasmon resonance assays.	Water	111-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
23018093-7	2012	This work demonstrates the power of structure-based design for the rapid evolution of potent Hsp90 inhibitors and the importance of considering conserved water molecules in drug design.	Water	154-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
23330093-0	2012	Dependence of blood levels of HSP70 and HSP90 on genotypes of HSP70, GSTT1, and GSTM1 gene polymorphism in individuals chronically exposed to mercury.	Mercury	142-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
23212626-0	2012	Recent updates on the development of ganetespib as a Hsp90 inhibitor.	STA 9090	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
23212626-2	2012	Ganetespib (STA-9090) is a potent, synthetic, small molecule inhibitor of Hsp90, and its binding to Hsp90 is known to result in the degradation of its client proteins and subsequent death of cancer cells.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
23212626-2	2012	Ganetespib (STA-9090) is a potent, synthetic, small molecule inhibitor of Hsp90, and its binding to Hsp90 is known to result in the degradation of its client proteins and subsequent death of cancer cells.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
23212626-2	2012	Ganetespib (STA-9090) is a potent, synthetic, small molecule inhibitor of Hsp90, and its binding to Hsp90 is known to result in the degradation of its client proteins and subsequent death of cancer cells.	xylometazoline	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
23212626-2	2012	Ganetespib (STA-9090) is a potent, synthetic, small molecule inhibitor of Hsp90, and its binding to Hsp90 is known to result in the degradation of its client proteins and subsequent death of cancer cells.	xylometazoline	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
23212626-3	2012	This article provides a review of ganetespib as one of the leading Hsp90 inhibitors, which is under investigation in a broad range of clinical stages for the treatment of cancer.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
23350198-2	2012	It was found that nanomolar concentrations of inhibitors of the HSP90 activity (17AAG or radicicol) slowed down chaperone-dependent reactivation of a thermo-labile reporter (luciferase) in heat-stressed HeLa cells and slightly enhanced their death following incubation for 60 min at 43 degrees C. Herein, the inhibitors of HSP90 activity stimulated de novo induction of additional chaperones (HSP70 and HSP27) that significantly increased the intracellular HSP levels.	tanespimycin	80-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
23350198-2	2012	It was found that nanomolar concentrations of inhibitors of the HSP90 activity (17AAG or radicicol) slowed down chaperone-dependent reactivation of a thermo-labile reporter (luciferase) in heat-stressed HeLa cells and slightly enhanced their death following incubation for 60 min at 43 degrees C. Herein, the inhibitors of HSP90 activity stimulated de novo induction of additional chaperones (HSP70 and HSP27) that significantly increased the intracellular HSP levels.	tanespimycin	80-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	323-328
23350198-2	2012	It was found that nanomolar concentrations of inhibitors of the HSP90 activity (17AAG or radicicol) slowed down chaperone-dependent reactivation of a thermo-labile reporter (luciferase) in heat-stressed HeLa cells and slightly enhanced their death following incubation for 60 min at 43 degrees C. Herein, the inhibitors of HSP90 activity stimulated de novo induction of additional chaperones (HSP70 and HSP27) that significantly increased the intracellular HSP levels.	monorden	89-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
23350198-2	2012	It was found that nanomolar concentrations of inhibitors of the HSP90 activity (17AAG or radicicol) slowed down chaperone-dependent reactivation of a thermo-labile reporter (luciferase) in heat-stressed HeLa cells and slightly enhanced their death following incubation for 60 min at 43 degrees C. Herein, the inhibitors of HSP90 activity stimulated de novo induction of additional chaperones (HSP70 and HSP27) that significantly increased the intracellular HSP levels.	monorden	89-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	323-328
23350198-3	2012	If the cells were treated with 17AAG or radicicol along with an inhibitor of the HSP induction (e.g. quercetin or triptolid, or NZ28), this fully prevented the increase in intracellular chaperone levels resulting from the inhibition of HSP90 activity and subsequent heating.	tanespimycin	31-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
23350198-3	2012	If the cells were treated with 17AAG or radicicol along with an inhibitor of the HSP induction (e.g. quercetin or triptolid, or NZ28), this fully prevented the increase in intracellular chaperone levels resulting from the inhibition of HSP90 activity and subsequent heating.	monorden	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
23350198-3	2012	If the cells were treated with 17AAG or radicicol along with an inhibitor of the HSP induction (e.g. quercetin or triptolid, or NZ28), this fully prevented the increase in intracellular chaperone levels resulting from the inhibition of HSP90 activity and subsequent heating.	Quercetin	101-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
23350198-3	2012	If the cells were treated with 17AAG or radicicol along with an inhibitor of the HSP induction (e.g. quercetin or triptolid, or NZ28), this fully prevented the increase in intracellular chaperone levels resulting from the inhibition of HSP90 activity and subsequent heating.	triptolide	114-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
23350198-3	2012	If the cells were treated with 17AAG or radicicol along with an inhibitor of the HSP induction (e.g. quercetin or triptolid, or NZ28), this fully prevented the increase in intracellular chaperone levels resulting from the inhibition of HSP90 activity and subsequent heating.	nz28	128-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
22843495-3	2012	We show that inhibition of Hsp90 with geldanamycin (GD) destabilizes Cdc25A independent of Chk1/2, whereas the standard drug for pancreas carcinoma treatment, gemcitabine (GEM), causes Cdc25A degradation through the activation of Chk2.	geldanamycin	38-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22562379-8	2012	Bortezomib-mediated immunogenic apoptosis, characterized by elevated surface expression of hsp90, triggered higher phagocytosis of U266 cells by DCs involving specific DC-derived receptors.	Bortezomib	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
22843495-3	2012	We show that inhibition of Hsp90 with geldanamycin (GD) destabilizes Cdc25A independent of Chk1/2, whereas the standard drug for pancreas carcinoma treatment, gemcitabine (GEM), causes Cdc25A degradation through the activation of Chk2.	geldanamycin	52-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22843495-3	2012	We show that inhibition of Hsp90 with geldanamycin (GD) destabilizes Cdc25A independent of Chk1/2, whereas the standard drug for pancreas carcinoma treatment, gemcitabine (GEM), causes Cdc25A degradation through the activation of Chk2.	gemcitabine	159-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22843495-3	2012	We show that inhibition of Hsp90 with geldanamycin (GD) destabilizes Cdc25A independent of Chk1/2, whereas the standard drug for pancreas carcinoma treatment, gemcitabine (GEM), causes Cdc25A degradation through the activation of Chk2.	gemcitabine	172-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22843495-5	2012	The role of Hsp90 as stabilizer of Cdc25A in pancreas carcinoma cells is further supported by two novel synthetic inhibitors 4-tosylcyclonovobiocic acid and 7-tosylcyclonovobiocic acid and specific Hsp90AB1 (Hsp90beta) shRNA.	4-tosylcyclonovobiocic acid	125-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
22843495-5	2012	The role of Hsp90 as stabilizer of Cdc25A in pancreas carcinoma cells is further supported by two novel synthetic inhibitors 4-tosylcyclonovobiocic acid and 7-tosylcyclonovobiocic acid and specific Hsp90AB1 (Hsp90beta) shRNA.	7-tosylcyclonovobiocic acid	157-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
22843495-6	2012	Our data show that targeting Hsp90 reduced the resistance of pancreas carcinoma cells to treatment with GEM.	gemcitabine	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
22888115-3	2012	The C-terminal NP-repeat domain of Tic40 (Tic40-NP) is homologous to the DP-repeat domain of co-chaperones Hsp70-interacting and Hsp70/Hsp90-organizing proteins.	dp	73-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
23012248-0	2012	Targeting KRAS-mutant non-small cell lung cancer with the Hsp90 inhibitor ganetespib.	STA 9090	74-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
23012248-4	2012	Here, we examined the activity of ganetespib, a small-molecule inhibitor of Hsp90 currently in clinical trials for NSCLCs in a panel of lung cancer cell lines harboring a diverse spectrum of KRAS mutations.	STA 9090	34-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
22707278-2	2012	Towards this end, we docked 83 diverse Hsp90alpha inhibitors into the ATP-binding site of this chaperone using several docking-scoring settings.	Adenosine Triphosphate	70-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-49
22707278-6	2012	The optimal dbCICA models were translated into valid pharmacophore models that were used as 3D search queries to mine the National Cancer Institute"s structural database for new inhibitors of Hsp90alpha that could potentially be used as anticancer agents.	dbcica	12-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	192-202
22964853-5	2012	In TGF-beta1-treated HK2 cells and unilateral ureteral obstruction (UUO) kidneys, we found that 17-allylamino-17-demethoxygeldanamycin (17AAG), an Hsp90 inhibitor, decreased the expression of alpha-smooth muscle actin, fibronectin, and collagen I and largely restored the expression of E-cadherin.	tanespimycin	96-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
22964853-9	2012	Furthermore, 17AAG blocked the interaction between Hsp90 and TGF-beta type II receptor (TbetaRII) and promoted ubiquitination of TbetaRII, leading to the decreased availability of TbetaRII.	tanespimycin	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
22865487-0	2012	18beta-glycyrrhetinic acid potentiates Hsp90 inhibition-induced apoptosis in human epithelial ovarian carcinoma cells via activation of death receptor and mitochondrial pathway.	18alpha-glycyrrhetinic acid	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
22865487-6	2012	18beta-Glycyrrhetinic acid enhanced Hsp90 inhibitor-induced apoptosis-related protein activation, nuclear damage, and cell death.	18alpha-glycyrrhetinic acid	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
22865487-7	2012	The results suggest that 18beta-glycyrrhetinic acid may potentiate the Hsp90 inhibition-induced apoptosis in ovarian carcinoma cell lines via the activation of the caspase-8- and Bid-dependent pathways and the mitochondria-mediated cell death pathway, leading to activation of caspases.	18alpha-glycyrrhetinic acid	25-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
22869587-8	2012	Most strikingly, hydralazine selectively boosted the levels of cytoskeletal-associated Hsp90, including a high-mass species that was sensitive to the Hsp90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin.	Hydralazine	17-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
22646928-0	2012	Heat shock protein-90 inhibitor, NVP-AUY922, is effective in combination with fludarabine against chronic lymphocytic leukemia cells cultured on CD40L-stromal layer and inhibits their activated/proliferative phenotype.	fludarabine	78-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
22869587-8	2012	Most strikingly, hydralazine selectively boosted the levels of cytoskeletal-associated Hsp90, including a high-mass species that was sensitive to the Hsp90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin.	Hydralazine	17-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
22869587-8	2012	Most strikingly, hydralazine selectively boosted the levels of cytoskeletal-associated Hsp90, including a high-mass species that was sensitive to the Hsp90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin.	tanespimycin	166-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
22869587-8	2012	Most strikingly, hydralazine selectively boosted the levels of cytoskeletal-associated Hsp90, including a high-mass species that was sensitive to the Hsp90 inhibitor 17-N-allylamino-17-demethoxygeldanamycin.	tanespimycin	166-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
22869587-9	2012	Biochemical fractionation of acrolein- and hydralazine-treated cells revealed that hydralazine likely promoted Hsp90 migration from cytosol into other subcellular compartments.	Acrolein	29-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
22869587-9	2012	Biochemical fractionation of acrolein- and hydralazine-treated cells revealed that hydralazine likely promoted Hsp90 migration from cytosol into other subcellular compartments.	Hydralazine	43-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
22869587-9	2012	Biochemical fractionation of acrolein- and hydralazine-treated cells revealed that hydralazine likely promoted Hsp90 migration from cytosol into other subcellular compartments.	Hydralazine	83-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
22869587-10	2012	A role for Hsp90 mobilization in cytoprotection was confirmed by the finding that brief heat shock treatment suppressed acute acrolein toxicity in A549 cells.	Acrolein	126-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
23041319-4	2012	Here, we establish that pharmacological inhibition of lysine deacetylases (KDACs) blocks the emergence and maintenance of Hsp90-dependent resistance to the most widely deployed antifungals, the azoles, in the human fungal pathogen Candida albicans and the model yeast Saccharomyces cerevisiae.	Azoles	194-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
22941268-0	2012	17AEP-GA, an HSP90 antagonist, is a potent inhibitor of glioblastoma             cell proliferation, survival, migration and invasion.	17aep-ga	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22941268-3	2012	We used geldanamycins (GAs) (inhibitors of HSP90) in order to block glioblastoma growth and HGF-dependent cell migration and invasion.	geldanamycin	8-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
24280702-7	2012	17-allylamino,17-demethoxygeldanamycin is the first Hsp90 inhibitor that has clinically been investigated in phase II trial, yielding promising results in patients with HER2-overexpressing metastatic breast cancer, whilst other Hsp90 inhibitors (retaspimycin HCL, NVP-AUY922, NVP-BEP800, CNF2024/BIIB021, SNX-5422, STA-9090, etc.)	17-allylamino	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
22952228-5	2012	Client protein activation by Hsp90 relies on a conformational change of the chaperone, whose ATPase activity is competitively inhibited by geldanamycin.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
22952228-6	2012	We demonstrate a novel regulatory mechanism of heat- and Hsp90-dependent induced morphogenesis, whereby the nonreducing disaccharide trehalose acts as a negative regulator of Hsp90 release.	Disaccharides	120-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
22952228-6	2012	We demonstrate a novel regulatory mechanism of heat- and Hsp90-dependent induced morphogenesis, whereby the nonreducing disaccharide trehalose acts as a negative regulator of Hsp90 release.	Disaccharides	120-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
22952228-6	2012	We demonstrate a novel regulatory mechanism of heat- and Hsp90-dependent induced morphogenesis, whereby the nonreducing disaccharide trehalose acts as a negative regulator of Hsp90 release.	Trehalose	133-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
22952228-6	2012	We demonstrate a novel regulatory mechanism of heat- and Hsp90-dependent induced morphogenesis, whereby the nonreducing disaccharide trehalose acts as a negative regulator of Hsp90 release.	Trehalose	133-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
22952228-10	2012	These results place Gpr1 as a regulator of trehalose metabolism in C. albicans and illustrate that trehalose modulates Hsp90-dependent activation of client proteins and signaling pathways leading to filamentation in the human fungal pathogen.	Trehalose	99-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
23042933-9	2012	Further characterization using proteolytic footprinting experiments indicated that nelfinavir inhibited HSP90 in breast cancer cells through a novel mechanism.	Nelfinavir	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
23042933-12	2012	CONCLUSION: Nelfinavir was found to be a new class of HSP90 inhibitor and can be brought to HER2-breast cancer treatment trials with the same dosage regimen as that used among HIV patients.	Nelfinavir	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
23047241-0	2012	Neurite outgrowth mediated by the heat shock protein Hsp90alpha: a novel target for the antipsychotic drug aripiprazole.	Aripiprazole	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-63
23047241-9	2012	Using proteomic analysis, we found that aripiprazole significantly increased levels of the heat shock protein Hsp90alpha in cultured cells.	Aripiprazole	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-120
23047241-10	2012	The effects of aripiprazole on NGF-induced neurite outgrowth were significantly attenuated by treatment with Hsp90alpha RNA interference, but not by the negative control of Hsp90alpha.	Aripiprazole	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-119
23047241-12	2012	Furthermore, aripiprazole-induced increases in Hsp90alpha protein expression may form part of the therapeutic mechanism for this drug.	Aripiprazole	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-57
22849407-4	2012	Geldanamycin, an Hsp90 inhibitor, significantly decreased the PTK6 protein level through proteasome-dependent degradation, but did not affect the level of Src.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
22849407-7	2012	Geldanamycin increased the interaction of PTK6 with CHIP, but decreased the interaction of PTK6 with Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
22694478-0	2012	The apoptotic effect and associated signalling of HSP90 inhibitor 17-DMAG in hepatocellular carcinoma cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	66-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
22694478-5	2012	In this study, we evaluated the therapeutic effect of specific HSP90 inhibitor 17-DMAG (17-dimethylaminoethylamino-17-demethoxy geldanamycin) in HCC cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	79-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
22694478-5	2012	In this study, we evaluated the therapeutic effect of specific HSP90 inhibitor 17-DMAG (17-dimethylaminoethylamino-17-demethoxy geldanamycin) in HCC cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	88-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
22694478-14	2012	Inhibition of HSP90 activity by 400 nmol/l 17-DMAG decreased protein levels of survivin, cyclin D1 and NF-kappaB protein levels, whereas increased p53 protein level.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	43-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22694478-15	2012	HSP90 plays a key role in HCC cell growth and survival through regulation of survivin, cyclin D1, p53 and nucleus NF-kappaB protein levels and the specific HSP90 inhibitor 17-DMAG can play a therapeutic role in HCC treatment.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	172-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22694478-15	2012	HSP90 plays a key role in HCC cell growth and survival through regulation of survivin, cyclin D1, p53 and nucleus NF-kappaB protein levels and the specific HSP90 inhibitor 17-DMAG can play a therapeutic role in HCC treatment.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	172-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
22749932-11	2012	In LPTs from patients with Crohn"s disease, survivin bound to the heat shock protein (HSP)90, and therefore was resistant to proteasome degradation.	lpts	3-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-92
22749932-12	2012	Incubating LPTs with 17-N-allylamino-17-demethoxygeldanamycin, an inhibitor of HSP90, reduced levels of survivin and induced apoptosis.	lpts	11-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
22749932-12	2012	Incubating LPTs with 17-N-allylamino-17-demethoxygeldanamycin, an inhibitor of HSP90, reduced levels of survivin and induced apoptosis.	tanespimycin	21-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
22913511-3	2012	Here we describe our lead optimization studies centered on the purine-based Hsp90 inhibitor 28a containing a piperidine moiety at the purine N9 position.	purine	63-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
22913511-3	2012	Here we describe our lead optimization studies centered on the purine-based Hsp90 inhibitor 28a containing a piperidine moiety at the purine N9 position.	piperidine	109-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
22913511-3	2012	Here we describe our lead optimization studies centered on the purine-based Hsp90 inhibitor 28a containing a piperidine moiety at the purine N9 position.	purine	134-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
22825378-0	2012	Fluorine- and rhenium-containing geldanamycin derivatives as leads for the development of molecular probes for imaging Hsp90.	Fluorine	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
22825378-0	2012	Fluorine- and rhenium-containing geldanamycin derivatives as leads for the development of molecular probes for imaging Hsp90.	Rhenium	14-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
22825378-0	2012	Fluorine- and rhenium-containing geldanamycin derivatives as leads for the development of molecular probes for imaging Hsp90.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
22825378-1	2012	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone responsible for protein quality control in cells.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
22825378-1	2012	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone responsible for protein quality control in cells.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
22825378-4	2012	This work describes the development of various fluorine-containing and rhenium-containing geldanamycin derivatives as leads for the development of corresponding (18)F-labeled and (99m)Tc-labeled PET and SPECT probes for molecular imaging of Hsp90 expression.	Fluorine	47-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
22825378-4	2012	This work describes the development of various fluorine-containing and rhenium-containing geldanamycin derivatives as leads for the development of corresponding (18)F-labeled and (99m)Tc-labeled PET and SPECT probes for molecular imaging of Hsp90 expression.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
22825378-4	2012	This work describes the development of various fluorine-containing and rhenium-containing geldanamycin derivatives as leads for the development of corresponding (18)F-labeled and (99m)Tc-labeled PET and SPECT probes for molecular imaging of Hsp90 expression.	Technetium	184-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	241-246
22851178-2	2012	P2X1 receptor currents in HEK293 cells were reduced by ~70-85% by the selective HSP90 inhibitor geldanamycin (2 muM, 20 min).	geldanamycin	96-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
22851178-9	2012	Platelet P2X1 receptor-, but not P2Y1 receptor-, mediated increases in intracellular calcium were reduced by 40-45% following HSP90 inhibition with geldanamycin or radicicol.	geldanamycin	148-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
22851178-10	2012	Collagen stimulation leads to ATP release from platelets, and calcium increases to low doses of collagen were also reduced by ~40% by the HSP90 inhibitors consistent with an effect on P2X1 receptors.	Adenosine Triphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
22851178-10	2012	Collagen stimulation leads to ATP release from platelets, and calcium increases to low doses of collagen were also reduced by ~40% by the HSP90 inhibitors consistent with an effect on P2X1 receptors.	Calcium	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
22892119-0	2012	Sequences in the HSP90 promoter form G-quadruplex structures with selectivity for disubstituted phenyl bis-oxazole derivatives.	phenyl bis-oxazole	96-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
22892119-2	2012	We report here that stable quadruplex DNAs can be formed from a promoter sequence in the HSP90 gene, on the basis of melting, circular and NMR studies, and show that these can be selectively targeted by non-macrocyclic quadruplex-stabilizing phenyl bis-oxazole derivatives.	phenyl bis-oxazole	242-260	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22938030-2	2012	Alkyne 40 is more potent than 14 in an Hsp90alpha binding assay (IC(50) = 1.1 vs 5.1 nM) as well as in its ability to degrade Her-2 in MCF-7 cells (EC(50) = 14 vs 38 nM).	Alkynes	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-49
24280702-7	2012	17-allylamino,17-demethoxygeldanamycin is the first Hsp90 inhibitor that has clinically been investigated in phase II trial, yielding promising results in patients with HER2-overexpressing metastatic breast cancer, whilst other Hsp90 inhibitors (retaspimycin HCL, NVP-AUY922, NVP-BEP800, CNF2024/BIIB021, SNX-5422, STA-9090, etc.)	17-demethoxygeldanamycin	14-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
24280702-7	2012	17-allylamino,17-demethoxygeldanamycin is the first Hsp90 inhibitor that has clinically been investigated in phase II trial, yielding promising results in patients with HER2-overexpressing metastatic breast cancer, whilst other Hsp90 inhibitors (retaspimycin HCL, NVP-AUY922, NVP-BEP800, CNF2024/BIIB021, SNX-5422, STA-9090, etc.)	tanespimycin	246-262	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
22718860-2	2012	This provides the rationale for the development of small-molecule ATP competitors that, inhibiting Hsp90 function, lead to degradation of the "client" proteins.	Adenosine Triphosphate	66-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
22433057-0	2012	Combined effect of Hsp90 inhibitor geldanamycin and parthenolide via reactive oxygen species-mediated apoptotic process on epithelial ovarian cancer cells.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
22433057-0	2012	Combined effect of Hsp90 inhibitor geldanamycin and parthenolide via reactive oxygen species-mediated apoptotic process on epithelial ovarian cancer cells.	Reactive Oxygen Species	69-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
22433057-1	2012	Hsp90 inhibitor geldanamycin and parthenolide have been shown to induce apoptosis in cancer cells.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22825030-6	2012	Treatment with vorinostat induced hsp90 acetylation and inhibited its chaperone association with AKs, leading to depletion of AKs and Survivin.	Vorinostat	15-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
24280696-3	2012	We discuss four mechanisms by which Hsp90 inhibitors can potentially synergize with anti-cancer drugs: by making a drug-resistant protein that is a client for Hsp90 more sensitive to the drug, by increasing chromosomal aneuploidy and the effectiveness of DNA-damaging drugs, by inhibiting Trithorax proteins which trimethylate histone 3 at lysine 4 (H3K4me3) and thereby decreasing expression of tumor promoter genes, and by interacting with the negative elongation factor (NELF) complex in tumors.	trimethylate histone	314-334	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
22710416-7	2012	NAC successfully blocked the inhibition             of HSP70 and HSP90 as well as the activation of caspase-3, suggesting that ROS             is essential in Cr(VI)-induced caspase-3 activation.	Acetylcysteine	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
21751262-0	2012	A novel cyano derivative of 11-keto-beta-boswellic acid causes apoptotic death by disrupting PI3K/AKT/Hsp-90 cascade, mitochondrial integrity, and other cell survival signaling events in HL-60 cells.	11-keto-boswellic acid	28-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-108
22338602-5	2012	This review summarizes the current state and progress achieved in the development of HSP90 inhibitors targeting the N-terminal ATP pocket, C-terminal domain, different compartmentalized isoforms, and protein (cochaperones and/or client proteins)/HSP90 interactions.	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
24280696-3	2012	We discuss four mechanisms by which Hsp90 inhibitors can potentially synergize with anti-cancer drugs: by making a drug-resistant protein that is a client for Hsp90 more sensitive to the drug, by increasing chromosomal aneuploidy and the effectiveness of DNA-damaging drugs, by inhibiting Trithorax proteins which trimethylate histone 3 at lysine 4 (H3K4me3) and thereby decreasing expression of tumor promoter genes, and by interacting with the negative elongation factor (NELF) complex in tumors.	trimethylate histone	314-334	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
24280696-3	2012	We discuss four mechanisms by which Hsp90 inhibitors can potentially synergize with anti-cancer drugs: by making a drug-resistant protein that is a client for Hsp90 more sensitive to the drug, by increasing chromosomal aneuploidy and the effectiveness of DNA-damaging drugs, by inhibiting Trithorax proteins which trimethylate histone 3 at lysine 4 (H3K4me3) and thereby decreasing expression of tumor promoter genes, and by interacting with the negative elongation factor (NELF) complex in tumors.	Lysine	340-346	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
24280696-3	2012	We discuss four mechanisms by which Hsp90 inhibitors can potentially synergize with anti-cancer drugs: by making a drug-resistant protein that is a client for Hsp90 more sensitive to the drug, by increasing chromosomal aneuploidy and the effectiveness of DNA-damaging drugs, by inhibiting Trithorax proteins which trimethylate histone 3 at lysine 4 (H3K4me3) and thereby decreasing expression of tumor promoter genes, and by interacting with the negative elongation factor (NELF) complex in tumors.	Lysine	340-346	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	tanespimycin	64-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
22913813-6	2012	Antp-TPR also did not induce the up-regulation of Hsp70 and Hsp90 proteins, although a small-molecule inhibitor of Hsp90, 17-AAG, induced the up-regulation of these proteins.	tanespimycin	122-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	tanespimycin	64-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	tanespimycin	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	tanespimycin	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	tanespimycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	tanespimycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	Platinum	312-320	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
22869732-6	2012	We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin [17-AAG (Tanespimycin)], currently in Phase II/III clinical evaluation for several cancers, induces BRCA1 ubiquitination and proteasomal degradation, resulting in compromised repair of ionizing radiation- and platinum-induced DNA damage.	Platinum	312-320	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
21964864-0	2012	Potential role of Hsp90 inhibitors in overcoming cisplatin resistance of bladder cancer-initiating cells.	Cisplatin	49-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
21964864-4	2012	In this study, the authors have isolated BCICs from cultured human bladder cancer cells to analyze their sensitivity to CDDP and to investigate whether heat-shock protein 90 (Hsp90) inhibitors potentiate the cytotoxicity of CDDP on BCICs.	Cisplatin	224-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-173
21964864-4	2012	In this study, the authors have isolated BCICs from cultured human bladder cancer cells to analyze their sensitivity to CDDP and to investigate whether heat-shock protein 90 (Hsp90) inhibitors potentiate the cytotoxicity of CDDP on BCICs.	Cisplatin	224-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
21964864-7	2012	The Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), which simultaneously inactivated both Akt and ERK signaling at noncytocidal concentrations, synergistically potentiated the cytotoxicity of CDDP against BCICs by enhancing CDDP-induced apoptosis in vitro.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21964864-7	2012	The Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), which simultaneously inactivated both Akt and ERK signaling at noncytocidal concentrations, synergistically potentiated the cytotoxicity of CDDP against BCICs by enhancing CDDP-induced apoptosis in vitro.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22727666-0	2012	Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.	Tyrosine	8-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
22727666-2	2012	After initially forming a ternary complex with kinase client and the cochaperone p50(Cdc37), Hsp90 proceeds through a cycle of conformational changes facilitated by ATP binding and hydrolysis.	Adenosine Triphosphate	165-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
22727666-4	2012	We demonstrate that a series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle.	Tyrosine	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
22727666-6	2012	Hsp90 phosphorylation on Y313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process.	y313	25-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22727666-6	2012	Hsp90 phosphorylation on Y313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process.	y313	25-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
22753480-5	2012	Here we show that HSP90alpha is phosphorylated by DNA-PK on threonines 5 and 7 early during apoptosis and that both phosphorylated HSP90alpha and DNA-PK colocalize in the apoptotic ring.	Threonine	60-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-28
22753480-7	2012	In contrast, HSP90 inhibition by geldanamycin markedly enhances TRAIL-induced DNA-PK and H2AX activation.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22837396-3	2012	The present study reveals that hsp90 is required to drive heme insertion into sGC and complete its maturation.	Heme	58-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
21964864-7	2012	The Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), which simultaneously inactivated both Akt and ERK signaling at noncytocidal concentrations, synergistically potentiated the cytotoxicity of CDDP against BCICs by enhancing CDDP-induced apoptosis in vitro.	Cisplatin	225-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21964864-7	2012	The Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), which simultaneously inactivated both Akt and ERK signaling at noncytocidal concentrations, synergistically potentiated the cytotoxicity of CDDP against BCICs by enhancing CDDP-induced apoptosis in vitro.	bcics	238-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21964864-7	2012	The Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), which simultaneously inactivated both Akt and ERK signaling at noncytocidal concentrations, synergistically potentiated the cytotoxicity of CDDP against BCICs by enhancing CDDP-induced apoptosis in vitro.	Cisplatin	257-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21964864-9	2012	Finally, the authors have confirmed that, though human BCIC xenografts exhibited resistance to a single administration of CDDP and the Hsp90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17-AAG), 17-AAG sensitized them to CDDP in a mouse model.	tanespimycin	151-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
21964864-9	2012	Finally, the authors have confirmed that, though human BCIC xenografts exhibited resistance to a single administration of CDDP and the Hsp90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17-AAG), 17-AAG sensitized them to CDDP in a mouse model.	tanespimycin	193-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
21964864-10	2012	These data encourage clinical trials of Hsp90 inhibitors as they may improve therapeutic outcomes of CDDP-based combination chemotherapy against advanced bladder cancer.	Cisplatin	101-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
22428803-1	2012	Heat shock protein-90 (HSP90) is an ATP-dependent molecular chaperone with intrinsic ATPase activity.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
22428803-1	2012	Heat shock protein-90 (HSP90) is an ATP-dependent molecular chaperone with intrinsic ATPase activity.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
22714264-0	2012	The HSP90 inhibitor, AT13387, is effective against imatinib-sensitive and -resistant gastrointestinal stromal tumor models.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	21-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22714264-0	2012	The HSP90 inhibitor, AT13387, is effective against imatinib-sensitive and -resistant gastrointestinal stromal tumor models.	Imatinib Mesylate	51-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22952420-5	2012	Further, the HSP90 inhibitors geldanamycin (GA) and AT13387 cause a decrease in WT-EGFR in cultured head and neck cancer cells.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22952420-5	2012	Further, the HSP90 inhibitors geldanamycin (GA) and AT13387 cause a decrease in WT-EGFR in cultured head and neck cancer cells.	geldanamycin	44-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22952420-5	2012	Further, the HSP90 inhibitors geldanamycin (GA) and AT13387 cause a decrease in WT-EGFR in cultured head and neck cancer cells.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	52-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22653663-3	2012	Previous structural and biochemical work identified a conserved arginine residue (R380 in yeast) in the Hsp90 middle domain (MD) that is required for wild type hydrolysis activity in yeast, and hence proposed to be a catalytic residue.	Arginine	64-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
22653663-4	2012	As part of our investigations on the origins of species-specific differences in Hsp90 conformational dynamics we probed the role of this MD arginine in bacterial, yeast, and human Hsp90s using a combination of structural and functional approaches.	Arginine	140-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
22750442-4	2012	Here, we report that treatment of 17-AAG, an Hsp90 inhibitor, facilitates the folding of Pendrin through heat shock transcription factor 1 (Hsf1)-dependent induction of molecular chaperones.	tanespimycin	34-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
22837396-6	2012	Our findings suggest that hsp90 complexes with apo-sGC, drives heme insertion through its inherent ATPase activity, and then dissociates from the mature, heme-replete sGC.	Heme	63-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
22837396-6	2012	Our findings suggest that hsp90 complexes with apo-sGC, drives heme insertion through its inherent ATPase activity, and then dissociates from the mature, heme-replete sGC.	Heme	154-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
24280675-2	2012	Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1) benzoquinone ansamycin and its derivatives, (2) radicicol and its derivates, and (3) small synthetic inhibitors.	benzoquinone ansamycin	125-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24280675-2	2012	Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1) benzoquinone ansamycin and its derivatives, (2) radicicol and its derivates, and (3) small synthetic inhibitors.	benzoquinone ansamycin	125-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
24280675-2	2012	Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1) benzoquinone ansamycin and its derivatives, (2) radicicol and its derivates, and (3) small synthetic inhibitors.	monorden	173-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
24280675-2	2012	Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1) benzoquinone ansamycin and its derivatives, (2) radicicol and its derivates, and (3) small synthetic inhibitors.	monorden	173-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
22696415-0	2012	Asymmetric synthesis of pochonin E and F, revision of their proposed structure, and their conversion to potent Hsp90 inhibitors.	pochonin	24-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
22704890-3	2012	The synthetic analogues SNX-25a, SNX-2112 and SNX-7081, which selectively bind to the N-terminal ATP pocket of heat shock protein 90 (HSP90), exhibited significant anti-HSV-1 and HSV-2 activities at non-cytotoxic concentrations in Vero cells, with EC(50) values close to that of acyclovir (ACV).	SNX-7081	46-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22704890-3	2012	The synthetic analogues SNX-25a, SNX-2112 and SNX-7081, which selectively bind to the N-terminal ATP pocket of heat shock protein 90 (HSP90), exhibited significant anti-HSV-1 and HSV-2 activities at non-cytotoxic concentrations in Vero cells, with EC(50) values close to that of acyclovir (ACV).	Adenosine Triphosphate	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22704890-3	2012	The synthetic analogues SNX-25a, SNX-2112 and SNX-7081, which selectively bind to the N-terminal ATP pocket of heat shock protein 90 (HSP90), exhibited significant anti-HSV-1 and HSV-2 activities at non-cytotoxic concentrations in Vero cells, with EC(50) values close to that of acyclovir (ACV).	Acyclovir	279-288	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22704890-3	2012	The synthetic analogues SNX-25a, SNX-2112 and SNX-7081, which selectively bind to the N-terminal ATP pocket of heat shock protein 90 (HSP90), exhibited significant anti-HSV-1 and HSV-2 activities at non-cytotoxic concentrations in Vero cells, with EC(50) values close to that of acyclovir (ACV).	Acyclovir	290-293	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22704890-6	2012	Our results for the first time confirmed the anti-HSV efficacies of these 2-aminobenzamide derivatives and suggest that with alternative mechanisms of action these novel HSP90 inhibitors, especially SNX-25a, could be potent as new anti-HSV clinical trial candidates.	snx-25a	199-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
22555844-6	2012	The protective effect of H(2)S on ER stress was attenuated by blockade of Akt activity with an Akt inhibitor or inhibition of heat shock protein (Hsp)90 with geldanamycin but not by suppression of ERK1/2 with PD-98059.	Hydrogen Sulfide	25-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-152
22555844-6	2012	The protective effect of H(2)S on ER stress was attenuated by blockade of Akt activity with an Akt inhibitor or inhibition of heat shock protein (Hsp)90 with geldanamycin but not by suppression of ERK1/2 with PD-98059.	geldanamycin	158-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-152
22555844-9	2012	In conclusion, the protective effect of H(2)S against 6-OHDA-induced ER stress injury in SH-SY5Y cells involves the Akt-Hsp90 pathway.	Hydrogen Sulfide	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
22555844-9	2012	In conclusion, the protective effect of H(2)S against 6-OHDA-induced ER stress injury in SH-SY5Y cells involves the Akt-Hsp90 pathway.	Oxidopamine	54-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
22632933-0	2012	Fragment-based discovery of hydroxy-indazole-carboxamides as novel small molecule inhibitors of Hsp90.	hydroxy-indazole-carboxamides	28-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
22564525-6	2012	Treatment with the HSP90 inhibitor 17-DMAG or ligation of CD44 with hyaluronan caused nuclear depletion of FRMD4A, nuclear accumulation of YAP and reduced SCC growth and metastasis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	35-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
22573351-4	2012	RESULTS: In cell lines, both NVP-AUY922 and NVP-HSP990 showed greater potency than 17-AAG with regard to modulation of Hsp90 client proteins, inhibition of proliferation, and induction of apoptotic cell death.	tanespimycin	83-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
22470109-2	2012	Because HDAC inhibition disrupts the chaperon function of heat shock protein             (HSP) 90, we hypothesized that the combination of 17-allylamino-17-demethoxygeldanamycin             (17-AAG), an inhibitor of HSP90, and the HIV protease inhibitor ritonavir would             also act against renal cancer.	tanespimycin	139-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-97
22470109-2	2012	Because HDAC inhibition disrupts the chaperon function of heat shock protein             (HSP) 90, we hypothesized that the combination of 17-allylamino-17-demethoxygeldanamycin             (17-AAG), an inhibitor of HSP90, and the HIV protease inhibitor ritonavir would             also act against renal cancer.	tanespimycin	139-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	216-221
22470109-2	2012	Because HDAC inhibition disrupts the chaperon function of heat shock protein             (HSP) 90, we hypothesized that the combination of 17-allylamino-17-demethoxygeldanamycin             (17-AAG), an inhibitor of HSP90, and the HIV protease inhibitor ritonavir would             also act against renal cancer.	tanespimycin	191-197	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-97
22099584-1	2012	BACKGROUND: 17-Allylamino-17-demethoxygeldanamycin (17-AAG) specifically targets heat shock protein (HSP)90 and inhibits its chaperoning functions for multiple kinases involved in cancer cell growth and survival.	tanespimycin	12-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-107
22704890-0	2012	Anti-herpes simplex virus efficacies of 2-aminobenzamide derivatives as novel HSP90 inhibitors.	anthranilamide	40-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
22704890-3	2012	The synthetic analogues SNX-25a, SNX-2112 and SNX-7081, which selectively bind to the N-terminal ATP pocket of heat shock protein 90 (HSP90), exhibited significant anti-HSV-1 and HSV-2 activities at non-cytotoxic concentrations in Vero cells, with EC(50) values close to that of acyclovir (ACV).	snx-25a	24-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22704890-3	2012	The synthetic analogues SNX-25a, SNX-2112 and SNX-7081, which selectively bind to the N-terminal ATP pocket of heat shock protein 90 (HSP90), exhibited significant anti-HSV-1 and HSV-2 activities at non-cytotoxic concentrations in Vero cells, with EC(50) values close to that of acyclovir (ACV).	SNX 2112	33-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
21538821-0	2012	Initial testing (Stage 1) of AT13387, an HSP90 inhibitor, by the pediatric preclinical testing program.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	29-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
21538821-1	2012	AT13387, a non-geldanamycin inhibitor of heat-shock protein 90 (HSP90), was tested against the PPTP in vitro panel (1.0 nM to 10 microM) and against the PPTP in vivo panels (40 or 60 mg/kg) administered orally twice weekly.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
21538821-1	2012	AT13387, a non-geldanamycin inhibitor of heat-shock protein 90 (HSP90), was tested against the PPTP in vitro panel (1.0 nM to 10 microM) and against the PPTP in vivo panels (40 or 60 mg/kg) administered orally twice weekly.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
21837531-4	2012	METHODS: MDA-1986 HNSCC cells were treated with doses of 17-AAG or KU363 (a CT-Hsp90-I) and compared for antiproliferation by GLO-Titer and trypan blue exclusion and for apoptosis by PARP cleavage and caspase-3 inactivation by Western analysis.	ku363	67-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
22753713-0	2012	Targeting HSP90 by the novel inhibitor NVP-AUY922 reduces growth and angiogenesis of pancreatic cancer.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
22706627-7	2012	We further determined that the HSP90 inhibitor 17-DMAG suppressed the growth of the AI-resistant cell lines studied.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	47-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
22547655-0	2012	HSP90 inhibition by 17-DMAG attenuates oxidative stress in experimental atherosclerosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22547655-3	2012	In this work, we investigated the antioxidant properties of the HSP90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) in experimental atherosclerosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	81-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
22547655-3	2012	In this work, we investigated the antioxidant properties of the HSP90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) in experimental atherosclerosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	134-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
22547655-7	2012	In addition, a marked reduction in NADPH oxidase dependent ROS production was observed with HSP90siRNA and the opposite pattern with HSP70siRNA.	Reactive Oxygen Species	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
22538015-0	2012	Isoxazolo(aza)naphthoquinones: a new class of cytotoxic Hsp90 inhibitors.	isoxazolo(aza)naphthoquinones	0-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
22538015-1	2012	A series of 3-aryl-naphtho[2,3-d]isoxazole-4,9-diones and some of their 6-aza analogues were synthesized and found to inhibit the heat shock protein 90 (Hsp90).	3-aryl-naphtho[2,3-d]isoxazole-4,9-diones	12-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-151
22538015-1	2012	A series of 3-aryl-naphtho[2,3-d]isoxazole-4,9-diones and some of their 6-aza analogues were synthesized and found to inhibit the heat shock protein 90 (Hsp90).	3-aryl-naphtho[2,3-d]isoxazole-4,9-diones	12-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
22538015-1	2012	A series of 3-aryl-naphtho[2,3-d]isoxazole-4,9-diones and some of their 6-aza analogues were synthesized and found to inhibit the heat shock protein 90 (Hsp90).	6-aza	72-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-151
22538015-1	2012	A series of 3-aryl-naphtho[2,3-d]isoxazole-4,9-diones and some of their 6-aza analogues were synthesized and found to inhibit the heat shock protein 90 (Hsp90).	6-aza	72-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
22639078-9	2012	The HSP90 subset from real life fragment optimization programs revealed that Glide is able to reproduce the positions of multiple bound fragments if conserved water molecules are considered.	Water	159-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22609743-3	2012	Taxifolin (a natural phytochemical) was found to bind at ATP-binding site of Hsp90 and stabilized the inactive "open" or "lid-up" conformation as evidenced by molecular dynamic simulation.	taxifolin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
22609743-3	2012	Taxifolin (a natural phytochemical) was found to bind at ATP-binding site of Hsp90 and stabilized the inactive "open" or "lid-up" conformation as evidenced by molecular dynamic simulation.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
22609743-4	2012	Furthermore, taxifolin was found to bind to interface of Hsp90 and Cdc37 complex and disrupt the interaction of residues of both proteins which were essential for the formation of active super-chaperone complex.	taxifolin	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
22149137-0	2012	The Hsp90 inhibitor SNX-7081 synergizes with and restores sensitivity to fludarabine in chronic lymphocytic leukemia cells with lesions in the TP53 pathway: a potential treatment strategy for fludarabine refractory disease.	SNX-7081	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22149137-0	2012	The Hsp90 inhibitor SNX-7081 synergizes with and restores sensitivity to fludarabine in chronic lymphocytic leukemia cells with lesions in the TP53 pathway: a potential treatment strategy for fludarabine refractory disease.	fludarabine	73-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22149137-0	2012	The Hsp90 inhibitor SNX-7081 synergizes with and restores sensitivity to fludarabine in chronic lymphocytic leukemia cells with lesions in the TP53 pathway: a potential treatment strategy for fludarabine refractory disease.	fludarabine	192-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22700507-4	2012	Inhibition of Hsp90 activity in thiram-induced TD resulted in increased Flk-1 levels, re-instated normal growth-plate angiogenesis and morphology, and abrogated lameness.	Thiram	32-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22726688-3	2012	We found that, during aldosterone-induced nuclear translocation, MR is bound to HSP90 both in the cytosol and the nucleus.	Aldosterone	22-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
22700507-5	2012	In the present study, we evaluated the efficacy of various concentrations of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), an inhibitor of Hsp90 activity, in preventing growth-plate histopathology and lameness in TD-affected chicks.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	77-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
22700507-5	2012	In the present study, we evaluated the efficacy of various concentrations of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), an inhibitor of Hsp90 activity, in preventing growth-plate histopathology and lameness in TD-affected chicks.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	132-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
22496241-0	2012	Hsp90 regulates O-linked beta-N-acetylglucosamine transferase: a novel mechanism of modulation of protein O-linked beta-N-acetylglucosamine modification in endothelial cells.	Acetylglucosamine	25-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22496241-6	2012	Inhibition of Hsp90 by its specific inhibitors, radicicol or 17-N-allylamino-17-demethoxygeldanamycin, destabilized OGT in primary endothelial cell cultures and enhanced its degradation by the proteasome.	monorden	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22496241-6	2012	Inhibition of Hsp90 by its specific inhibitors, radicicol or 17-N-allylamino-17-demethoxygeldanamycin, destabilized OGT in primary endothelial cell cultures and enhanced its degradation by the proteasome.	tanespimycin	61-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22496241-7	2012	Furthermore, Hsp90 inhibition downregulated O-GlcNAc protein modifications and attenuated the high glucose-induced increase in O-GlcNAc protein modification, including high glucose-induced increase in endothelial or type 3 isoform of nitric oxide synthase (eNOS) O-GlcNAcylation.	Glucose	99-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22496241-7	2012	Furthermore, Hsp90 inhibition downregulated O-GlcNAc protein modifications and attenuated the high glucose-induced increase in O-GlcNAc protein modification, including high glucose-induced increase in endothelial or type 3 isoform of nitric oxide synthase (eNOS) O-GlcNAcylation.	Glucose	173-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22504172-3	2012	Complexes formed by Aha1 with Hsp90 in RRL were stabilized by molybdate and contained the co-chaperones FKBP52 and p23/Sba1, but lacked HOP/Sti1 and Cdc37.	molybdate	62-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
22652777-0	2012	Geldanamycin and its derivatives as Hsp90 inhibitors.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
22652777-4	2012	The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and its analogues 17AAG and 17DMAG.	Adenosine Triphosphate	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22652777-4	2012	The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and its analogues 17AAG and 17DMAG.	Adenosine Triphosphate	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
22566604-5	2012	In the present study, we investigated the antitumor effects of inhibiting mTORC2 plus HSP90 in mouse and human leukemia cell models and show that the HSP90 inhibitor 17-allylaminogeldanamycin (17-AAG) preferentially inhibits Akt and cPKC expression and promotes cell death in mTORC2 deficient pre-B leukemia cells.	tanespimycin	166-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
22691173-2	2012	We evaluated the effects of the proteasome inhibitor Bortezomib and of 17-DMAG, a competitive inhibitor of Hsp90, in rhabdomyosarcoma (RMS) cells, and analyzed the efficacy of single-agent exposures with combination treatments.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	71-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
22691173-9	2012	CONCLUSION: The combination of proteasome inhibitor Bortezomib with Hsp90 inhibitor 17-DMAG, appears to have important therapeutic advantages in the treatment of RMS cells compared with single-agent exposure, because compensatory survival mechanisms that occur as side effects of treatment may be prevented.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	84-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
22467305-1	2012	Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor.	geldanamycin	188-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
22467305-1	2012	Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor.	geldanamycin	188-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
22467305-1	2012	Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor.	geldanamycin	188-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
22467305-1	2012	Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor.	geldanamycin	202-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
22467305-1	2012	Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor.	geldanamycin	202-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
22467305-1	2012	Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor.	geldanamycin	202-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
22445681-1	2012	Heat shock protein (Hsp) 90 is an ATP-dependent chaperone and its expression has been reported to be associated with poor prognosis of breast cancer.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-27
22445681-6	2012	Geldanamycin (GA), a Hsp90 inhibitor, could suppress ALDH + breast cancer cells in a dose dependent manner.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
22445681-6	2012	Geldanamycin (GA), a Hsp90 inhibitor, could suppress ALDH + breast cancer cells in a dose dependent manner.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
22377218-1	2012	Low water solubility and hepatotoxicity limited the clinical use of 17-allylamino-17-demethoxy geldanamycin (17-AAG), an inhibitor of heat shock protein 90 (HSP90).	tanespimycin	68-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-155
22377218-1	2012	Low water solubility and hepatotoxicity limited the clinical use of 17-allylamino-17-demethoxy geldanamycin (17-AAG), an inhibitor of heat shock protein 90 (HSP90).	tanespimycin	68-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
21928319-7	2012	More robust reduction of EGFR and Her2 levels was observed when knocked-down cells were treated with HSP90 inhibitor geldanamycin (GA).	geldanamycin	117-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
22652777-4	2012	The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and its analogues 17AAG and 17DMAG.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22652777-4	2012	The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and its analogues 17AAG and 17DMAG.	geldanamycin	139-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
22554482-5	2012	Animals were divided into groups of five: no treatment and 12 hours and 1 week after treatment of the tumors with the Hsp90 inhibitor 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	134-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
22554482-5	2012	Animals were divided into groups of five: no treatment and 12 hours and 1 week after treatment of the tumors with the Hsp90 inhibitor 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	187-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
22182451-0	2012	SNX-2112, an Hsp90 inhibitor, induces apoptosis and autophagy via degradation of Hsp90 client proteins in human melanoma A-375 cells.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22182451-0	2012	SNX-2112, an Hsp90 inhibitor, induces apoptosis and autophagy via degradation of Hsp90 client proteins in human melanoma A-375 cells.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
22182451-1	2012	SNX-2112 is an Hsp90 inhibitor which is currently undergoing multiple phase 1 clinical trials; however, its mechanism of action needs to be further elaborated.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
22182451-3	2012	SNX-2112 induced the degradation of multiple Hsp90 client proteins, activated both the mitochondrial-mediated and death receptor-mediated apoptotic pathways, downregulated Bcl-2 and Bcl-xL, upregulated Bid, cleaved caspase-9, caspase-7, caspase-3 and PARP, and activated caspase-8.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
22380712-7	2012	Conversion of the carboxylic acid functionality to amides and long-chain analogues, however, yielded bioactive compounds that induced the heat shock response (HSR) and antioxidant response and inhibited Hsp90 activity.	Carboxylic Acids	18-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
22380712-7	2012	Conversion of the carboxylic acid functionality to amides and long-chain analogues, however, yielded bioactive compounds that induced the heat shock response (HSR) and antioxidant response and inhibited Hsp90 activity.	Amides	51-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
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
22194440-8	2012	The treatment of the cell lines BON and beta-TC-3 with the HSP90 inhibitors 17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxy-geldanamycin resulted in significant, dose-dependent reduction of cell viability, cell cycle arrest, and increased apoptosis.	tanespimycin	76-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
22194440-10	2012	HSP90 inhibitors increased the therapeutic effects of doxorubicin and 5-fluorucacil in BON and beta-TC-3 cells.	Doxorubicin	54-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22194440-10	2012	HSP90 inhibitors increased the therapeutic effects of doxorubicin and 5-fluorucacil in BON and beta-TC-3 cells.	5-fluorucacil	70-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22194440-10	2012	HSP90 inhibitors increased the therapeutic effects of doxorubicin and 5-fluorucacil in BON and beta-TC-3 cells.	beta-tc-3	95-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22351686-0	2012	The HSP90 inhibitor XL888 overcomes BRAF inhibitor resistance mediated through diverse mechanisms.	XL 888	20-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22351686-2	2012	This study shows the potential therapeutic use of the HSP90 inhibitor (XL888) in six different models of vemurafenib resistance.	XL 888	71-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
22351686-2	2012	This study shows the potential therapeutic use of the HSP90 inhibitor (XL888) in six different models of vemurafenib resistance.	Vemurafenib	105-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
21928319-7	2012	More robust reduction of EGFR and Her2 levels was observed when knocked-down cells were treated with HSP90 inhibitor geldanamycin (GA).	geldanamycin	131-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
21928319-8	2012	Low concentration of GA (50-100 nm)-induced apoptosis of the Rab7 knocked-down cells but not control cells, suggesting that Rab7 and HSP90 together contribute to the optimal stability of EGFR and Her2 as well as to protect cancer cells from apoptosis.	geldanamycin	21-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22533508-0	2012	Proteomic identification of a novel hsp90-containing protein-mineral complex which can be induced in cells in response to massive calcium influx.	Calcium	130-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
22533508-5	2012	In addition, purified native Hsp90 directly bound both amorphous calcium phosphate and hydroxyapatite and underwent conformational changes and oligomerization in the presence of excess calcium and phosphate.	calcium phosphate	65-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
22533508-5	2012	In addition, purified native Hsp90 directly bound both amorphous calcium phosphate and hydroxyapatite and underwent conformational changes and oligomerization in the presence of excess calcium and phosphate.	Durapatite	87-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
22533508-5	2012	In addition, purified native Hsp90 directly bound both amorphous calcium phosphate and hydroxyapatite and underwent conformational changes and oligomerization in the presence of excess calcium and phosphate.	Calcium	65-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
22533508-5	2012	In addition, purified native Hsp90 directly bound both amorphous calcium phosphate and hydroxyapatite and underwent conformational changes and oligomerization in the presence of excess calcium and phosphate.	Phosphates	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
22533508-7	2012	When cultured SiHa cells were treated with a calcium ionophore or damaged by scratch to induce the massive calcium influx, a complex was formed and observed at discrete sites near the plasma membrane as revealed by antibodies against Hsp90, annexin A5, calreticulin, nucleolin, and other proteins.	Calcium	45-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
22533508-7	2012	When cultured SiHa cells were treated with a calcium ionophore or damaged by scratch to induce the massive calcium influx, a complex was formed and observed at discrete sites near the plasma membrane as revealed by antibodies against Hsp90, annexin A5, calreticulin, nucleolin, and other proteins.	Calcium	107-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	234-239
22337586-8	2012	Of the 288 identified protein kinases, 98 were geldanamycin treatment including &gt;50 kinases not formerly known to be regulated by HSP90.	geldanamycin	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22337586-11	2012	The proteomic responses of the HSP90 drugs geldanamycin and PU-H71 were highly similar suggesting that both drugs work by similar molecular mechanisms.	geldanamycin	43-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
21796766-0	2012	Anti-tumor activity of the HSP90 inhibitor SNX-2112 in pediatric cancer cell lines.	SNX 2112	43-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21796766-2	2012	SNX-2112 is an orally administered potent HSP90 inhibitor that has demonstrated pre-clinical anti-tumor activity in adult malignancies.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
21796766-14	2012	CONCLUSIONS: SNX-2112 showed marked single-agent activity in pediatric cancer cell lines with downstream effects on HSP90 client proteins.	SNX 2112	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
21796766-16	2012	Further studies of HSP90 inhibitors such as SNX-2112 as a single agent or in combination with chemotherapy are warranted in pediatric cancer.	SNX 2112	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
22441439-0	2012	Radiosensitizing effect of the novel Hsp90 inhibitor NVP-AUY922 in human tumour cell lines silenced for Hsp90alpha.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
22621282-1	2012	BACKGROUND: The importance of ERBB2/NEU/HER2 in the response of breast tumours to the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG; tanespimycin) has been demonstrated in the clinic.	tanespimycin	126-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-107
22621282-1	2012	BACKGROUND: The importance of ERBB2/NEU/HER2 in the response of breast tumours to the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG; tanespimycin) has been demonstrated in the clinic.	tanespimycin	126-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
22621282-1	2012	BACKGROUND: The importance of ERBB2/NEU/HER2 in the response of breast tumours to the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG; tanespimycin) has been demonstrated in the clinic.	tanespimycin	174-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
22521890-7	2012	Silencing of Hsp90 also reduced cell viability, as determined by MTT assay.	monooxyethylene trimethylolpropane tristearate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22543833-0	2012	Heat shock protein 90 inhibition by 17-DMAG lessens disease in the MRL/lpr mouse model of systemic lupus erythematosus.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	36-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
22490666-4	2012	Here, we show that Hsp90 inhibition by 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) destabilizes phosphoinositide-dependent kinase-1 (PDK1), an upstream kinase of the protein kinase C-related kinase 2 (PRK2) responsible for phosphorylation of HCV RNA polymerase, through the proteosome pathway.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	39-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
21866552-0	2012	Paraptosis accompanied by autophagy and apoptosis was induced by celastrol, a natural compound with influence on proteasome, ER stress and Hsp90.	celastrol	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
21866552-10	2012	The potency of celastrol to induce paraptosis, apoptosis and autophagy at the same dose might be related to its capability to affect a variety of pathways including proteasome, ER stress and Hsp90.	celastrol	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
22619113-0	2012	The Hsp90 inhibitor NVP-AUY922-AG inhibits NF-kappaB signaling, overcomes microenvironmental cytoprotection and is highly synergistic with fludarabine in primary CLL cells.	fludarabine	139-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22537224-9	2012	Six small molecules, including bortezomib (proteasome inhibitor), CA-074-Me (cathepsin B inhibitor) and 17-AAG (HSP90 inhibitor), synergized with cisplatin specifically in FA-proficient ovarian cancer cells (2008 + FANCF), but not in FA-deficient isogenic cells (2008).	Cisplatin	146-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
22537224-10	2012	In addition, geldanamycin (HSP90 inhibitor) and two CHK1 inhibitors (UCN-01 and SB218078) exhibited a significantly stronger synergism with cisplatin in FA-proficient cells when compared to FA-deficient cells, suggesting a contribution of their FA pathway inhibitory activity to cisplatin sensitization.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22537224-10	2012	In addition, geldanamycin (HSP90 inhibitor) and two CHK1 inhibitors (UCN-01 and SB218078) exhibited a significantly stronger synergism with cisplatin in FA-proficient cells when compared to FA-deficient cells, suggesting a contribution of their FA pathway inhibitory activity to cisplatin sensitization.	Cisplatin	140-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22120678-4	2012	A phase II study of the Hsp90 inhibitor 17-AAG and trastuzumab showed that this combination therapy has anticancer activity in patients with HER2-positive metastatic breast cancer progressing on trastuzumab.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
22246317-4	2012	We studied the antineoplastic             activity of the Hsp90 inhibitor IPI-504 on GEP-NET cells, and characterized its             mechanism of action.	tanespimycin	74-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
22490666-4	2012	Here, we show that Hsp90 inhibition by 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) destabilizes phosphoinositide-dependent kinase-1 (PDK1), an upstream kinase of the protein kinase C-related kinase 2 (PRK2) responsible for phosphorylation of HCV RNA polymerase, through the proteosome pathway.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	94-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
23316269-0	2012	3-Arylcoumarin derivatives manifest anti-proliferative activity through Hsp90 inhibition.	3-arylcoumarin	0-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
23316269-2	2012	KU-398, a novobiocin analogue, and silybin were recently identified as new Hsp90 inhibitors.	ku-398	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
23316269-2	2012	KU-398, a novobiocin analogue, and silybin were recently identified as new Hsp90 inhibitors.	Novobiocin	10-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
23316269-2	2012	KU-398, a novobiocin analogue, and silybin were recently identified as new Hsp90 inhibitors.	Silybin	35-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
23316269-4	2012	Western blot analysis confirmed that the resulting 3-arylcoumarin hybrids target the Hsp90 protein folding machinery.	arylcoumarin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
22413817-2	2012	KU-32 is a novobiocin-based, C-terminal inhibitor of the molecular chaperone, heat shock protein 90 (Hsp90).	KU-32	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
22413817-2	2012	KU-32 is a novobiocin-based, C-terminal inhibitor of the molecular chaperone, heat shock protein 90 (Hsp90).	KU-32	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
22413817-2	2012	KU-32 is a novobiocin-based, C-terminal inhibitor of the molecular chaperone, heat shock protein 90 (Hsp90).	Novobiocin	11-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
22413817-2	2012	KU-32 is a novobiocin-based, C-terminal inhibitor of the molecular chaperone, heat shock protein 90 (Hsp90).	Novobiocin	11-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
22318716-0	2012	Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-102
22318716-1	2012	The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-59
22318716-1	2012	The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
22318716-2	2012	Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.	Adenosine Triphosphate	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
22318716-2	2012	Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.	Adenosine Triphosphate	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	211-216
22318716-2	2012	Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.	Adenosine Triphosphate	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
22374841-0	2012	Disease-stabilizing treatment with all-trans retinoic acid and valproic acid in acute myeloid leukemia: serum hsp70 and hsp90 levels and serum cytokine profiles are determined by the disease, patient age, and anti-leukemic treatment.	Valproic Acid	63-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
22374841-4	2012	Patients with untreated AML showed increased HSP90 levels and a distinct serum cytokine profile when compared with healthy controls, and low pre-therapy HSP90 levels were associated with a prolonged survival during treatment with ATRA + valproic acid + theophyllin.	Tretinoin	230-234	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
22374841-4	2012	Patients with untreated AML showed increased HSP90 levels and a distinct serum cytokine profile when compared with healthy controls, and low pre-therapy HSP90 levels were associated with a prolonged survival during treatment with ATRA + valproic acid + theophyllin.	Valproic Acid	237-250	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
22374841-4	2012	Patients with untreated AML showed increased HSP90 levels and a distinct serum cytokine profile when compared with healthy controls, and low pre-therapy HSP90 levels were associated with a prolonged survival during treatment with ATRA + valproic acid + theophyllin.	Theophylline	253-264	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
22374841-6	2012	Furthermore, disease-stabilizing therapy altered the serum-cytokine profile, but the correlations between HSP70/HSP90/IL-1ra/HGF were maintained only when ATRA + valproic acid were combined with theophyllin but not when combined with cytarabine.	Tretinoin	155-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
22374841-6	2012	Furthermore, disease-stabilizing therapy altered the serum-cytokine profile, but the correlations between HSP70/HSP90/IL-1ra/HGF were maintained only when ATRA + valproic acid were combined with theophyllin but not when combined with cytarabine.	Valproic Acid	162-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
22374841-6	2012	Furthermore, disease-stabilizing therapy altered the serum-cytokine profile, but the correlations between HSP70/HSP90/IL-1ra/HGF were maintained only when ATRA + valproic acid were combined with theophyllin but not when combined with cytarabine.	Theophylline	195-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
22386527-2	2012	These aminoquinazoline derivatives, represented by compound 15 (SNX-6833) or 1-(2-amino-4-methylquinazolin-7-yl)-3,6,6-trimethyl-6,7-dihydro-1H-indol-4(5H)-one, selectively bind to Hsp90 and inhibit its cellular activities at concentrations as low as single digit nanomolar.	1-(2-amino-4-methylquinazolin-7-yl)-3,6,6-trimethyl-6,7-dihydro-1h-indol-4(5h)-one	77-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
22668512-3	2012	Here we show that chemical cross-linking with ethylene glycolbis (succinimidylsuccinate), but not shorter cross-linkers, generated an abundant 240-kDa heteroconjugate of the molecular chaperone Hsp90 in different cell types.	ethylene glycolbis	46-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
22668512-3	2012	Here we show that chemical cross-linking with ethylene glycolbis (succinimidylsuccinate), but not shorter cross-linkers, generated an abundant 240-kDa heteroconjugate of the molecular chaperone Hsp90 in different cell types.	succinimidylsuccinate	66-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
22829970-0	2012	Anti-tumor activity against multiple myeloma by combination of KW-2478, an Hsp90 inhibitor, with bortezomib.	KW-2478	63-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
22829970-2	2012	We previously reported the anti-tumor activity of a novel Hsp90 inhibitor, KW-2478, in multiple myeloma (MM) as a single agent.	KW-2478	75-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
22200869-8	2012	Analysis of serial tumor biopsies in seven patients showed increased acetylation of Hsp90 and alpha-tubulin following vorinostat.	Vorinostat	118-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
22200869-9	2012	Vorinostat induces histone and alpha tubulin acetylation and functional inhibition of Hsp90 in breast cancer in vivo and can be safely combined with paclitaxel and bevacizumab.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
22286776-8	2012	Under both oxygen tensions, Hsp90 inhibition downregulated the cell cycle-associated proteins, Cdk1, Cdk4 and pRb.	Oxygen	11-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
22537224-11	2012	CONCLUSION: Our findings suggest that, despite their lack of specificity, pharmaceutical inhibition of the FA pathway by bortezomib, CA-074-Me, CHK1 inhibitors or HSP90 inhibitors may be a promising strategy to sensitize cisplatin-resistant, FA pathway-proficient tumor cells to cisplatin.	Cisplatin	221-230	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
22537224-11	2012	CONCLUSION: Our findings suggest that, despite their lack of specificity, pharmaceutical inhibition of the FA pathway by bortezomib, CA-074-Me, CHK1 inhibitors or HSP90 inhibitors may be a promising strategy to sensitize cisplatin-resistant, FA pathway-proficient tumor cells to cisplatin.	Cisplatin	279-288	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
22374940-3	2012	Inhibitors of Hsp90 ATPase cause a rapid decrease in levels of AhR, an Hsp90 client protein, and thereby block PAH-mediated induction of CYP1A1 and CYP1B1.	Polycyclic Aromatic Hydrocarbons	111-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22374940-3	2012	Inhibitors of Hsp90 ATPase cause a rapid decrease in levels of AhR, an Hsp90 client protein, and thereby block PAH-mediated induction of CYP1A1 and CYP1B1.	Polycyclic Aromatic Hydrocarbons	111-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
22374940-7	2012	Both Zyflamend and carnosol suppressed these effects of B[a]P. Notably, both Zyflamend and carnosol inhibited Hsp90 ATPase activity and caused a rapid reduction in AhR levels.	carnosol	91-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
22374940-9	2012	Collectively, these results show that Zyflamend and carnosol inhibit Hsp90 ATPase leading to reduced levels of AhR, suppression of B[a]P-mediated induction of CYP1A1 and CYP1B1, and inhibition of mutagenesis.	carnosol	52-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
22374940-10	2012	Carnosol-mediated inhibition of Hsp90 ATPase activity can help explain the chemopreventive activity of herbs such as Rosemary, which contain this phenolic antioxidant.	carnosol	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
22178220-4	2012	Hsp90 is found to interact with AMPK and to maintain its AMP-activated kinase activity, which in turn is required for the phosphorylation of its substrate, acetyl-CoA carboxylase (ACC), the key enzyme in fatty acid metabolism.	Fatty Acids	204-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22178220-6	2012	We demonstrate that Hsp90 inhibitors, including geldanamycin (GA) and mycoepoxydiene (MED), can induce the dissociation of AMPK from Hsp90, and cause a significant decrease in phosphorylation of AMPK and ACC.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
22178220-6	2012	We demonstrate that Hsp90 inhibitors, including geldanamycin (GA) and mycoepoxydiene (MED), can induce the dissociation of AMPK from Hsp90, and cause a significant decrease in phosphorylation of AMPK and ACC.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22178220-6	2012	We demonstrate that Hsp90 inhibitors, including geldanamycin (GA) and mycoepoxydiene (MED), can induce the dissociation of AMPK from Hsp90, and cause a significant decrease in phosphorylation of AMPK and ACC.	geldanamycin	62-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
22178220-6	2012	We demonstrate that Hsp90 inhibitors, including geldanamycin (GA) and mycoepoxydiene (MED), can induce the dissociation of AMPK from Hsp90, and cause a significant decrease in phosphorylation of AMPK and ACC.	geldanamycin	62-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22178220-6	2012	We demonstrate that Hsp90 inhibitors, including geldanamycin (GA) and mycoepoxydiene (MED), can induce the dissociation of AMPK from Hsp90, and cause a significant decrease in phosphorylation of AMPK and ACC.	mycoepoxydiene	70-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
22178220-6	2012	We demonstrate that Hsp90 inhibitors, including geldanamycin (GA) and mycoepoxydiene (MED), can induce the dissociation of AMPK from Hsp90, and cause a significant decrease in phosphorylation of AMPK and ACC.	mycoepoxydiene	70-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22178220-8	2012	These findings not only establish a novel interaction between Hsp90 and AMPK but also suggest a new mechanism for regulating tumour cell fatty acid metabolism.	Fatty Acids	137-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
22217465-2	2012	6-Chloro-9-(4-methoxy-3, 5-dimethyl-pyridin-2-ylmethyl)-9H-purin-2-ylamine (BIIB021), a synthetic HSP90 inhibitor, exhibited promising antitumor activity in preclinical models.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	0-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
22217465-2	2012	6-Chloro-9-(4-methoxy-3, 5-dimethyl-pyridin-2-ylmethyl)-9H-purin-2-ylamine (BIIB021), a synthetic HSP90 inhibitor, exhibited promising antitumor activity in preclinical models.	6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamine	76-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
21864883-7	2012	Nuclear HSP90 expression was significantly higher in post-chemotherapy compared to pre-chemotherapy effusions (P = .005), significantly related to previous treatment with both platinol (P = .024) and paclitaxel (P = .007).	Cisplatin	176-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21864883-7	2012	Nuclear HSP90 expression was significantly higher in post-chemotherapy compared to pre-chemotherapy effusions (P = .005), significantly related to previous treatment with both platinol (P = .024) and paclitaxel (P = .007).	Paclitaxel	200-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21864883-13	2012	However, HSP90 may be of predictive value as to who will benefit from treatment with HSP90 inhibitors to potentiate the effectiveness of platinol and paclitaxel in patients with recurrent advanced ovarian carcinoma effusions.	Cisplatin	137-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
21864883-13	2012	However, HSP90 may be of predictive value as to who will benefit from treatment with HSP90 inhibitors to potentiate the effectiveness of platinol and paclitaxel in patients with recurrent advanced ovarian carcinoma effusions.	Cisplatin	137-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
21864883-13	2012	However, HSP90 may be of predictive value as to who will benefit from treatment with HSP90 inhibitors to potentiate the effectiveness of platinol and paclitaxel in patients with recurrent advanced ovarian carcinoma effusions.	Paclitaxel	150-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
21864883-13	2012	However, HSP90 may be of predictive value as to who will benefit from treatment with HSP90 inhibitors to potentiate the effectiveness of platinol and paclitaxel in patients with recurrent advanced ovarian carcinoma effusions.	Paclitaxel	150-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
23650580-0	2012	The Hsp90 inhibitor 17-AAG represses calcium-induced cytokeratin 1 and 10 expression in HaCaT keratinocytes.	Calcium	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
23650580-2	2012	17-Allylamino-17-demethoxygeldanamycin (17-AAG) is an ansamycin antibiotic that binds to Hsp90 and inhibits its function.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
23650580-2	2012	17-Allylamino-17-demethoxygeldanamycin (17-AAG) is an ansamycin antibiotic that binds to Hsp90 and inhibits its function.	Rifabutin	54-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22270370-2	2012	We found that the threonine 7 (Thr-7) residue of heat shock protein 90alpha (Hsp90alpha) was phosphorylated immediately after DNA damage.	Threonine	18-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-87
21840346-4	2012	Mechanistically, co-chaperones alter the kinetics of the ATP-coupled conformational changes of Hsp90.	Adenosine Triphosphate	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
21840346-11	2012	Finally, I will present evidence showing how Hsp90"s active site, although being highly conserved, can be altered to show resistance to drug binding, but still maintain ATP binding and ATPase activity.	Adenosine Triphosphate	169-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
21856339-3	2012	Hsp90 function in vivo is coupled to its ability to hydrolyze ATP and this can be regulated by co-chaperones and post-translational modifications.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22001401-2	2012	HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22008467-4	2012	One of the key differences is that cytosolic Hsp90 interacts with a large number of cochaperones that regulate the ATPase activity of Hsp90 or have other functions, such as targeting clients to Hsp90.	cochaperones	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
22008467-4	2012	One of the key differences is that cytosolic Hsp90 interacts with a large number of cochaperones that regulate the ATPase activity of Hsp90 or have other functions, such as targeting clients to Hsp90.	cochaperones	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22008467-4	2012	One of the key differences is that cytosolic Hsp90 interacts with a large number of cochaperones that regulate the ATPase activity of Hsp90 or have other functions, such as targeting clients to Hsp90.	cochaperones	84-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22062686-1	2012	Hsp90 is an ATP dependent molecular chaperone protein which integrates multiple oncogenic pathways.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22062686-3	2012	Several inhibitors that act on Hsp90 by binding to its N-terminal ATP pocket have entered clinical evaluation.	Adenosine Triphosphate	66-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
22120110-5	2012	Moreover, treatment of MCF-7 cells overexpressed FLAG-GABARAPL1-6HIS with the HSP90 inhibitor 17-AAG promotes the GABARAPL1 degradation, a process that is blocked by proteasome inhibitors such as MG132, bortezomib and lactacystin.	6his	64-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
22120110-5	2012	Moreover, treatment of MCF-7 cells overexpressed FLAG-GABARAPL1-6HIS with the HSP90 inhibitor 17-AAG promotes the GABARAPL1 degradation, a process that is blocked by proteasome inhibitors such as MG132, bortezomib and lactacystin.	tanespimycin	94-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
22120110-5	2012	Moreover, treatment of MCF-7 cells overexpressed FLAG-GABARAPL1-6HIS with the HSP90 inhibitor 17-AAG promotes the GABARAPL1 degradation, a process that is blocked by proteasome inhibitors such as MG132, bortezomib and lactacystin.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	196-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
22120110-5	2012	Moreover, treatment of MCF-7 cells overexpressed FLAG-GABARAPL1-6HIS with the HSP90 inhibitor 17-AAG promotes the GABARAPL1 degradation, a process that is blocked by proteasome inhibitors such as MG132, bortezomib and lactacystin.	Bortezomib	203-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
22120110-5	2012	Moreover, treatment of MCF-7 cells overexpressed FLAG-GABARAPL1-6HIS with the HSP90 inhibitor 17-AAG promotes the GABARAPL1 degradation, a process that is blocked by proteasome inhibitors such as MG132, bortezomib and lactacystin.	lactacystin	218-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
22155720-2	2012	Key aspects of Hsp90"s molecular mechanism and its adenosine-5"-triphosphate (ATP)-controlled active cycle remain elusive.	Adenosine Triphosphate	51-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
22155720-2	2012	Key aspects of Hsp90"s molecular mechanism and its adenosine-5"-triphosphate (ATP)-controlled active cycle remain elusive.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
22270370-2	2012	We found that the threonine 7 (Thr-7) residue of heat shock protein 90alpha (Hsp90alpha) was phosphorylated immediately after DNA damage.	Threonine	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-87
22270370-8	2012	In vivo, reverse phase protein array data for tumors revealed that basal levels of Thr-7-phosphorylated Hsp90alpha were correlated with phosphorylated histone H2AX levels.	Threonine	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-114
22270370-9	2012	The Thr-7 phosphorylation of the ubiquitously produced and secreted Hsp90alpha may therefore serve as a surrogate biomarker of DNA damage.	Threonine	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-78
22151618-6	2012	These two genes, HIF-1alpha and HSP90, were further validated using siRNA gene knockdown, pharmacological inhibition using 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an inhibitor of both HSP90 and HIF-1alpha and in vivo orthotopic animal model.	tanespimycin	123-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
22151618-6	2012	These two genes, HIF-1alpha and HSP90, were further validated using siRNA gene knockdown, pharmacological inhibition using 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an inhibitor of both HSP90 and HIF-1alpha and in vivo orthotopic animal model.	tanespimycin	123-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
22151618-6	2012	These two genes, HIF-1alpha and HSP90, were further validated using siRNA gene knockdown, pharmacological inhibition using 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an inhibitor of both HSP90 and HIF-1alpha and in vivo orthotopic animal model.	tanespimycin	165-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
22181674-0	2012	The heat shock protein 90 inhibitor, AT13387, displays a long duration of action in vitro and in vivo in non-small cell lung cancer.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	37-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
22066472-0	2012	Human heat shock protein (Hsp) 90 interferes with Neisseria meningitidis adhesin A (NadA)-mediated adhesion and invasion.	arachidonyl dopamine	84-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-33
22066472-2	2012	While investigating these host factors in human epithelial cells by affinity chromatography, we discovered an unanticipated interaction of NadA with heat shock protein (Hsp) 90, a molecular chaperone.	arachidonyl dopamine	139-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-176
22066472-3	2012	The specific in vitro interaction of recombinant soluble NadA and Hsp90 was confirmed by co-immunoprecipitations, dot and far-Western blot.	arachidonyl dopamine	57-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
22066472-4	2012	Intriguingly, ADP, but not ATP, was required for this association, and the Hsp90 inhibitor 17-AAG promoted complex formation.	tanespimycin	91-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
22066472-5	2012	Hsp90 binding to an Escherichia coli strain used as carrier to express surface exposed NadA confirmed these results in live bacteria.	arachidonyl dopamine	87-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22066472-7	2012	Together, these data suggest an inverse correlation between the amount of host Hsp90 and the NadA adhesive/invasive phenotype.	arachidonyl dopamine	93-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
22066472-9	2012	Altogether our results show that variation of host Hsp90 expression or activity interferes with adhesive and invasive events driven by NadA.	arachidonyl dopamine	135-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21498475-4	2012	17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) and quercetin were used to inhibit the activity of HSP90 and HSP70.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
21498475-4	2012	17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) and quercetin were used to inhibit the activity of HSP90 and HSP70.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
21498475-4	2012	17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) and quercetin were used to inhibit the activity of HSP90 and HSP70.	Quercetin	66-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
21498475-8	2012	The co-inhibition of HSP70/HSP90 with quercetin plus 17-DMAG significantly increased apoptosis in hyperthermia-treated HNE1 cells both in vitro and in vivo.	Quercetin	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21498475-8	2012	The co-inhibition of HSP70/HSP90 with quercetin plus 17-DMAG significantly increased apoptosis in hyperthermia-treated HNE1 cells both in vitro and in vivo.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
22209975-3	2012	We decided to study LY294002, which inhibits PI-3 kinase, and tanespimycin (17AAG), which inhibits Hsp90--a chaperone for a number of proteins, including Akt kinase.	tanespimycin	62-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
22209975-3	2012	We decided to study LY294002, which inhibits PI-3 kinase, and tanespimycin (17AAG), which inhibits Hsp90--a chaperone for a number of proteins, including Akt kinase.	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
22053010-9	2012	Moreover, the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) could decrease the etoposide-induced p38 MAPK-mediated ERCC1 expression and augment the cytotoxic effect and growth inhibition by etopsoside.	tanespimycin	30-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22053010-9	2012	Moreover, the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) could decrease the etoposide-induced p38 MAPK-mediated ERCC1 expression and augment the cytotoxic effect and growth inhibition by etopsoside.	tanespimycin	70-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22053010-9	2012	Moreover, the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) could decrease the etoposide-induced p38 MAPK-mediated ERCC1 expression and augment the cytotoxic effect and growth inhibition by etopsoside.	Etoposide	97-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22053010-9	2012	Moreover, the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) could decrease the etoposide-induced p38 MAPK-mediated ERCC1 expression and augment the cytotoxic effect and growth inhibition by etopsoside.	etopsoside	208-218	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
22185909-14	2012	The GSM-induced changes in HSC70, HSP90 and alpha-synuclein are most likely linked to temperature rise.	O-(glucuronic acid 2-sulfate)-(1--4)-O-(2,5)-anhydromannitol 6-sulfate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
22253097-4	2012	Moreover, monocillin II exhibited inhibition of heat shock protein 90 (Hsp90) and depleted its target proteins, Raf-1 and A-Raf, which are involved in Ras/Raf/MEK/ERK mitogen-activated protein kinase (MAPK) pathway.	monocillin II	10-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
22253097-4	2012	Moreover, monocillin II exhibited inhibition of heat shock protein 90 (Hsp90) and depleted its target proteins, Raf-1 and A-Raf, which are involved in Ras/Raf/MEK/ERK mitogen-activated protein kinase (MAPK) pathway.	monocillin II	10-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
22271573-10	2012	Systemic treatment with the HSP90 inhibitor 17AAG reduces MIF expression and blocks growth of MIF-expressing, but not MIF-deficient, tumors.	tanespimycin	44-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
22138446-4	2012	Lack of p53 is associated with an increase in sensitivity to the combination treatment; p53+/+ cells treated with the topoisomerase I poison topotecan (TPT) arrest at G2, whereas in p53-/- cells the additional presence of the Hsp90 inhibitor geldanamycin (GA) selectively abrogates the G2M checkpoint.	Topotecan	141-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
22138446-4	2012	Lack of p53 is associated with an increase in sensitivity to the combination treatment; p53+/+ cells treated with the topoisomerase I poison topotecan (TPT) arrest at G2, whereas in p53-/- cells the additional presence of the Hsp90 inhibitor geldanamycin (GA) selectively abrogates the G2M checkpoint.	tpt	152-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
25436526-2	2012	Among the ATP-dependent chaperones, heat shock proteins (Hsp90) proteins play a special role.	Adenosine Triphosphate	10-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
22083229-3	2012	17-Allylamino-17-demethoxygeldanamycin (17-AAG) is an intravenous Hsp90 inhibitor in development for breast cancer treatment.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
22083229-3	2012	17-Allylamino-17-demethoxygeldanamycin (17-AAG) is an intravenous Hsp90 inhibitor in development for breast cancer treatment.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
22050138-0	2012	Preclinical antitumor activity of the novel heat shock protein 90 inhibitor CH5164840 against human epidermal growth factor receptor 2 (HER2)-overexpressing cancers.	CH5164840	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-65
22050138-2	2012	We identified the novel Hsp90 inhibitor, CH5164840, and investigated its induction of oncogenic client protein degradation, antiproliferative activity, and apoptosis against an NCI-N87 gastric cancer cell line and a BT-474 breast cancer cell line.	CH5164840	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
22050138-6	2012	These data demonstrate the potent antitumor efficacy of CH5164840 when administered alone, and its significant combination efficacy when combined with trastuzumab or lapatinib, supporting the clinical development of CH5164840 as an Hsp90 inhibitor for combination therapy with HER2-targeted agents against HER2-overexpressing tumors.	CH5164840	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
22050138-6	2012	These data demonstrate the potent antitumor efficacy of CH5164840 when administered alone, and its significant combination efficacy when combined with trastuzumab or lapatinib, supporting the clinical development of CH5164840 as an Hsp90 inhibitor for combination therapy with HER2-targeted agents against HER2-overexpressing tumors.	CH5164840	216-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
21413014-0	2012	Hemin, an iron-binding porphyrin, inhibits HIF-1alpha induction through its binding with heat shock protein 90.	Iron	10-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-110
21413014-8	2012	Intriguingly, hemin directly impeded the binding between heat shock protein 90 (HSP90) and HIF-1alpha, which was reversed by the addition of an excess amount of ATP required for HSP90 activity.	Adenosine Triphosphate	161-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
21413014-8	2012	Intriguingly, hemin directly impeded the binding between heat shock protein 90 (HSP90) and HIF-1alpha, which was reversed by the addition of an excess amount of ATP required for HSP90 activity.	Adenosine Triphosphate	161-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
21413014-8	2012	Intriguingly, hemin directly impeded the binding between heat shock protein 90 (HSP90) and HIF-1alpha, which was reversed by the addition of an excess amount of ATP required for HSP90 activity.	Adenosine Triphosphate	161-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
21413014-9	2012	In addition, hemin decreased the expression of client proteins of HSP90.	Hemin	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
21413014-11	2012	Moreover, treatment of protoporphyrin IX, ZnPP or Co(III)PP, but not Mn(III)PP, inhibited HIF-1alpha induction, indicating that protoporphyrin ring in association with the nature of binding metal leads to HSP90 inhibition.	protoporphyrin IX	23-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
21413014-11	2012	Moreover, treatment of protoporphyrin IX, ZnPP or Co(III)PP, but not Mn(III)PP, inhibited HIF-1alpha induction, indicating that protoporphyrin ring in association with the nature of binding metal leads to HSP90 inhibition.	zinc protoporphyrin	42-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
21413014-11	2012	Moreover, treatment of protoporphyrin IX, ZnPP or Co(III)PP, but not Mn(III)PP, inhibited HIF-1alpha induction, indicating that protoporphyrin ring in association with the nature of binding metal leads to HSP90 inhibition.	co(iii)pp	50-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
21413014-11	2012	Moreover, treatment of protoporphyrin IX, ZnPP or Co(III)PP, but not Mn(III)PP, inhibited HIF-1alpha induction, indicating that protoporphyrin ring in association with the nature of binding metal leads to HSP90 inhibition.	protoporphyrin IX	23-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
20683637-1	2012	PURPOSE: A Phase II study to screen for anti-melanoma activity of the heat shock protein 90 (HSP90) inhibitor, 17-AAG (17-allylamino-17-demethoxygeldanamycin) was performed.	tanespimycin	119-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-91
20683637-1	2012	PURPOSE: A Phase II study to screen for anti-melanoma activity of the heat shock protein 90 (HSP90) inhibitor, 17-AAG (17-allylamino-17-demethoxygeldanamycin) was performed.	tanespimycin	119-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
21465483-7	2012	Moreover, the Hsp90 inhibitor radicicol (RA) prevents accumulation of ubiquitinated caALK5 and phospho-Hsp27 in the cytoskeletal fraction and restore the decreased EC permeability induced by caALK5.	monorden	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21465483-7	2012	Moreover, the Hsp90 inhibitor radicicol (RA) prevents accumulation of ubiquitinated caALK5 and phospho-Hsp27 in the cytoskeletal fraction and restore the decreased EC permeability induced by caALK5.	monorden	41-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21767894-0	2012	The anti-proliferative effect of heat shock protein 90 inhibitor, 17-DMAG, on non-small-cell lung cancers being resistant to EGFR tyrosine kinase inhibitor.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	66-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-54
22144665-0	2012	Ganetespib, a unique triazolone-containing Hsp90 inhibitor, exhibits potent antitumor activity and a superior safety profile for cancer therapy.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
22144665-0	2012	Ganetespib, a unique triazolone-containing Hsp90 inhibitor, exhibits potent antitumor activity and a superior safety profile for cancer therapy.	5-((3-(((3,5-bis(trifluoromethyl)phenyl)methyl)oxy)-2-phenylpiperidino)methyl)-3-oxo-1,2,4-triazolone	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
22144665-2	2012	Ganetespib (formerly known as STA-9090) is a unique resorcinolic triazolone inhibitor of Hsp90 that is currently in clinical trials for a number of human cancers.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22144665-2	2012	Ganetespib (formerly known as STA-9090) is a unique resorcinolic triazolone inhibitor of Hsp90 that is currently in clinical trials for a number of human cancers.	STA 9090	30-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22144665-2	2012	Ganetespib (formerly known as STA-9090) is a unique resorcinolic triazolone inhibitor of Hsp90 that is currently in clinical trials for a number of human cancers.	5-((3-(((3,5-bis(trifluoromethyl)phenyl)methyl)oxy)-2-phenylpiperidino)methyl)-3-oxo-1,2,4-triazolone	65-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22144665-4	2012	Ganetespib treatment rapidly induced the degradation of known Hsp90 client proteins, displayed superior potency to the ansamycin inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG), and exhibited sustained activity even with short exposure times.	STA 9090	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
22144665-8	2012	Taken together, this preclinical activity profile indicates that ganetespib may have broad application for a variety of human malignancies, and with select mechanistic and safety advantages over other first- and second-generation Hsp90 inhibitors.	STA 9090	65-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-235
22277058-5	2012	METHODS: We quantitatively profiled the effects of Hsp90 inhibition by geldanamycin on the kinome of one primary (Hs68) and three tumour cell lines (SW480, U2OS, A549) by affinity proteomics based on immobilized broad spectrum kinase inhibitors ("kinobeads").	geldanamycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
22277058-10	2012	RESULTS: We measured relative abundances of &gt; 140 protein kinases from the four cell lines in response to geldanamycin treatment and identified many new potential Hsp90 substrates.	geldanamycin	109-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
22277058-12	2012	Co-treatment with the proteasome inhibitor MG132 enabled us to classify 64 kinases as true Hsp90 clients.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	43-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
22192591-0	2012	Design and synthesis of novel macrocyclic 2-amino-6-arylpyrimidine Hsp90 inhibitors.	2-amino-6-arylpyrimidine	42-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
22192591-1	2012	Macrocyclic compounds bearing a 2-amino-6-arylpyrimidine moiety were identified as potent heat shock protein 90 (Hsp90) inhibitors by modification of 2-amino-6-aryltriazine derivative (CH5015765).	2-amino-6-arylpyrimidine	32-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-111
22192591-1	2012	Macrocyclic compounds bearing a 2-amino-6-arylpyrimidine moiety were identified as potent heat shock protein 90 (Hsp90) inhibitors by modification of 2-amino-6-aryltriazine derivative (CH5015765).	2-amino-6-arylpyrimidine	32-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
22192591-1	2012	Macrocyclic compounds bearing a 2-amino-6-arylpyrimidine moiety were identified as potent heat shock protein 90 (Hsp90) inhibitors by modification of 2-amino-6-aryltriazine derivative (CH5015765).	2-amino-6-aryltriazine	150-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-111
22192591-1	2012	Macrocyclic compounds bearing a 2-amino-6-arylpyrimidine moiety were identified as potent heat shock protein 90 (Hsp90) inhibitors by modification of 2-amino-6-aryltriazine derivative (CH5015765).	2-amino-6-aryltriazine	150-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
22192591-1	2012	Macrocyclic compounds bearing a 2-amino-6-arylpyrimidine moiety were identified as potent heat shock protein 90 (Hsp90) inhibitors by modification of 2-amino-6-aryltriazine derivative (CH5015765).	CH5015765	185-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-111
22192591-1	2012	Macrocyclic compounds bearing a 2-amino-6-arylpyrimidine moiety were identified as potent heat shock protein 90 (Hsp90) inhibitors by modification of 2-amino-6-aryltriazine derivative (CH5015765).	CH5015765	185-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
22192591-2	2012	We employed a macrocyclic structure as a skeleton of new inhibitors to mimic the geldanamycin-Hsp90 interactions.	geldanamycin	81-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
22192591-3	2012	Among the identified inhibitors, CH5164840 showed high binding affinity for N-terminal Hsp90alpha (K(d)=0.52nM) and strong anti-proliferative activity against human cancer cell lines (HCT116 IC(50)=0.15muM, NCI-N87 IC(50)=0.066muM).	CH5164840	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-97
22241783-0	2012	Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization.	Lysine	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
22063096-2	2012	In previous work, a model Hsp90 substrate revealed an activation process in which substrate binding accelerates a large open/closed conformational change required for ATP hydrolysis by Hsp90.	Adenosine Triphosphate	167-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
22063096-2	2012	In previous work, a model Hsp90 substrate revealed an activation process in which substrate binding accelerates a large open/closed conformational change required for ATP hydrolysis by Hsp90.	Adenosine Triphosphate	167-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
22123826-5	2012	To characterize the mechanism of mHtt degradation, we used the potent and selective Hsp90 inhibitor NVP-AUY922.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
22123826-7	2012	In HN10 cells, Hsp90 inhibition by NVP-AUY922 enhanced mHtt clearance in the absence of any detectable Hsp70 induction.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	39-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
22123826-7	2012	In HN10 cells, Hsp90 inhibition by NVP-AUY922 enhanced mHtt clearance in the absence of any detectable Hsp70 induction.	mhtt	55-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
22123826-9	2012	Together, these data provided evidence that direct inhibition of Hsp90 chaperone function was crucial for mHtt degradation rather than heat shock response induction and Hsp70 up-regulation.	mhtt	106-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
22123826-12	2012	Our data suggest that Htt is an Hsp90 client protein and that Hsp90 inhibition may provide a means to reduce mHtt in HD.	mhtt	109-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
22123826-12	2012	Our data suggest that Htt is an Hsp90 client protein and that Hsp90 inhibition may provide a means to reduce mHtt in HD.	mhtt	109-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
22128174-0	2012	Modulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitination.	Heme	14-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
22128174-7	2012	Treatment of cells with N(G)-nitro-L-arginine, a slowly reversible competitive inhibitor that stabilizes nNOS, decreases both nNOS ubiquitination and binding of Hsp90, Hsp70, and CHIP.	Nitroarginine	24-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
22128174-8	2012	Treatment with the calcium ionophore A23187, which increases Ca(2+)-calmodulin binding to nNOS, increases nNOS ubiquitination and binding of Hsp90, Hsp70, and CHIP in a manner that is specific for changes in the heme/substrate binding cleft.	Calcium	19-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
22128174-8	2012	Treatment with the calcium ionophore A23187, which increases Ca(2+)-calmodulin binding to nNOS, increases nNOS ubiquitination and binding of Hsp90, Hsp70, and CHIP in a manner that is specific for changes in the heme/substrate binding cleft.	Calcimycin	37-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
22128174-8	2012	Treatment with the calcium ionophore A23187, which increases Ca(2+)-calmodulin binding to nNOS, increases nNOS ubiquitination and binding of Hsp90, Hsp70, and CHIP in a manner that is specific for changes in the heme/substrate binding cleft.	Heme	212-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
22128174-9	2012	Both Hsp90 and Hsp70 are bound to the expressed nNOS oxygenase domain, which contains the heme/substrate binding cleft, but not to the reductase domain, and binding is increased to an expressed fragment containing both the oxygenase domain and the calmodulin binding site.	Heme	90-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
23606927-2	2012	Extensive structural modifications to novobiocin, the first Hsp90 C-terminal inhibitor discovered, have produced a library of novobiocin analogues and revealed some structure-activity relationships.	Novobiocin	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
21998134-1	2012	OBJECTIVE: Geranylgeranylacetone (GGA) induces expression of heat shock protein 90 (Hsp90), an adaptor molecule for assembly of endothelial nitric oxide synthase (eNOS) phosphorylation complex.	geranylgeranylacetone	11-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-82
21998134-1	2012	OBJECTIVE: Geranylgeranylacetone (GGA) induces expression of heat shock protein 90 (Hsp90), an adaptor molecule for assembly of endothelial nitric oxide synthase (eNOS) phosphorylation complex.	geranylgeranylacetone	11-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	trichostatin A	15-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	trichostatin A	15-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	263-268
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	Docetaxel	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	Docetaxel	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	263-268
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	trichostatin A	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	trichostatin A	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	263-268
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	Erlotinib Hydrochloride	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
22994780-7	2012	Treatment with TSA/TXT or TSA/erlotinib led to a significant increase of cleaved caspase-3 expression, also resulting in elevated acetylation of alpha-tubulin or hsp90 and decreased expression of EGFR, which was negatively associated with the level of acetylated hsp90.	Erlotinib Hydrochloride	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	263-268
21919888-3	2012	It is now well accepted that both ATP binding and co-chaperone association are involved in regulating the Hsp90 chaperone machinery.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
21919888-8	2012	Thr90 phosphorylation affects the binding affinity of Hsp90alpha to ATP.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-64
22687408-3	2012	The HSP90 inhibitors geldanamycin (GA), 17(allylamino)-17-demethoxygeldanamycin (17-AAG), and radicicol dramatically inhibited cell proliferation and induced apoptosis of PEL cells through caspase activation.	geldanamycin	21-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22687408-3	2012	The HSP90 inhibitors geldanamycin (GA), 17(allylamino)-17-demethoxygeldanamycin (17-AAG), and radicicol dramatically inhibited cell proliferation and induced apoptosis of PEL cells through caspase activation.	geldanamycin	35-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22687408-3	2012	The HSP90 inhibitors geldanamycin (GA), 17(allylamino)-17-demethoxygeldanamycin (17-AAG), and radicicol dramatically inhibited cell proliferation and induced apoptosis of PEL cells through caspase activation.	tanespimycin	40-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22215907-1	2012	Heat shock protein (Hsp) 90 is an ATP-dependent molecular chaperone that is exploited by malignant cells to support activated oncoproteins, including many cancer-associated kinases and transcription factors, and it is essential for oncogenic transformation.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-27
22215907-3	2012	Investigators established Hsp90"s druggability using the natural products geldanamycin and radicicol, which mimic the unusual ATP structure adopted in the chaperone"s N-terminal nucleotide-binding pocket and cause potent and selective blockade of ATP binding/hydrolysis, inhibit chaperone function, deplete oncogenic clients, and show antitumor activity.	geldanamycin	74-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
22215907-3	2012	Investigators established Hsp90"s druggability using the natural products geldanamycin and radicicol, which mimic the unusual ATP structure adopted in the chaperone"s N-terminal nucleotide-binding pocket and cause potent and selective blockade of ATP binding/hydrolysis, inhibit chaperone function, deplete oncogenic clients, and show antitumor activity.	monorden	91-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
22215907-3	2012	Investigators established Hsp90"s druggability using the natural products geldanamycin and radicicol, which mimic the unusual ATP structure adopted in the chaperone"s N-terminal nucleotide-binding pocket and cause potent and selective blockade of ATP binding/hydrolysis, inhibit chaperone function, deplete oncogenic clients, and show antitumor activity.	Adenosine Triphosphate	126-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
22215907-3	2012	Investigators established Hsp90"s druggability using the natural products geldanamycin and radicicol, which mimic the unusual ATP structure adopted in the chaperone"s N-terminal nucleotide-binding pocket and cause potent and selective blockade of ATP binding/hydrolysis, inhibit chaperone function, deplete oncogenic clients, and show antitumor activity.	Adenosine Triphosphate	247-250	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
23167798-0	2012	Biological evaluation of 3-acyl-2-arylamino-1,4-naphthoquinones as inhibitors of Hsp90 chaperoning function.	3-acyl-2-arylamino-1,4-naphthoquinones	25-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
23167798-4	2012	We have shown that ascorbate- driven menadione-redox cycling inhibits Hsp90 activity by provoking an N-terminal cleavage of the protein, inducing the degradation of several of its client proteins.	Ascorbic Acid	19-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
23167798-4	2012	We have shown that ascorbate- driven menadione-redox cycling inhibits Hsp90 activity by provoking an N-terminal cleavage of the protein, inducing the degradation of several of its client proteins.	Vitamin K 3	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
23167798-5	2012	Since the mechanism involves an oxidative stress, we explored the effect of a series of diverse donor-acceptor 3-acyl-2-phenylamino 1,4-naphthoquinones on Hsp90 integrity, in the presence of ascorbate.	3-acyl-2-phenylamino 1,4-naphthoquinones	111-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
23167798-6	2012	Results show that quinone-derivatives that bear two electroactive groups (namely quinone and nitro) exhibit the highest inhibitory activity (Hsp90 cleavage and cell death).	quinone	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
23167798-6	2012	Results show that quinone-derivatives that bear two electroactive groups (namely quinone and nitro) exhibit the highest inhibitory activity (Hsp90 cleavage and cell death).	quinone	81-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
23167798-6	2012	Results show that quinone-derivatives that bear two electroactive groups (namely quinone and nitro) exhibit the highest inhibitory activity (Hsp90 cleavage and cell death).	nitro	93-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
23167798-8	2012	As observed with other redox cycling quinones, the protein cleavage is blocked in the presence of N-terminal Hsp90 inhibitors suggesting that the availability or occupancy of nucleotide binding site in the N-terminal pocket of Hsp90 plays a critical role.	Quinones	37-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
23167798-8	2012	As observed with other redox cycling quinones, the protein cleavage is blocked in the presence of N-terminal Hsp90 inhibitors suggesting that the availability or occupancy of nucleotide binding site in the N-terminal pocket of Hsp90 plays a critical role.	Quinones	37-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	227-232
21830942-1	2012	We investigated whether the combined treatment of 17-(allylamino)-17-demethoxygeldanamycin (17-AAG), an inhibitor of heat-shock protein 90 (hsp90), and celecoxib, an inhibitor of cyclooxygenase-2, can cooperatively enhance the radiosensitivity of various human cancer cells.	tanespimycin	50-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-138
21830942-1	2012	We investigated whether the combined treatment of 17-(allylamino)-17-demethoxygeldanamycin (17-AAG), an inhibitor of heat-shock protein 90 (hsp90), and celecoxib, an inhibitor of cyclooxygenase-2, can cooperatively enhance the radiosensitivity of various human cancer cells.	tanespimycin	50-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
22915839-0	2012	17AAG Treatment Accelerates Doxorubicin Induced Cellular Senescence: Hsp90 Interferes with Enforced Senescence of Tumor Cells.	tanespimycin	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21983172-6	2012	We also observed a reduction of UBR1 protein levels in geldanamycin-treated mouse embryonic fibroblasts and human breast cancer cells, suggesting that UBR1 is an Hsp90 client.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
21983172-8	2012	Our findings show that UBR1 function is conserved in controlling the levels of Hsp90-dependent protein kinases upon geldanamycin treatment, and suggest that it plays a role in determining the sensitivity of cancer cells to the chemotherapeutic effects of Hsp90 inhibitors.	geldanamycin	116-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
21983172-8	2012	Our findings show that UBR1 function is conserved in controlling the levels of Hsp90-dependent protein kinases upon geldanamycin treatment, and suggest that it plays a role in determining the sensitivity of cancer cells to the chemotherapeutic effects of Hsp90 inhibitors.	geldanamycin	116-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	255-260
23197975-1	2012	KU-32 is a novel, novobiocin-based Hsp90 inhibitor that protects against neuronal glucotoxicity and reverses multiple clinical indices of diabetic peripheral neuropathy in a rodent model.	KU-32	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
23197975-1	2012	KU-32 is a novel, novobiocin-based Hsp90 inhibitor that protects against neuronal glucotoxicity and reverses multiple clinical indices of diabetic peripheral neuropathy in a rodent model.	Novobiocin	18-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
22991673-0	2012	In Silico Studies on Fungal Metabolite against Skin Cancer Protein (4,5-Diarylisoxazole HSP90 Chaperone).	4,5-diarylisoxazole	68-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
21985437-9	2012	We concluded that the GA-mediated protection against OGD/zVAD-induced neuronal injury was associated with enhanced RIP1 protein instability by decreasing Hsp90 protein level.	geldanamycin	22-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	154-159
23037999-6	2012	Among them, heat shock protein 90 (HSP90) and HSP70 are of interest because covalent modification of these chaperones causes activation of heat shock factor-1, which plays a role in the cellular response against electrophiles such as 1,4-NQ.	1,4-naphthoquinone	234-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-33
23037999-6	2012	Among them, heat shock protein 90 (HSP90) and HSP70 are of interest because covalent modification of these chaperones causes activation of heat shock factor-1, which plays a role in the cellular response against electrophiles such as 1,4-NQ.	1,4-naphthoquinone	234-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
23038012-9	2012	In HeLa cells, however, GA treatment decreased the release of AA via cytosolic phospholipase A(2)alpha"s activation probably because of dysfunctional Hsp90 clients.	geldanamycin	24-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
22222448-7	2012	Additionally, a protocol describing the expression, purification, and crystallization of the ATP-binding domain of the important cancer target Hsp90 provides the reader with an example of methods that can be adapted to a wider set of crystallographic target proteins.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
21800052-0	2012	Radicicol, an inhibitor of Hsp90, enhances TRAIL-induced apoptosis in human epithelial ovarian carcinoma cells by promoting activation of apoptosis-related proteins.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
23233786-6	2012	Geldanamycin, an inhibitor of Hsp90, was used to investigate the roles of Hsp90 in CB2 receptor-mediated ERK1/2 phosphorylation and actin cytoskeleton remodeling.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
23233786-8	2012	Treatment of TM cells with geldanamycin significantly inhibited the interaction of Hsp90 with the CB2 receptor.	geldanamycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
23233786-9	2012	Disruption of the CB2/Hsp90 interaction by treating TM cells with geldanamycin inhibited CB2 receptor-mediated ERK1/2 phosphorylation, as well as actin cytoskeleton remodeling.	geldanamycin	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
23285036-10	2012	Finally we demonstrate that the CaM KMT interacts with the middle portion of the Hsp90 molecular chaperon and is probably a client protein since it is degraded upon treatment of cells with the Hsp90 inhibitor geldanamycin.	geldanamycin	209-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
23285036-10	2012	Finally we demonstrate that the CaM KMT interacts with the middle portion of the Hsp90 molecular chaperon and is probably a client protein since it is degraded upon treatment of cells with the Hsp90 inhibitor geldanamycin.	geldanamycin	209-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
23300891-12	2012	Moreover, these protrusions were suppressed by colchicine or inhibitors of heat shock protein 90 (HSP-90) and protein phosphatase 2A.	Colchicine	47-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-104
23272037-0	2012	Dexamethasone regulates CFTR expression in Calu-3 cells with the involvement of chaperones HSP70 and HSP90.	Dexamethasone	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
23272037-10	2012	Assessment of the B band of CFTR within 15 min of metabolic pulse labeling showed a 1.5-fold increase in CFTR protein after treatment with dexamethasone for 24 h. Chaperone 90 (HSP90) binding to CFTR increased 1.55-fold after treatment with dexamethasone for 24 h, whereas chaperone 70 (HSP70) binding decreased 0.30 fold in an immunoprecipitation assay.	Dexamethasone	139-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
23272037-10	2012	Assessment of the B band of CFTR within 15 min of metabolic pulse labeling showed a 1.5-fold increase in CFTR protein after treatment with dexamethasone for 24 h. Chaperone 90 (HSP90) binding to CFTR increased 1.55-fold after treatment with dexamethasone for 24 h, whereas chaperone 70 (HSP70) binding decreased 0.30 fold in an immunoprecipitation assay.	Dexamethasone	241-254	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
23272037-11	2012	CONCLUSION: Mature wild-type CFTR protein is regulated by dexamethasone post transcription, involving cotranslational mechanisms with HSP90 and HSP70, which enhances maturation and expression of wild-type CFTR.	Dexamethasone	58-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
22984537-0	2012	Co-crystalization and in vitro biological characterization of 5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors.	5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole	62-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
22984537-1	2012	A potential therapeutic strategy for targeting cancer that has gained much interest is the inhibition of the ATP binding and ATPase activity of the molecular chaperone Hsp90.	Adenosine Triphosphate	109-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
22984537-2	2012	We have determined the structure of the human Hsp90alpha N-terminal domain in complex with a series of 5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazoles.	5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazoles	103-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-56
22984537-8	2012	This work provides a framework for the further optimization of thiadiazole inhibitors of Hsp90.	Thiadiazoles	63-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
22984537-9	2012	Importantly, we demonstrate that the thiadiazole inhibitors display a more limited core set of interactions relative to the clinical trial candidate NVP-AUY922, and consequently may be less susceptible to resistance derived through mutations in Hsp90.	Thiadiazoles	37-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	245-250
22916240-0	2012	Natural iminosugar (+)-lentiginosine inhibits ATPase and chaperone activity of hsp90.	Imino Sugars	8-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
22916240-0	2012	Natural iminosugar (+)-lentiginosine inhibits ATPase and chaperone activity of hsp90.	lentiginosine	19-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
22916240-5	2012	Our result suggested that the middle domain of Hsp90, as opposed to its ATP-binding pocket, is a promising binding site for new classes of Hsp90 inhibitors with multi-target anti-cancer potential.	Adenosine Triphosphate	72-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
22848402-0	2012	Hsp90 is cleaved by reactive oxygen species at a highly conserved N-terminal amino acid motif.	Reactive Oxygen Species	20-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22848402-2	2012	In this study, we demonstrate that free radicals formed during oxidative stress conditions can cleave Hsp90.	Free Radicals	35-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
22848402-6	2012	Using a proteomic analysis, we determined that the cleavage occurs in a conserved motif of the N-terminal nucleotide binding site, between Ile-126 and Gly-127 in Hsp90beta, and between Ile-131 and Gly-132 in Hsp90alpha.	Isoleucine	139-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-218
22848402-6	2012	Using a proteomic analysis, we determined that the cleavage occurs in a conserved motif of the N-terminal nucleotide binding site, between Ile-126 and Gly-127 in Hsp90beta, and between Ile-131 and Gly-132 in Hsp90alpha.	Glycine	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-218
22848402-6	2012	Using a proteomic analysis, we determined that the cleavage occurs in a conserved motif of the N-terminal nucleotide binding site, between Ile-126 and Gly-127 in Hsp90beta, and between Ile-131 and Gly-132 in Hsp90alpha.	Isoleucine	185-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-218
22848402-6	2012	Using a proteomic analysis, we determined that the cleavage occurs in a conserved motif of the N-terminal nucleotide binding site, between Ile-126 and Gly-127 in Hsp90beta, and between Ile-131 and Gly-132 in Hsp90alpha.	Glycine	197-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-218
22701533-2	2012	We have previously demonstrated that a withanolide, tubocapsenolide A, induced cycle arrest and apoptosis in human breast cancer cells, which was associated with the inhibition of heat shock protein 90 (Hsp90).	Withanolides	39-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-201
22701533-2	2012	We have previously demonstrated that a withanolide, tubocapsenolide A, induced cycle arrest and apoptosis in human breast cancer cells, which was associated with the inhibition of heat shock protein 90 (Hsp90).	Withanolides	39-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
22701533-2	2012	We have previously demonstrated that a withanolide, tubocapsenolide A, induced cycle arrest and apoptosis in human breast cancer cells, which was associated with the inhibition of heat shock protein 90 (Hsp90).	TUBOCAPSENOLIDE A	52-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-201
22701533-2	2012	We have previously demonstrated that a withanolide, tubocapsenolide A, induced cycle arrest and apoptosis in human breast cancer cells, which was associated with the inhibition of heat shock protein 90 (Hsp90).	TUBOCAPSENOLIDE A	52-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
22701533-4	2012	Our data show that the 2,3-unsaturated double bond-containing withanolides inhibited Hsp90 function, as evidenced by selective depletion of Hsp90 client proteins and induction of Hsp70.	2,3-unsaturated	23-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
22701533-4	2012	Our data show that the 2,3-unsaturated double bond-containing withanolides inhibited Hsp90 function, as evidenced by selective depletion of Hsp90 client proteins and induction of Hsp70.	2,3-unsaturated	23-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
22701533-4	2012	Our data show that the 2,3-unsaturated double bond-containing withanolides inhibited Hsp90 function, as evidenced by selective depletion of Hsp90 client proteins and induction of Hsp70.	Withanolides	62-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
22701533-4	2012	Our data show that the 2,3-unsaturated double bond-containing withanolides inhibited Hsp90 function, as evidenced by selective depletion of Hsp90 client proteins and induction of Hsp70.	Withanolides	62-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
22701533-5	2012	The inhibitory effect of the withanolides on Hsp90 chaperone activity was further confirmed using in vivo heat shock luciferase activity recovery assays.	Withanolides	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
22701533-6	2012	Importantly, Hsp90 inhibition by the withanolides was correlated with their ability to induce cancer cell death.	Withanolides	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
22701533-7	2012	In addition, the withanolides reduced constitutive NF-kappaB activation by depleting IkappaB kinase complex (IKK) through inhibition of Hsp90.	Withanolides	17-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
22701533-8	2012	In estrogen receptor (ER)-positive MCF-7 cells, the withanolides also reduced the expression of ER, and this may be partly due to Hsp90 inhibition.	Withanolides	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
22701533-9	2012	Taken together, our results suggest that Hsp90 inhibition is a general feature of cytotoxic withanolides and plays an important role in their anticancer activity.	Withanolides	92-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
22624053-5	2012	We have found that these functional motifs may be utilized by the molecular chaperone machinery to act collectively as central regulators of Hsp90 dynamics and activity, including the inter-domain communications, control of ATP hydrolysis, and protein client binding.	Adenosine Triphosphate	224-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
22655030-0	2012	Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90.	aryl-dihydroxyphenyl-thiadiazole	18-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
22655030-2	2012	Here we present a detailed thermodynamic study of binding of aryl-dihydroxyphenyl-thiadiazole inhibitor series to recombinant human Hsp90 alpha isozyme.	aryl-dihydroxyphenyl-thiadiazole	61-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-143
22523597-0	2012	The HSP90 inhibitor NVP-AUY922 radiosensitizes by abrogation of homologous recombination resulting in mitotic entry with unresolved DNA damage.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	24-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
22384180-8	2012	Subsequently, we found that As(2)O(3) treatment in a dose- and time-dependent fashion markedly increased the level of acetylated alpha-tubulin and acetylated Hsp90, and inhibited the chaperone association with IKKalpha activities and increased degradation of IKKalpha.	(2)o(3)	30-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
22347373-3	2012	By comparing the toxicity of the HSP90 inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) to two known cytostatic compounds, colchicine and gemcitabine, we provide evidence that 17-AAG exerts its antiviral effects indirectly through slowing cell growth.	tanespimycin	50-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
22347373-3	2012	By comparing the toxicity of the HSP90 inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) to two known cytostatic compounds, colchicine and gemcitabine, we provide evidence that 17-AAG exerts its antiviral effects indirectly through slowing cell growth.	tanespimycin	92-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
22347373-3	2012	By comparing the toxicity of the HSP90 inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) to two known cytostatic compounds, colchicine and gemcitabine, we provide evidence that 17-AAG exerts its antiviral effects indirectly through slowing cell growth.	tanespimycin	188-194	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
22615574-8	2012	To discover strategies to abrogate echinocandin resistance, we focused on the molecular chaperone Hsp90 and downstream effector calcineurin.	Echinocandins	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
22615574-10	2012	Hsp90 and calcineurin were required for caspofungin-dependent FKS2 induction, providing a mechanism governing echinocandin resistance.	Echinocandins	110-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23209418-3	2012	All Hsp90 inhibitors exhibited nanomolar EC(50) in culture and AUY922 reduced tumor burden in a xenograft model of KS.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	63-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21647838-10	2012	In addition, the resorcinol substructure was used to select commercially available compounds that were filtered using focussed docking in the Hsp90 active site to select further sets of compounds for assay.	resorcinol	17-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
21924824-0	2011	A novel C-terminal HSP90 inhibitor KU135 induces apoptosis and cell cycle arrest in melanoma cells.	KU135	35-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
21924824-2	2011	We investigated a novobiocin-derived Hsp90 C-terminal inhibitor, KU135, for anti-proliferative effects in melanoma cells.	Novobiocin	18-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
21924824-2	2011	We investigated a novobiocin-derived Hsp90 C-terminal inhibitor, KU135, for anti-proliferative effects in melanoma cells.	KU135	65-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
21924824-4	2011	KU135 induced a more potent anti-proliferative effect in most melanoma cells versus N-terminal Hsp90 inhibitor 17AAG.	tanespimycin	111-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
21924824-6	2011	KU135 reduced levels of Hsp90 client proteins Akt, BRAF, RAF-1, cyclin B and cdc25.	KU135	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
21998300-4	2011	The nucleolin level decreased upon geldanamycin treatment, and Hsp90 maintained the cyclin-dependent kinase 1 (CDK1) activity to phosphorylate nucleolin at Thr-641/707.	Threonine	156-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
22066525-1	2011	A structural investigation on the isoxazole scaffold led to the discovery of 3,4-isoxazolediamide compounds endowed with potent Hsp90 inhibitory properties.	Isoxazoles	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
22066525-1	2011	A structural investigation on the isoxazole scaffold led to the discovery of 3,4-isoxazolediamide compounds endowed with potent Hsp90 inhibitory properties.	3,4-isoxazolediamide	77-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
22066525-2	2011	We have found that compounds possessing a nitrogen atom directly attached to the C-4 heterocycle ring possess in vitro Hsp90 inhibitory properties at least comparable to those of the structurally related 4,5-diarylisoxazole derivatives.	Nitrogen	42-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
22066525-4	2011	The 3,4-isoxazolediamides were also very effective in causing dramatic depletion of the examined client proteins and, as expected for the Hsp90 inhibitors, always induced a very strong increase in the expression levels of the chaperone Hsp70.	3,4-isoxazolediamides	4-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
21932796-2	2011	A series of resorcylic acid macrolactams, nitrogen analogues of the naturally occurring macrolactone radicicol, have been prepared by chemical synthesis and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents.	2,3-Dihydroxybenzoic acid	12-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-205
21932796-2	2011	A series of resorcylic acid macrolactams, nitrogen analogues of the naturally occurring macrolactone radicicol, have been prepared by chemical synthesis and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents.	2,3-Dihydroxybenzoic acid	12-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
21932796-2	2011	A series of resorcylic acid macrolactams, nitrogen analogues of the naturally occurring macrolactone radicicol, have been prepared by chemical synthesis and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents.	monorden	101-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-205
21932796-2	2011	A series of resorcylic acid macrolactams, nitrogen analogues of the naturally occurring macrolactone radicicol, have been prepared by chemical synthesis and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents.	monorden	101-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
21932796-5	2011	These new resorcylic acid lactams exhibit metabolic stability greater than that of related lactone counterparts, while co-crystallization of three macrolactams with the N-terminal domain ATP site of Hsp90 confirms that they bind in a similar way to the natural product radicicol and to our previous synthetic lactone analogues.	resorcylic acid lactams	10-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
21932796-5	2011	These new resorcylic acid lactams exhibit metabolic stability greater than that of related lactone counterparts, while co-crystallization of three macrolactams with the N-terminal domain ATP site of Hsp90 confirms that they bind in a similar way to the natural product radicicol and to our previous synthetic lactone analogues.	Lactones	91-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
21932796-5	2011	These new resorcylic acid lactams exhibit metabolic stability greater than that of related lactone counterparts, while co-crystallization of three macrolactams with the N-terminal domain ATP site of Hsp90 confirms that they bind in a similar way to the natural product radicicol and to our previous synthetic lactone analogues.	Adenosine Triphosphate	187-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
21932796-5	2011	These new resorcylic acid lactams exhibit metabolic stability greater than that of related lactone counterparts, while co-crystallization of three macrolactams with the N-terminal domain ATP site of Hsp90 confirms that they bind in a similar way to the natural product radicicol and to our previous synthetic lactone analogues.	Lactones	309-316	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
22030396-6	2011	Uncoupling FKBP38 from Hsp90 by substituting a conserved lysine in the TPR domain modestly enhances CFTR maturation and further reduces its synthesis.	Lysine	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
22134243-10	2011	These results encourage clinical trials of Hsp90 inhibitors to overcome CRT resistance in patients with MIBC.	4-METHYL-2-PENTANOL	104-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
22087583-0	2011	Remarkable stereospecific conjugate additions to the Hsp90 inhibitor celastrol.	celastrol	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
22087583-1	2011	Celastrol, an important natural product and Hsp90 inhibitor with a wide range of biological and medical activities and broad use as a biological probe, acts by an as yet undetermined mode of action.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
21882818-4	2011	Currently, various Hsp90 inhibitors that bind to Hsp90 at its ATP-binding site are in preclinical and clinical trials.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
21882818-4	2011	Currently, various Hsp90 inhibitors that bind to Hsp90 at its ATP-binding site are in preclinical and clinical trials.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
21882818-5	2011	Some of the most promising Hsp90 ATP-binding site inhibitors are the well characterized geldanamycin derivative 17-AAG and the recently described compounds PU-H71 and NVP-AUY922.	Adenosine Triphosphate	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21882818-5	2011	Some of the most promising Hsp90 ATP-binding site inhibitors are the well characterized geldanamycin derivative 17-AAG and the recently described compounds PU-H71 and NVP-AUY922.	geldanamycin	88-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21882818-5	2011	Some of the most promising Hsp90 ATP-binding site inhibitors are the well characterized geldanamycin derivative 17-AAG and the recently described compounds PU-H71 and NVP-AUY922.	tanespimycin	112-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21967761-5	2011	The capabilities of MDpocket are illustrated for three relevant cases: (i) the detection of transient subpockets using an ensemble of crystal structures of HSP90; (ii) the detection of known xenon binding sites and migration pathways in myoglobin; and (iii) the identification of suitable pockets for molecular docking in P38 Map kinase.	Xenon	191-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
22014546-0	2011	Synthesis and biological evaluation of arylated novobiocin analogs as Hsp90 inhibitors.	Novobiocin	48-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
22014546-1	2011	Novobiocin analogs lacking labile glycosidic ether have been designed, synthesized and evaluated for Hsp90 inhibitory activity.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
22014826-1	2011	Described is the synthesis of three different fluorescein-tagged derivatives of a macrocycle, and their binding affinity to heat shock protein 90 (Hsp90).	Fluorescein	46-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-145
22014826-1	2011	Described is the synthesis of three different fluorescein-tagged derivatives of a macrocycle, and their binding affinity to heat shock protein 90 (Hsp90).	Fluorescein	46-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
22014826-2	2011	Using fluorescence polarization anisotropy, we report the binding affinity of these fluorescein-labeled compounds to Hsp90 in its open state and ATP-dependent closed state.	Fluorescein	84-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
21637290-0	2011	SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis.	Vorinostat	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
21976548-8	2011	Unlike the sensitive controls, HEL/TGR and UKE/TGR cells were collaterally sensitive to the hsp90 inhibitors AUY922 and 17-AAG, accompanied by marked reduction in p-JAK2, p-STAT5, p-AKT, and Bcl-xL, with concomitant induction of BIM.	tanespimycin	120-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
21777196-5	2011	The naturally occurring Hsp90 inhibitor geldanamycin (GA) was the first to demonstrate anticancer activity but its significant toxicity profile in pre-clinical models precluded its clinical development.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
21777196-5	2011	The naturally occurring Hsp90 inhibitor geldanamycin (GA) was the first to demonstrate anticancer activity but its significant toxicity profile in pre-clinical models precluded its clinical development.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
22019372-7	2011	Moreover, a cell-impermeable inhibitor, 17-N,N-dimethylaminoethylamino-17-demethoxy-geldanamycin-N-oxide, also efficiently inhibited necrosis-induced cytokine production and TNF-alpha/IL-1beta-induced increase in ARPE-19 cell permeability in vitro and endotoxin-induced development of uveitis in vivo, suggesting that HSP90 can contribute to necrosis-induced RPE inflammatory responses.	17-n	40-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	318-323
20533075-0	2011	The synthetic heat shock protein 90 (Hsp90) inhibitor EC141 induces degradation of Bcr-Abl p190 protein and apoptosis of Ph-positive acute lymphoblastic leukemia cells.	ec141	54-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
20533075-0	2011	The synthetic heat shock protein 90 (Hsp90) inhibitor EC141 induces degradation of Bcr-Abl p190 protein and apoptosis of Ph-positive acute lymphoblastic leukemia cells.	ec141	54-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
20533075-9	2011	In conclusion, our data suggest that EC141 is a potent Hsp90 inhibitor with activity against Ph+ ALL.	ec141	37-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
21323861-6	2011	Functioning of the PI3K/Akt pathway was crucially dependent on functional heat-shock protein (HSP)90, and both Grp94-IgG and CTT caused and increased expression of HSP90, promoting its localization to podosomes.	CTTHWGFTLC peptide	125-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
21323861-7	2011	CTT appeared to enhance the angiogenic-like effect of Grp94-IgG by increasing the rate of secretion of both HSP90 and MMP-9.	CTTHWGFTLC peptide	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
21323861-8	2011	By preventing the chaperoning capacity of HSP90 with the inhibitor purine-scaffold (PU)-H71 that blocked the ATP-binding site on HSP90, it was possible to inhibit the expression of Akt and secretion of HSP90 and MMP-9 induced by Grp94-IgG, thus completely reversing the angiogenic pattern.	purine	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
21323861-8	2011	By preventing the chaperoning capacity of HSP90 with the inhibitor purine-scaffold (PU)-H71 that blocked the ATP-binding site on HSP90, it was possible to inhibit the expression of Akt and secretion of HSP90 and MMP-9 induced by Grp94-IgG, thus completely reversing the angiogenic pattern.	purine	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
21323861-8	2011	By preventing the chaperoning capacity of HSP90 with the inhibitor purine-scaffold (PU)-H71 that blocked the ATP-binding site on HSP90, it was possible to inhibit the expression of Akt and secretion of HSP90 and MMP-9 induced by Grp94-IgG, thus completely reversing the angiogenic pattern.	purine	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
21323861-8	2011	By preventing the chaperoning capacity of HSP90 with the inhibitor purine-scaffold (PU)-H71 that blocked the ATP-binding site on HSP90, it was possible to inhibit the expression of Akt and secretion of HSP90 and MMP-9 induced by Grp94-IgG, thus completely reversing the angiogenic pattern.	Adenosine Triphosphate	109-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
21323861-8	2011	By preventing the chaperoning capacity of HSP90 with the inhibitor purine-scaffold (PU)-H71 that blocked the ATP-binding site on HSP90, it was possible to inhibit the expression of Akt and secretion of HSP90 and MMP-9 induced by Grp94-IgG, thus completely reversing the angiogenic pattern.	Adenosine Triphosphate	109-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
21323861-8	2011	By preventing the chaperoning capacity of HSP90 with the inhibitor purine-scaffold (PU)-H71 that blocked the ATP-binding site on HSP90, it was possible to inhibit the expression of Akt and secretion of HSP90 and MMP-9 induced by Grp94-IgG, thus completely reversing the angiogenic pattern.	Adenosine Triphosphate	109-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
21369933-0	2011	A combined molecular modeling study on a series of pyrazole/isoxazole based human Hsp90alpha inhibitors.	pyrazole	51-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-92
21369933-0	2011	A combined molecular modeling study on a series of pyrazole/isoxazole based human Hsp90alpha inhibitors.	Isoxazoles	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-92
21369933-2	2011	In this work, a molecular modeling study combining pharmacophore model, molecular docking and three-dimensional quantitative structure-activity relationships (3D-QSAR) was performed to investigate a series of pyrazole/isoxazole scaffold inhibitors of human Hsp90alpha.	pyrazole	209-217	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-267
21369933-2	2011	In this work, a molecular modeling study combining pharmacophore model, molecular docking and three-dimensional quantitative structure-activity relationships (3D-QSAR) was performed to investigate a series of pyrazole/isoxazole scaffold inhibitors of human Hsp90alpha.	Isoxazoles	218-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-267
21401309-11	2011	Furthermore, pre-treatment of U937 cells with heat shock protein 90 (Hsp90) inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), prior to exposure to Nano-Ni significantly abolished Nano-Ni-induced MMP-2 and MMP-9 mRNA upregulation and increased pro-MMP-2 and pro-MMP-9 activity.	tanespimycin	87-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
21401309-11	2011	Furthermore, pre-treatment of U937 cells with heat shock protein 90 (Hsp90) inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), prior to exposure to Nano-Ni significantly abolished Nano-Ni-induced MMP-2 and MMP-9 mRNA upregulation and increased pro-MMP-2 and pro-MMP-9 activity.	tanespimycin	87-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21401309-11	2011	Furthermore, pre-treatment of U937 cells with heat shock protein 90 (Hsp90) inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), prior to exposure to Nano-Ni significantly abolished Nano-Ni-induced MMP-2 and MMP-9 mRNA upregulation and increased pro-MMP-2 and pro-MMP-9 activity.	tanespimycin	129-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-67
21401309-11	2011	Furthermore, pre-treatment of U937 cells with heat shock protein 90 (Hsp90) inhibitor, 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), prior to exposure to Nano-Ni significantly abolished Nano-Ni-induced MMP-2 and MMP-9 mRNA upregulation and increased pro-MMP-2 and pro-MMP-9 activity.	tanespimycin	129-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21787283-6	2011	Therefore, we propose that autophosphorylation of HRI is critical for catalytic regulation by Hsp90 under heme-shortage conditions.	Heme	106-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
22116673-6	2011	In particular, we found GTE inhibited molecular chaperones heat-shock protein 90 (Hsp90), its mitochondrial localized homologue Hsp75 (tumor necrosis factor receptor-associated protein 1, or Trap1) and heat-shock protein 27 (Hsp27) concomitantly.	gte	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-80
22318716-2	2012	Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.	Adenosine Triphosphate	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	211-216
22318716-2	2012	Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.	Adenosine Triphosphate	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
22318716-2	2012	Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.	Adenosine Triphosphate	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	211-216
22318716-3	2012	Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.	Adenosine Triphosphate	29-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
22318716-3	2012	Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.	Adenosine Triphosphate	188-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
22271514-7	2012	Destabilizing mutation of STAT3 at arginine residues 414/417 to alanine in the DNA-binding domain, previously shown to disrupt nuclear translocation in vivo, reduced interaction with a STAT3 DNA binding site oligonucleotide and Hsp90beta in vitro, indicating that STAT3 requires a functional DNA-binding domain for full direct interaction with Hsp90.	Arginine	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	228-233
22271514-7	2012	Destabilizing mutation of STAT3 at arginine residues 414/417 to alanine in the DNA-binding domain, previously shown to disrupt nuclear translocation in vivo, reduced interaction with a STAT3 DNA binding site oligonucleotide and Hsp90beta in vitro, indicating that STAT3 requires a functional DNA-binding domain for full direct interaction with Hsp90.	Alanine	64-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	228-233
22167270-2	2012	Here we use high resolution, quantitative mass spectrometry to map protein expression changes associated with the application of the Hsp90 inhibitor, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	150-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22167270-2	2012	Here we use high resolution, quantitative mass spectrometry to map protein expression changes associated with the application of the Hsp90 inhibitor, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	205-212	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
22181674-2	2012	AT13387 (2,4-dihydroxy-5-isopropyl-phenyl)-[5-(4-methyl-piperazin-1-ylmethyl)-1,3-dihydro-isoindol-2-yl] methanone, l-lactic acid salt) a novel, high-affinity HSP90 inhibitor, which is currently being clinically tested, has shown activity against a wide array of tumor cell lines, including lung cancer cell lines.	l-lactic acid salt)	116-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
22181674-8	2012	The use of longer-acting HSP90 inhibitors, such as AT13387, on less frequent dosing regimens has the potential to maintain antitumor efficacy as well as minimize systemic exposure and unwanted effects on normal tissues.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	51-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
22118669-4	2011	We further demonstrate that a sulfoxythiocarbamate inducer conjugates to the negative regulator of HSF1, Hsp90.	sulfoxythiocarbamate	30-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
22116673-6	2011	In particular, we found GTE inhibited molecular chaperones heat-shock protein 90 (Hsp90), its mitochondrial localized homologue Hsp75 (tumor necrosis factor receptor-associated protein 1, or Trap1) and heat-shock protein 27 (Hsp27) concomitantly.	gte	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
22116673-7	2011	Western blot analysis confirmed the inhibition of Hsp90, Hsp75 and Hsp27 by GTE, but increased phosphorylation of Ser78 of Hsp27.	gte	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
21908572-1	2011	PURPOSE: To determine the maximum tolerated dose (MTD), toxicities, and pharmacokinetic/pharmacodynamic profile of the Hsp90 inhibitor PF-04929113 (SNX-5422) in patients with advanced solid tumors and lymphomas.	SNX-5422	135-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
21925251-5	2011	Short-term NaAsO(2) treatment resulted in the down-regulation of most proteins, with heat shock 90-kDa protein (HSP90) and valosin-containing protein (VCP) being significantly downregulated.	naaso	11-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
27721334-0	2011	Photodynamic Therapy with Hypericin Improved by Targeting HSP90 Associated Proteins.	hypericin	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
21791475-1	2011	BACKGROUND: In preclinical studies the heat shock protein 90 (Hsp90) inhibitor tanespimycin induced down-regulation of checkpoint kinase 1 (Chk1) and other client proteins as well as increased sensitivity of acute leukemia cells to cytarabine.	tanespimycin	79-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-60
21791475-1	2011	BACKGROUND: In preclinical studies the heat shock protein 90 (Hsp90) inhibitor tanespimycin induced down-regulation of checkpoint kinase 1 (Chk1) and other client proteins as well as increased sensitivity of acute leukemia cells to cytarabine.	tanespimycin	79-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
21791475-1	2011	BACKGROUND: In preclinical studies the heat shock protein 90 (Hsp90) inhibitor tanespimycin induced down-regulation of checkpoint kinase 1 (Chk1) and other client proteins as well as increased sensitivity of acute leukemia cells to cytarabine.	Cytarabine	232-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-60
21791475-1	2011	BACKGROUND: In preclinical studies the heat shock protein 90 (Hsp90) inhibitor tanespimycin induced down-regulation of checkpoint kinase 1 (Chk1) and other client proteins as well as increased sensitivity of acute leukemia cells to cytarabine.	Cytarabine	232-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
21821695-7	2011	HSP90 requires ATP to stabilize client proteins; hence, expression of signal transducer and activator of transcription 3 (STAT3), Raf-1, and Akt was analyzed.	Adenosine Triphosphate	15-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
22039910-4	2011	Herein, the development of a C-terminal Hsp90 inhibitor, KU174, is described, which demonstrates anti-cancer activity in prostate cancer cells in the absence of a HSR and describe a novel approach to characterize Hsp90 inhibition in cancer cells.	ku174	57-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
21821695-2	2011	The chaperone function of HSP90 is blocked by 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), although it results in transcription and translation of antiapoptotic HSP proteins.	tanespimycin	46-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21821695-2	2011	The chaperone function of HSP90 is blocked by 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), although it results in transcription and translation of antiapoptotic HSP proteins.	tanespimycin	88-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
22039910-4	2011	Herein, the development of a C-terminal Hsp90 inhibitor, KU174, is described, which demonstrates anti-cancer activity in prostate cancer cells in the absence of a HSR and describe a novel approach to characterize Hsp90 inhibition in cancer cells.	ku174	57-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	213-218
22039910-7	2011	RESULTS: KU174 exhibits robust anti-proliferative and cytotoxic activity along with client protein degradation and disruption of Hsp90 native complexes without induction of a HSR.	ku174	9-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
22039910-8	2011	Furthermore, KU174 demonstrates direct binding to the Hsp90 protein and Hsp90 complexes in cancer cells.	ku174	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
22039910-8	2011	Furthermore, KU174 demonstrates direct binding to the Hsp90 protein and Hsp90 complexes in cancer cells.	ku174	13-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
21846483-6	2011	To inhibit HSP90, we have chosen geldanamycin (GA), a potent HSP90 inhibitor.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
21846483-6	2011	To inhibit HSP90, we have chosen geldanamycin (GA), a potent HSP90 inhibitor.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
21846483-6	2011	To inhibit HSP90, we have chosen geldanamycin (GA), a potent HSP90 inhibitor.	geldanamycin	47-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
21846483-6	2011	To inhibit HSP90, we have chosen geldanamycin (GA), a potent HSP90 inhibitor.	geldanamycin	47-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
21875802-3	2011	With the aim of efficiently identifying a new class of orally available inhibitors of the ATP binding site of this protein, we conducted fragment screening and virtual screening in parallel against Hsp90.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
21972823-0	2011	Tricyclic series of heat shock protein 90 (Hsp90) inhibitors part I: discovery of tricyclic imidazo[4,5-c]pyridines as potent inhibitors of the Hsp90 molecular chaperone.	tricyclic imidazo[4,5-c]pyridines	82-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-41
21972823-0	2011	Tricyclic series of heat shock protein 90 (Hsp90) inhibitors part I: discovery of tricyclic imidazo[4,5-c]pyridines as potent inhibitors of the Hsp90 molecular chaperone.	tricyclic imidazo[4,5-c]pyridines	82-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
21972823-0	2011	Tricyclic series of heat shock protein 90 (Hsp90) inhibitors part I: discovery of tricyclic imidazo[4,5-c]pyridines as potent inhibitors of the Hsp90 molecular chaperone.	tricyclic imidazo[4,5-c]pyridines	82-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
21972823-5	2011	These optimized molecules make productive interactions within the ATP binding site as reported by other Hsp90 inhibitors.	Adenosine Triphosphate	66-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
21866939-2	2011	These studies have led to (1) validation of alkyne-alkyne coupling to produce geldanamycin analogs that lack the problematic quinone, (2) the discovery that C6-C7 bis-carbamate functionality is compatible with Hsp90 inhibition, and (3) the identification of 1 as a nonquinone geldanamycin-inspired paralog-selective Hsp90 inhibitor.	bis-carbamate	163-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	210-215
21866939-2	2011	These studies have led to (1) validation of alkyne-alkyne coupling to produce geldanamycin analogs that lack the problematic quinone, (2) the discovery that C6-C7 bis-carbamate functionality is compatible with Hsp90 inhibition, and (3) the identification of 1 as a nonquinone geldanamycin-inspired paralog-selective Hsp90 inhibitor.	bis-carbamate	163-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	316-321
21812426-0	2011	Blockade of Her2/neu binding to Hsp90 by emodin azide methyl anthraquinone derivative induces proteasomal degradation of Her2/neu.	Azides	48-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
21812426-0	2011	Blockade of Her2/neu binding to Hsp90 by emodin azide methyl anthraquinone derivative induces proteasomal degradation of Her2/neu.	methyl anthraquinone	54-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
21812426-6	2011	Molecular docking studies predicted that AMAD can interact with the ATP-binding pocket of both Hsp90 and Her2/neu.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
21875802-4	2011	This approach quickly identified 2-aminotriazine and 2-aminopyrimidine derivatives as specific ligands to Hsp90 with high ligand efficiency.	2-aminotriazine	33-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
21875802-4	2011	This approach quickly identified 2-aminotriazine and 2-aminopyrimidine derivatives as specific ligands to Hsp90 with high ligand efficiency.	2-aminopyrimidine	53-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
21825009-0	2011	The heat shock protein 90 inhibitor IPI-504 induces KIT degradation, tumor shrinkage, and cell proliferation arrest in xenograft models of gastrointestinal stromal tumors.	tanespimycin	36-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
21190426-0	2011	Some sulfonamide drugs inhibit ATPase activity of heat shock protein 90: investigation by docking simulation and experimental validation.	Sulfonamides	5-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-71
21190426-1	2011	Eight selected sulfonamide drugs were investigated as inhibitors of heat shock protein 90 (Hsp90).	Sulfonamides	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
21190426-1	2011	Eight selected sulfonamide drugs were investigated as inhibitors of heat shock protein 90 (Hsp90).	Sulfonamides	15-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
21190426-3	2011	The selected molecules were found to readily fit within the ATP-binding pocket of Hsp90 in low-energy poses.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
21190426-4	2011	The sulfonamides torsemide, sulfathiazole, and sulfadiazine were found to inhibit the ATPase activity of Hsp90 with IC(50) values of 1.0, 2.6, and 1.5 muM, respectively.	Sulfonamides	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
21190426-4	2011	The sulfonamides torsemide, sulfathiazole, and sulfadiazine were found to inhibit the ATPase activity of Hsp90 with IC(50) values of 1.0, 2.6, and 1.5 muM, respectively.	Torsemide	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
21190426-4	2011	The sulfonamides torsemide, sulfathiazole, and sulfadiazine were found to inhibit the ATPase activity of Hsp90 with IC(50) values of 1.0, 2.6, and 1.5 muM, respectively.	Sulfathiazole	28-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
21190426-4	2011	The sulfonamides torsemide, sulfathiazole, and sulfadiazine were found to inhibit the ATPase activity of Hsp90 with IC(50) values of 1.0, 2.6, and 1.5 muM, respectively.	Sulfadiazine	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
21190426-5	2011	Our results suggest that these well-established sulfonamides can be good leads for subsequent optimization into potent Hsp90 inhibitors.	Sulfonamides	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
21825009-3	2011	The observation that heat shock protein 90 (HSP90) inhibition results in KIT degradation prompted us to assess the efficacy of the HSP90 inhibitor retaspimycin hydrochloride (IPI-504) alone or in combination with imatinib or sunitinib in two GIST xenografts with distinctive KIT mutations.	tanespimycin	147-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
22335904-12	2011	The expression of HSP90 exposed to quercetin for 48 h was decreased to 49.3% of the normal HepG2 cells, and the expression of HSP70 was decreased to 43.6% of the normal Hep G2 cells.	Quercetin	35-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
21946277-2	2011	We show that the inhibitor PU-H71 preferentially targets tumor-enriched Hsp90 complexes and affinity captures Hsp90-dependent oncogenic client proteins.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
21946277-2	2011	We show that the inhibitor PU-H71 preferentially targets tumor-enriched Hsp90 complexes and affinity captures Hsp90-dependent oncogenic client proteins.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
21620825-0	2011	BJ-B11, a novel Hsp90 inhibitor, induces apoptosis in human chronic myeloid leukemia K562 cells through the mitochondria-dependent pathway.	2-(4-acetyloxycyclohexylamino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indazol-1-yl)-benzamide	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
21620825-2	2011	We investigated, for the first time, the antitumor activity of a novel Hsp90 inhibitor 2-(4-acetyloxycyclohexylamino)-4-(3, 6, 6-trimethyl-4-oxo-4, 5, 6, 7-tetrahydro-1H-indazol-1-yl)-benzamide (BJ-B11) and the molecular mechanism underlying the apoptosis it induces in human chronic myeloid leukemia K562 cells.	2-(4-acetyloxycyclohexylamino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indazol-1-yl)-benzamide	195-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
21519787-5	2011	Exogenous administration of NaHS (a donor of H2S) augmented not only HSP90 expression under normal conditions, but also CoCl2-induced overexpression of HSP90.	sodium bisulfide	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21519787-5	2011	Exogenous administration of NaHS (a donor of H2S) augmented not only HSP90 expression under normal conditions, but also CoCl2-induced overexpression of HSP90.	sodium bisulfide	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
21519787-5	2011	Exogenous administration of NaHS (a donor of H2S) augmented not only HSP90 expression under normal conditions, but also CoCl2-induced overexpression of HSP90.	Hydrogen Sulfide	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21519787-5	2011	Exogenous administration of NaHS (a donor of H2S) augmented not only HSP90 expression under normal conditions, but also CoCl2-induced overexpression of HSP90.	Hydrogen Sulfide	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
21519787-5	2011	Exogenous administration of NaHS (a donor of H2S) augmented not only HSP90 expression under normal conditions, but also CoCl2-induced overexpression of HSP90.	cobaltous chloride	120-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
21632108-3	2011	Inhibition of Hsp90 by 17-allylamino-17-demethoxygeldanamycin (17-AAG) disrupted downstream signaling pathways of mutant KIT in Kasumi-1 cells.	tanespimycin	23-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21632108-3	2011	Inhibition of Hsp90 by 17-allylamino-17-demethoxygeldanamycin (17-AAG) disrupted downstream signaling pathways of mutant KIT in Kasumi-1 cells.	tanespimycin	63-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21663398-3	2011	17-DMAG, a heat-shock protein 90 (Hsp90) inhibitor, protects human T cells from ionizing radiation-induced apoptosis by inhibiting inducible nitric oxide synthase (iNOS) and subsequent caspase-3 activation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-32
21663398-3	2011	17-DMAG, a heat-shock protein 90 (Hsp90) inhibitor, protects human T cells from ionizing radiation-induced apoptosis by inhibiting inducible nitric oxide synthase (iNOS) and subsequent caspase-3 activation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
21663398-7	2011	Analysis of p53-Hsp90 interaction in ex vivo cell lysates indicated that the binding between the two molecules occurred after irradiation but 17-DMAG prevented the binding.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	142-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
21663398-9	2011	Hsp90 inhibitors such as 17-DMAG may prove useful with radiation-based cancer therapy as well as for general radioprotection.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	25-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21623862-2	2011	The aim of this study was to investigate the effects of DA-6034 on the interactions between IkappaB kinase (IKK) and heat shock protein 90 (Hsp90), and activation of the nuclear factor-kappaB (NF-kappaB) signalling pathway in human gastric epithelial cells infected with Helicobacter pylori.	recoflavone	56-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-138
21623862-2	2011	The aim of this study was to investigate the effects of DA-6034 on the interactions between IkappaB kinase (IKK) and heat shock protein 90 (Hsp90), and activation of the nuclear factor-kappaB (NF-kappaB) signalling pathway in human gastric epithelial cells infected with Helicobacter pylori.	recoflavone	56-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
21623862-7	2011	Treatment with DA-6034 dissociated the Hsp90 and IKK-gamma complex in H. pylori-infected cells, leading to the inhibition of IL-8 expression.	recoflavone	15-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
21623862-8	2011	These results suggest that the eupatilin derivative 7-carboxymethyloxy-3",4",5-trimethoxy flavone has anti-inflammatory activity in gastric epithelial cells infected with H. pylori through the promotion of the dissociation of the IKK-gamma-Hsp90 complex and suppression of NF-kappaB signalling.	eupatilin	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
21623862-8	2011	These results suggest that the eupatilin derivative 7-carboxymethyloxy-3",4",5-trimethoxy flavone has anti-inflammatory activity in gastric epithelial cells infected with H. pylori through the promotion of the dissociation of the IKK-gamma-Hsp90 complex and suppression of NF-kappaB signalling.	recoflavone	52-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
27721325-1	2011	Cross-linked nanoassemblies (CNAs) with a degradable core were prepared for sustained release of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), a potent inhibitor of heat shock protein 90 (HSP90).	tanespimycin	97-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-191
27721325-1	2011	Cross-linked nanoassemblies (CNAs) with a degradable core were prepared for sustained release of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), a potent inhibitor of heat shock protein 90 (HSP90).	tanespimycin	97-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
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
21968922-15	2011	The salt-stripped GR is then incubated with reticulocyte lysate, ATP, and K(+), which results in the reconstitution of the GR hsp90 heterocomplex and reactivation of steroid binding activity (7).	Salts	4-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
21968922-15	2011	The salt-stripped GR is then incubated with reticulocyte lysate, ATP, and K(+), which results in the reconstitution of the GR hsp90 heterocomplex and reactivation of steroid binding activity (7).	Adenosine Triphosphate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
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
21802945-0	2011	Synthesis of purine-scaffold fluorescent probes for heat shock protein 90 with use in flow cytometry and fluorescence microscopy.	purine	13-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-73
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Fluorescein-5-isothiocyanate	93-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Fluorescein-5-isothiocyanate	93-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Fluorescein-5-isothiocyanate	121-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Fluorescein-5-isothiocyanate	121-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	4-nitrobenzofurazan	128-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	4-nitrobenzofurazan	128-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	nbd	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	nbd	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	sulforhodamine 101	187-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	sulforhodamine 101	187-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Texas red	207-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Texas red	207-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Plutonium	232-234	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
21802945-1	2011	Fluorescent ligands for the heat shock protein 90 (Hsp90) were synthesized containing either fluorescein isothiocyanate (FITC), 4-nitrobenzo[1,2,5]oxadiazole (NBD) or the red shifted dye sulforhodamine 101 (Texas Red) conjugated to PU-H71.	Plutonium	232-234	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21768087-4	2011	The Hsp90 inhibitor 17-allylaminodemethoxygeldanamycin (17-AAG) preferentially induced the polyubiquitination and proteasomal degradation of Flt3-ITD autophosphorylated on Tyr-591 in these cells.	17-allylaminodemethoxygeldanamycin	20-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21768087-4	2011	The Hsp90 inhibitor 17-allylaminodemethoxygeldanamycin (17-AAG) preferentially induced the polyubiquitination and proteasomal degradation of Flt3-ITD autophosphorylated on Tyr-591 in these cells.	tanespimycin	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21768087-4	2011	The Hsp90 inhibitor 17-allylaminodemethoxygeldanamycin (17-AAG) preferentially induced the polyubiquitination and proteasomal degradation of Flt3-ITD autophosphorylated on Tyr-591 in these cells.	Tyrosine	172-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21737488-0	2011	Clusterin inhibition using OGX-011 synergistically enhances Hsp90 inhibitor activity by suppressing the heat shock response in castrate-resistant prostate cancer.	OGX-011	27-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
21737488-4	2011	To test this hypothesis, we treated CRPC with the Hsp90 inhibitor PF-04929113 or 17-AAG in the absence or presence of OGX-011, an antisense drug that targets CLU.	SNX-5422	66-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
21737488-6	2011	Treatment-induced increases in CLU were blocked by OGX-011, which synergistically enhanced the activity of Hsp90 inhibition on CRPC cell growth and apoptosis.	OGX-011	51-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
21737488-8	2011	In vivo evaluation of the Hsp90 inhibitors with OGX-011 in xenograft models of human CRPC showed that OGX-011 markedly potentiated antitumor efficacy, leading to an 80% inhibition of tumor growth with prolonged survival compared with Hsp90 inhibitor monotherapy.	OGX-011	48-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21737488-8	2011	In vivo evaluation of the Hsp90 inhibitors with OGX-011 in xenograft models of human CRPC showed that OGX-011 markedly potentiated antitumor efficacy, leading to an 80% inhibition of tumor growth with prolonged survival compared with Hsp90 inhibitor monotherapy.	OGX-011	102-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21737488-9	2011	Together, our findings indicate that Hsp90 inhibitor-induced activation of the heat shock response and CLU is attenuated by OGX-011, with synergistic effects on delaying CRPC progression.	OGX-011	124-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
21737488-9	2011	Together, our findings indicate that Hsp90 inhibitor-induced activation of the heat shock response and CLU is attenuated by OGX-011, with synergistic effects on delaying CRPC progression.	crpc	170-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
21737509-0	2011	The Novel HSP90 inhibitor, IPI-493, is highly effective in human gastrostrointestinal stromal tumor xenografts carrying heterogeneous KIT mutations.	tanespimycin	27-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
21737509-3	2011	We evaluated the efficacy of the novel HSP90 inhibitor IPI-493 alone, or in combination with IMA or SUN in GIST xenografts with KIT mutations.	tanespimycin	55-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
21737509-10	2011	CONCLUSIONS: When administered as a single agent in a xenograft model, the HSP90 inhibitor IPI-493 has consistent antitumor activity and induces KIT downregulation in GISTs with heterogeneous KIT mutations.	tanespimycin	91-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
21871133-8	2011	In addition, apigenin had a greater effects in depleting Hsp90 clients when used in combination with the Hsp90 inhibitor geldanamycin and the histone deacetylase inhibitor vorinostat.	Apigenin	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
21871133-8	2011	In addition, apigenin had a greater effects in depleting Hsp90 clients when used in combination with the Hsp90 inhibitor geldanamycin and the histone deacetylase inhibitor vorinostat.	Apigenin	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
21871133-8	2011	In addition, apigenin had a greater effects in depleting Hsp90 clients when used in combination with the Hsp90 inhibitor geldanamycin and the histone deacetylase inhibitor vorinostat.	geldanamycin	121-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
21755987-2	2011	Novobiocin, a typically C-terminal inhibitor for Hsp90, will probably used as an important anticancer drug in the future.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
21764310-0	2011	Synthesis and evaluation of biotinylated sansalvamide A analogs and their modulation of Hsp90.	sansalvamide A	41-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
21749116-0	2011	Protein-selective capture to analyze electrophile adduction of hsp90 by 4-hydroxynonenal.	4-hydroxy-2-nonenal	72-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
21764310-2	2011	The tagged derivatives indicated in protein pull-down assays that they bind to Hsp90 at the same binding site (N-Middle domain) as the San A-amide peptide.	Amides	141-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
21558407-0	2011	HSP90 inhibition is effective in breast cancer: a phase II trial of tanespimycin (17-AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab.	tanespimycin	68-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21558407-2	2011	17-Demethoxygeldanamycin (17-AAG) is a natural product that binds to HSP90 and inhibits its activity, thereby inducing the degradation of these clients.	17-demethoxygeldanamycin	0-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21519806-1	2011	PURPOSE: We studied whether HSP90alpha was associated with the special carbohydrate structures IMH-2 epitopes, and investigated its mRNA expression and clinical relevance in colorectal cancer (CRC) patients.	Carbohydrates	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-38
21749116-5	2011	Geldanamycin-biotin capture afforded higher purity Hsp90 than did immunoprecipitation and enabled detection of endogenously phosphorylated protein by liquid chromatography-tandem mass spectrometry (LC-MS/MS).	Geldanamycin-Biotin	0-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21749116-6	2011	We applied this approach to map and quantify adducts formed on Hsp90 by 4-hydroxynonenal (HNE) in RKO cells.	4-hydroxy-2-nonenal	72-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
21749116-6	2011	We applied this approach to map and quantify adducts formed on Hsp90 by 4-hydroxynonenal (HNE) in RKO cells.	4-hydroxy-2-nonenal	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
21749116-7	2011	LC-MS/MS analyses of tryptic digests by identified His(450) and His(490) of Hsp90alpha as having a 158 Da modification, corresponding to NaBH(4)-reduced HNE adducts.	Histidine	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-86
21749116-7	2011	LC-MS/MS analyses of tryptic digests by identified His(450) and His(490) of Hsp90alpha as having a 158 Da modification, corresponding to NaBH(4)-reduced HNE adducts.	Histidine	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-86
21749116-7	2011	LC-MS/MS analyses of tryptic digests by identified His(450) and His(490) of Hsp90alpha as having a 158 Da modification, corresponding to NaBH(4)-reduced HNE adducts.	sodium borohydride	137-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-86
21749116-11	2011	Within the middle client-binding domain of Hsp90alpha, residue His(450) demonstrated the most rapid adduction with k(obs) of 1.08 +- 0.17 h(-1) in HNE-treated cells.	Histidine	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-53
21520056-8	2011	The application of HSP90 activity inhibitor geldanamycin (GA) and radicicol (RD) potentiates the telomerase inhibition and apoptosis induction of Abeta in CECs.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
21520056-8	2011	The application of HSP90 activity inhibitor geldanamycin (GA) and radicicol (RD) potentiates the telomerase inhibition and apoptosis induction of Abeta in CECs.	geldanamycin	58-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
21520056-9	2011	An increase in protein ubiquitination by Abeta(25-35), but not Abeta(35-25), treatment was examined, and Abeta-inhibited HSP90 and TERT protein expression and telomerase activity was reversed by adding proteasome inhibitor, MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	224-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
21670086-2	2011	The HSP90 inhibitor tanespimycin in combination with trastuzumab is active in patients with HER2-overexpressing metastatic breast cancer.	tanespimycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21519806-8	2011	HCT-8 cell migration induced by serum starvation-conditioned medium was blocked by anti-HSP90alpha antibody or the HSP90alpha inhibitor geldanamycin (GA) as efficient as by IMH-2 antibody, suggesting that IMH-2-associated HSP90alpha was involved in serum starvation-induced CRC cell migration.	geldanamycin	136-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-125
21519806-8	2011	HCT-8 cell migration induced by serum starvation-conditioned medium was blocked by anti-HSP90alpha antibody or the HSP90alpha inhibitor geldanamycin (GA) as efficient as by IMH-2 antibody, suggesting that IMH-2-associated HSP90alpha was involved in serum starvation-induced CRC cell migration.	geldanamycin	136-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-125
21519806-8	2011	HCT-8 cell migration induced by serum starvation-conditioned medium was blocked by anti-HSP90alpha antibody or the HSP90alpha inhibitor geldanamycin (GA) as efficient as by IMH-2 antibody, suggesting that IMH-2-associated HSP90alpha was involved in serum starvation-induced CRC cell migration.	geldanamycin	150-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-125
21519806-8	2011	HCT-8 cell migration induced by serum starvation-conditioned medium was blocked by anti-HSP90alpha antibody or the HSP90alpha inhibitor geldanamycin (GA) as efficient as by IMH-2 antibody, suggesting that IMH-2-associated HSP90alpha was involved in serum starvation-induced CRC cell migration.	geldanamycin	150-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-125
21523562-1	2011	The Hsp90-associated cis-trans peptidyl-prolyl isomerase--FK506 binding protein 51 (FKBP51)--was recently found to co-localize with the microtubule (MT)-associated protein tau in neurons and physically interact with tau in brain tissues from humans who died from Alzheimer"s disease (AD).	Tacrolimus	58-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
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
21602432-5	2011	We found that only anthracyclines induced a rapid translocation of calreticulin, HSP70, and HSP90 to the cell surface and the release of HMGB1 12 hours after the treatment.	Anthracyclines	19-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
21627535-5	2011	It was demonstrated, using a range of primary and transformed mesothelial and mesothelioma cell lines, that cells assembled high molecular weight kininogen and plasma prekallikrein to liberate bradykinin, a process inhibited by novobiocin, a heat shock protein 90 (HSP90) inhibitor, cysteine, bradykinin and protamine sulphate.	Novobiocin	228-238	heat shock protein 90 alpha family class A member 1	Homo sapiens	242-263
21627535-5	2011	It was demonstrated, using a range of primary and transformed mesothelial and mesothelioma cell lines, that cells assembled high molecular weight kininogen and plasma prekallikrein to liberate bradykinin, a process inhibited by novobiocin, a heat shock protein 90 (HSP90) inhibitor, cysteine, bradykinin and protamine sulphate.	Novobiocin	228-238	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
21566061-3	2011	We show that hsp90 inhibition with 17-allylamino-demehoxygeldanamycin or the novel, nongeldanamycin analogue AUY922 (resorcinylic isoxazole amide; Novartis Pharma) dose-dependently reduced the levels of ATR and CHK1 without affecting ATM levels.	17-allylamino-demehoxygeldanamycin	35-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
21382639-4	2011	VPA plus imatinib significantly increased acetylation of HSP90 and hnRNP L and decreased phosphorylation of HSPs and hnRNPs in imatinib resistant cells.	Valproic Acid	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
21382639-4	2011	VPA plus imatinib significantly increased acetylation of HSP90 and hnRNP L and decreased phosphorylation of HSPs and hnRNPs in imatinib resistant cells.	Imatinib Mesylate	9-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
21566061-3	2011	We show that hsp90 inhibition with 17-allylamino-demehoxygeldanamycin or the novel, nongeldanamycin analogue AUY922 (resorcinylic isoxazole amide; Novartis Pharma) dose-dependently reduced the levels of ATR and CHK1 without affecting ATM levels.	resorcinylic isoxazole amide	117-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
21566061-4	2011	AUY922-mediated depletion of ATR and CHK1 was associated with an increase in their polyubiquitylation and decreased binding to hsp90.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
21553822-1	2011	Development of the DNA gyrase inhibitor, novobiocin, into a selective Hsp90 inhibitor was accomplished through structural modifications to the amide side chain, coumarin ring, and sugar moiety.	Novobiocin	41-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21530541-8	2011	All proteins share the same core CS domain characteristic of proteins acting either as cochaperones of Hsp90 or as independent small heat shock proteins.	Cesium	33-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
21700222-2	2011	The ATP-dependent chaperone cycle involves significant conformational rearrangements of the Hsp90 dimer and interaction with a network of cochaperone proteins.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
21700222-5	2011	Hop stabilizes an alternate Hsp90 open state, where hydrophobic client-binding surfaces have converged and the N-terminal domains have rotated and match the closed, ATP conformation.	Adenosine Triphosphate	165-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
21700222-6	2011	Hsp90 is thus simultaneously poised for client loading by Hsp70 and subsequent N-terminal dimerization and ATP hydrolysis.	Adenosine Triphosphate	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21553822-1	2011	Development of the DNA gyrase inhibitor, novobiocin, into a selective Hsp90 inhibitor was accomplished through structural modifications to the amide side chain, coumarin ring, and sugar moiety.	Amides	143-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21553822-1	2011	Development of the DNA gyrase inhibitor, novobiocin, into a selective Hsp90 inhibitor was accomplished through structural modifications to the amide side chain, coumarin ring, and sugar moiety.	coumarin	161-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21553822-1	2011	Development of the DNA gyrase inhibitor, novobiocin, into a selective Hsp90 inhibitor was accomplished through structural modifications to the amide side chain, coumarin ring, and sugar moiety.	Sugars	180-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21553822-3	2011	Utilization of structure-activity relationships established for three novobiocin synthons produced optimized scaffolds, which manifest midnanomolar activity against a panel of cancer cell lines and serve as lead compounds that manifest their activities through Hsp90 inhibition.	Novobiocin	70-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	261-266
21487019-5	2011	Inhibition of Hsp90 function using the geldanamycin analog 17-AAG induces the ubiquitination and degradation of FGFR3 and reduces the signaling capacity of FGFR3.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21487019-5	2011	Inhibition of Hsp90 function using the geldanamycin analog 17-AAG induces the ubiquitination and degradation of FGFR3 and reduces the signaling capacity of FGFR3.	tanespimycin	59-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21489987-3	2011	In pCD-NSP3-transfected cells, treatment with Hsp90 inhibitor (17-N,N-dimethylethylenediamine-geldanamycin (17DMAG)) resulted in the proteasomal degradation of NSP3.	17-n,n-dimethylethylenediamine-geldanamycin	63-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
21489987-3	2011	In pCD-NSP3-transfected cells, treatment with Hsp90 inhibitor (17-N,N-dimethylethylenediamine-geldanamycin (17DMAG)) resulted in the proteasomal degradation of NSP3.	17DMAG	108-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
21489987-8	2011	In addition, inhibition of Hsp90 by 17DMAG resulted in reduced nuclear translocation of poly(A)-binding protein and translation of viral proteins.	17DMAG	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21489987-8	2011	In addition, inhibition of Hsp90 by 17DMAG resulted in reduced nuclear translocation of poly(A)-binding protein and translation of viral proteins.	Poly A	88-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21737627-2	2011	Therefore, this study investigated HSP90 client proteins sensitive to the HSP90 inhibitor geldanamycin in tumour and healthy breast tissue.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
21258415-0	2011	The Hsp90 inhibitor IPI-504 rapidly lowers EML4-ALK levels and induces tumor regression in ALK-driven NSCLC models.	tanespimycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21194376-0	2011	Hsp90 regulates NADPH oxidase activity and is necessary for superoxide but not hydrogen peroxide production.	Superoxides	60-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21194376-0	2011	Hsp90 regulates NADPH oxidase activity and is necessary for superoxide but not hydrogen peroxide production.	Hydrogen Peroxide	79-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21194376-1	2011	The goal of this study was to identify whether heat-shock protein 90 (Hsp90) regulates the production of superoxide and other reactive oxygen species from the NADPH oxidases (Nox).	Superoxides	105-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-68
21194376-1	2011	The goal of this study was to identify whether heat-shock protein 90 (Hsp90) regulates the production of superoxide and other reactive oxygen species from the NADPH oxidases (Nox).	Superoxides	105-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21194376-1	2011	The goal of this study was to identify whether heat-shock protein 90 (Hsp90) regulates the production of superoxide and other reactive oxygen species from the NADPH oxidases (Nox).	Reactive Oxygen Species	126-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-68
21194376-1	2011	The goal of this study was to identify whether heat-shock protein 90 (Hsp90) regulates the production of superoxide and other reactive oxygen species from the NADPH oxidases (Nox).	Reactive Oxygen Species	126-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21194376-2	2011	We found that pharmacological and genetic inhibition of Hsp90 directly reduced Nox5-derived superoxide without secondarily modifying signaling events.	Superoxides	92-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
21194376-5	2011	Inhibitors of Hsp90 also reduced superoxide from Nox1, Nox2 (neutrophils), and Nox3.	Superoxides	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21737627-2	2011	Therefore, this study investigated HSP90 client proteins sensitive to the HSP90 inhibitor geldanamycin in tumour and healthy breast tissue.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
21737627-6	2011	Further experiments inferred HSP40, -56/FKBP52, -60, -70, -105 and lumican to associate with HSP90 and to belong to this group of geldanamycin-sensitive proteins.	geldanamycin	130-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
21194376-9	2011	We conclude that Hsp90 binds to the C-terminus of Noxes1-3 and 5 and is necessary for enzyme stability and superoxide production.	Superoxides	107-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
21737627-10	2011	Geldanamycin resistance and lack of HSP90 client protein expression may limit clinical applications of HSP90 inhibitors.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
21515049-1	2011	A novel series of macrocyclic ortho-aminobenzamide Hsp90 inhibitors is reported.	anthranilamide	30-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21357526-0	2011	Hsp90 interacts with inducible NO synthase client protein in its heme-free state and then drives heme insertion by an ATP-dependent process.	Heme	65-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21534941-1	2011	This open-label, dose escalation, multicentre phase 1/2 trial was undertaken to determine the safety and tolerability of the heat shock protein 90 (HSP90) inhibitor tanespimycin (100-340 mg/m(2) )+ bortezomib (0 7-1 3 mg/m(2) ) given on days 1, 4, 8 and 11 in each 21-d cycle.	tanespimycin	165-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
21534941-7	2011	Pharmacodynamic analyses indicated that tanespimycin plus bortezomib effectively inhibited the proteasome, as evidenced by decreased 20S proteasome activity, and inhibited HSP90, as reflected by increased HSP70 expression.	tanespimycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
21534941-7	2011	Pharmacodynamic analyses indicated that tanespimycin plus bortezomib effectively inhibited the proteasome, as evidenced by decreased 20S proteasome activity, and inhibited HSP90, as reflected by increased HSP70 expression.	Bortezomib	58-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
21357526-0	2011	Hsp90 interacts with inducible NO synthase client protein in its heme-free state and then drives heme insertion by an ATP-dependent process.	Heme	97-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21357526-0	2011	Hsp90 interacts with inducible NO synthase client protein in its heme-free state and then drives heme insertion by an ATP-dependent process.	Adenosine Triphosphate	118-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21357526-4	2011	Pulldown experiments showed that the hsp90-iNOS complex was present in cells, but the extent of their association was inversely related to iNOS heme content.	Heme	144-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
21357526-5	2011	Hsp90 was primarily associated with apo-iNOS monomer and was associated 11-fold less with heme-containing iNOS monomer or dimer in cells.	Heme	90-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21357526-6	2011	Kinetic studies showed that hsp90 dissociation occurred coincident with cellular heme insertion into apo-iNOS (0.8 h(-1)).	Heme	81-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
21357526-7	2011	The hsp90 inhibitor radicicol or coexpression of an ATPase-defective hsp90 blocked heme insertion into apo-iNOS by 90 and 75%, respectively.	monorden	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21357526-7	2011	The hsp90 inhibitor radicicol or coexpression of an ATPase-defective hsp90 blocked heme insertion into apo-iNOS by 90 and 75%, respectively.	Heme	83-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21357526-7	2011	The hsp90 inhibitor radicicol or coexpression of an ATPase-defective hsp90 blocked heme insertion into apo-iNOS by 90 and 75%, respectively.	Heme	83-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21357526-8	2011	The ATPase activity of hsp90 was not required for complex formation with iNOS but was essential for heme insertion to occur.	Heme	100-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
21357526-9	2011	We conclude that hsp90 plays a primary role in maturation of iNOS protein by interacting with the apoenzyme in cells and then driving heme insertion in an ATP-dependent manner.	Heme	134-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
21357526-9	2011	We conclude that hsp90 plays a primary role in maturation of iNOS protein by interacting with the apoenzyme in cells and then driving heme insertion in an ATP-dependent manner.	Adenosine Triphosphate	155-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
21051589-9	2011	Results of reporter assays, immunoblot assays, and ELISA revealed that the heat shock protein 90 (Hsp90) inhibitors 17-allyamino-17-demethoxygeldanamycin and geldanamycin blocked IL-6-induced PSA gene expression.	17-allyamino-17-demethoxygeldanamycin	116-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
21511880-9	2011	Pharmacological interference of heat shock protein 90 (HSP90) with geldanamycin during the intranuclear chaperone cycle completely ablated GR"s cyclical activity, cyclical cAMP response element-binding protein (CREB) binding protein (CBP)/p300 recruitment, and the associated cyclical acetylation at the promoter region.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
21051589-9	2011	Results of reporter assays, immunoblot assays, and ELISA revealed that the heat shock protein 90 (Hsp90) inhibitors 17-allyamino-17-demethoxygeldanamycin and geldanamycin blocked IL-6-induced PSA gene expression.	17-allyamino-17-demethoxygeldanamycin	116-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
21051589-9	2011	Results of reporter assays, immunoblot assays, and ELISA revealed that the heat shock protein 90 (Hsp90) inhibitors 17-allyamino-17-demethoxygeldanamycin and geldanamycin blocked IL-6-induced PSA gene expression.	geldanamycin	141-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
21051589-9	2011	Results of reporter assays, immunoblot assays, and ELISA revealed that the heat shock protein 90 (Hsp90) inhibitors 17-allyamino-17-demethoxygeldanamycin and geldanamycin blocked IL-6-induced PSA gene expression.	geldanamycin	141-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
21511880-9	2011	Pharmacological interference of heat shock protein 90 (HSP90) with geldanamycin during the intranuclear chaperone cycle completely ablated GR"s cyclical activity, cyclical cAMP response element-binding protein (CREB) binding protein (CBP)/p300 recruitment, and the associated cyclical acetylation at the promoter region.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
21511880-9	2011	Pharmacological interference of heat shock protein 90 (HSP90) with geldanamycin during the intranuclear chaperone cycle completely ablated GR"s cyclical activity, cyclical cAMP response element-binding protein (CREB) binding protein (CBP)/p300 recruitment, and the associated cyclical acetylation at the promoter region.	Cyclic AMP	172-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-53
21511880-9	2011	Pharmacological interference of heat shock protein 90 (HSP90) with geldanamycin during the intranuclear chaperone cycle completely ablated GR"s cyclical activity, cyclical cAMP response element-binding protein (CREB) binding protein (CBP)/p300 recruitment, and the associated cyclical acetylation at the promoter region.	Cyclic AMP	172-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
21383049-0	2011	Antitumor activity of the Hsp90 inhibitor IPI-504 in HER2-positive trastuzumab-resistant breast cancer.	tanespimycin	42-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21645448-0	2011	[The correlation between the up-regulation of Hsp90 and drug resistance to cisplatin in lung cancer cell line].	Cisplatin	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
21645448-2	2011	The aim of this study is to investigate the relationship between the GGA-induced overexpression of Hsp90 and chemoresistance to Cisplatin in SPCA-1 and H446 cell line.	Cisplatin	128-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
21645448-5	2011	The effect of Hsp90 expression on the drug resistance to Cisplatin in two Cell Lines was analyzed.	Cisplatin	57-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21645448-9	2011	Up-regulated Hsp90 is associated with the chemoresistance to Cisplatin in SPCA-1and H446 cells.	Cisplatin	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
21486005-0	2011	Gambogic acid, a natural product inhibitor of Hsp90.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
21486005-1	2011	A high-throughput screening of natural product libraries identified (-)-gambogic acid (1), a component of the exudate of Garcinia harburyi, as a potential Hsp90 inhibitor, in addition to the known Hsp90 inhibitor celastrol (2).	gambogic acid	68-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
21486005-3	2011	Gambogic acid also disrupted the interaction of Hsp90, Hsp70, and Cdc37 with the heme-regulated eIF2alpha kinase (HRI, an Hsp90-dependent client) and blocked the maturation of HRI in vitro.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
21486005-3	2011	Gambogic acid also disrupted the interaction of Hsp90, Hsp70, and Cdc37 with the heme-regulated eIF2alpha kinase (HRI, an Hsp90-dependent client) and blocked the maturation of HRI in vitro.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
21517103-0	2011	Nano self-assembly of recombinant human gelatin conjugated with alpha-tocopheryl succinate for Hsp90 inhibitor, 17-AAG, delivery.	alpha-Tocopherol	64-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
21569548-12	2011	Celastrol downregulated HSP90 client proteins but did not disrupt the interaction between HSP90 and cdc37.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
21569548-13	2011	NAC completely inhibited celastrol-induced decrease of HSP90 client proteins, catalase and thioredoxin.	Acetylcysteine	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
21569548-13	2011	NAC completely inhibited celastrol-induced decrease of HSP90 client proteins, catalase and thioredoxin.	celastrol	25-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
21569548-18	2011	Celastrol induced the downregulation of HSP90 client proteins through ROS accumulation and facilitated ROS accumulation by inhibiting MRC complex I activity.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
21569548-18	2011	Celastrol induced the downregulation of HSP90 client proteins through ROS accumulation and facilitated ROS accumulation by inhibiting MRC complex I activity.	Reactive Oxygen Species	70-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
21438541-0	2011	Optimization of potent, selective, and orally bioavailable pyrrolodinopyrimidine-containing inhibitors of heat shock protein 90.	pyrrolodinopyrimidine	59-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-127
21374821-2	2011	Here, a novel series of Hsp90 inhibitors containing a quinolein-2-one scaffold was synthesized and evaluated in cell proliferation assays.	quinolein-2-one	54-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
21273068-0	2011	Identification and initial SAR of silybin: an Hsp90 inhibitor.	Silybin	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
21273068-1	2011	Through Hsp90-dependent firefly luciferase refolding and Hsp90-dependent heme-regulated eIF2alpha kinase (HRI) activation assays, silybin was identified as a novel Hsp90 inhibitor.	Silybin	130-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21273068-1	2011	Through Hsp90-dependent firefly luciferase refolding and Hsp90-dependent heme-regulated eIF2alpha kinase (HRI) activation assays, silybin was identified as a novel Hsp90 inhibitor.	Silybin	130-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
21273068-1	2011	Through Hsp90-dependent firefly luciferase refolding and Hsp90-dependent heme-regulated eIF2alpha kinase (HRI) activation assays, silybin was identified as a novel Hsp90 inhibitor.	Silybin	130-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
20652703-1	2011	PURPOSE: This crossover phase 1 study compared the pharmacokinetics and safety of tanespimycin, an HSP90 inhibitor, when administered as a suspension for injection and tanespimycin injection, a Cremophor-based formulation.	tanespimycin	82-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
21388435-8	2011	Immunoprecipitation of eNOS in human umbilical vein endothelial cells treated with 20-HETE revealed a decrease in basal and vascular endothelial growth factor-stimulated Hsp90 association with eNOS (P&lt;0.05).	20-hydroxy-5,8,11,14-eicosatetraenoic acid	83-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
21285336-1	2011	The benzoquinone ansamycins inhibit the ATPase activity of the 90-kDa heat shock protein (Hsp90), disrupting the function of numerous client proteins involved in oncogenesis.	benzoquinone ansamycins	4-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
21285336-2	2011	In this study, we examine the role of NAD(P)H:quinone oxidoreductase 1 (NQO1) in the metabolism of trans- and cis-amide isomers of the benzoquinone ansamycins and their mechanism of Hsp90 inhibition.	trans- and cis-amide	99-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
21285336-2	2011	In this study, we examine the role of NAD(P)H:quinone oxidoreductase 1 (NQO1) in the metabolism of trans- and cis-amide isomers of the benzoquinone ansamycins and their mechanism of Hsp90 inhibition.	benzoquinone ansamycins	135-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
21285336-3	2011	Inhibition of purified human Hsp90 by a series of benzoquinone ansamycins was examined in the presence and absence of NQO1, and their relative rate of NQO1-mediated reduction was determined.	benzoquinone ansamycins	50-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
21285336-5	2011	The trans-cis isomerization of the benzoquinone ansamycins in Hsp90 inhibition has been disputed in recent reports.	benzoquinone ansamycins	35-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
21285336-6	2011	Previous computational studies have used the closed or cocrystallized Hsp90 structures in an attempt to explore this isomerization step; however, we have successfully docked both the trans- and cis-amide isomers of the benzoquinone ansamycins into the open Hsp90 structure.	trans- and cis-amide	183-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21285336-6	2011	Previous computational studies have used the closed or cocrystallized Hsp90 structures in an attempt to explore this isomerization step; however, we have successfully docked both the trans- and cis-amide isomers of the benzoquinone ansamycins into the open Hsp90 structure.	trans- and cis-amide	183-203	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-262
21285336-6	2011	Previous computational studies have used the closed or cocrystallized Hsp90 structures in an attempt to explore this isomerization step; however, we have successfully docked both the trans- and cis-amide isomers of the benzoquinone ansamycins into the open Hsp90 structure.	benzoquinone ansamycins	219-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21285336-6	2011	Previous computational studies have used the closed or cocrystallized Hsp90 structures in an attempt to explore this isomerization step; however, we have successfully docked both the trans- and cis-amide isomers of the benzoquinone ansamycins into the open Hsp90 structure.	benzoquinone ansamycins	219-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-262
21285336-7	2011	The results of these studies indicate that both trans- and cis-amide isomers of the hydroquinone ansamycins exhibited increased binding affinity for Hsp90 relative to their parent quinones.	trans- and cis-amide	48-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
21285336-7	2011	The results of these studies indicate that both trans- and cis-amide isomers of the hydroquinone ansamycins exhibited increased binding affinity for Hsp90 relative to their parent quinones.	hydroquinone ansamycins	84-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
21285336-7	2011	The results of these studies indicate that both trans- and cis-amide isomers of the hydroquinone ansamycins exhibited increased binding affinity for Hsp90 relative to their parent quinones.	Quinones	180-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
21285336-8	2011	Our data support a mechanism in which trans- rather than cis-amide forms of benzoquinone ansamycins are metabolized by NQO1 to hydroquinone ansamycins and that Hsp90-mediated trans-cis isomerization via tautomerization plays an important role in subsequent Hsp90 inhibition.	trans- rather than cis-amide	38-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
21285336-8	2011	Our data support a mechanism in which trans- rather than cis-amide forms of benzoquinone ansamycins are metabolized by NQO1 to hydroquinone ansamycins and that Hsp90-mediated trans-cis isomerization via tautomerization plays an important role in subsequent Hsp90 inhibition.	trans- rather than cis-amide	38-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-262
21285336-8	2011	Our data support a mechanism in which trans- rather than cis-amide forms of benzoquinone ansamycins are metabolized by NQO1 to hydroquinone ansamycins and that Hsp90-mediated trans-cis isomerization via tautomerization plays an important role in subsequent Hsp90 inhibition.	benzoquinone ansamycins	76-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
21285336-8	2011	Our data support a mechanism in which trans- rather than cis-amide forms of benzoquinone ansamycins are metabolized by NQO1 to hydroquinone ansamycins and that Hsp90-mediated trans-cis isomerization via tautomerization plays an important role in subsequent Hsp90 inhibition.	benzoquinone ansamycins	76-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	257-262
21478269-8	2011	Interference with HSP90 either by RNA interference against HSF1, the transcriptional regulator of the HSP90 pathway, or by direct knockdown of Hsp90 protein or by pharmacologic inhibition of Hsp90 activity with 17AAG (17-allylamino-17-demethoxygeldanamycin) destroys the complex, liberates mutant p53, and reactivates endogenous MDM2 and CHIP to degrade mutant p53.	tanespimycin	211-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
21478269-8	2011	Interference with HSP90 either by RNA interference against HSF1, the transcriptional regulator of the HSP90 pathway, or by direct knockdown of Hsp90 protein or by pharmacologic inhibition of Hsp90 activity with 17AAG (17-allylamino-17-demethoxygeldanamycin) destroys the complex, liberates mutant p53, and reactivates endogenous MDM2 and CHIP to degrade mutant p53.	tanespimycin	211-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
21478269-8	2011	Interference with HSP90 either by RNA interference against HSF1, the transcriptional regulator of the HSP90 pathway, or by direct knockdown of Hsp90 protein or by pharmacologic inhibition of Hsp90 activity with 17AAG (17-allylamino-17-demethoxygeldanamycin) destroys the complex, liberates mutant p53, and reactivates endogenous MDM2 and CHIP to degrade mutant p53.	tanespimycin	218-256	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
21478269-8	2011	Interference with HSP90 either by RNA interference against HSF1, the transcriptional regulator of the HSP90 pathway, or by direct knockdown of Hsp90 protein or by pharmacologic inhibition of Hsp90 activity with 17AAG (17-allylamino-17-demethoxygeldanamycin) destroys the complex, liberates mutant p53, and reactivates endogenous MDM2 and CHIP to degrade mutant p53.	tanespimycin	218-256	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
21383049-2	2011	The aim of this study was to assess the antitumor activity of the Hsp90 inhibitor IPI-504 in trastuzumab-resistant, HER2-overexpressing breast cancer cells.	tanespimycin	82-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
21383049-9	2011	IPI-504-mediated Hsp90 inhibition may represent a novel therapeutic approach in trastuzumab refractory HER2-positive breast cancer.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
21414251-8	2011	For bacterial, yeast and human Hsp90, there is a conserved three-state (apo-ATP-ADP) conformational cycle; however; the equilibria between states are species specific.	atp-adp	76-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
21325639-6	2011	Treatment of Pnck-overexpressing cells with the pharmacologic Hsp90 inhibitor geldanamycin results in enhanced EGFR degradation, and destruction of Pnck.	geldanamycin	78-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
21325639-7	2011	In cells in which Pnck is inducing EGFR degradation, we observed that Hsp90 exhibits reduced electrophoretic mobility, and through mass spectrometric analysis of immunopurified Hsp90 protein we demonstrated enhanced phosphorylation at threonine 89 and 616 (in both Hsp90-alpha and -beta) and serine 391 (in Hsp90-alpha).	Threonine	235-244	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
21826987-0	2011	[Effect of heat shock protein 90 inhibitor 17-dimethylamino-ethylaminogeldanamycin on TNfalpha-mediated apoptosis and TNF-induced NF-kappaB activation].	17-dimethylamino-ethylaminogeldanamycin	43-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-32
21826987-1	2011	OBJECTIVE: To investigate the effect of heat shock protein 90 (HSP90) inhibitor 17-dimethylaminoethylaminogeldanamycin (17DMAG) on tumor necrosis factor alpha (TNFalpha) mediated apopotosis in cancer cells and the underlying molecular mechanisms.	17-dimethylaminoethylaminogeldanamycin	80-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
21826987-1	2011	OBJECTIVE: To investigate the effect of heat shock protein 90 (HSP90) inhibitor 17-dimethylaminoethylaminogeldanamycin (17DMAG) on tumor necrosis factor alpha (TNFalpha) mediated apopotosis in cancer cells and the underlying molecular mechanisms.	17-dimethylaminoethylaminogeldanamycin	80-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
21826987-1	2011	OBJECTIVE: To investigate the effect of heat shock protein 90 (HSP90) inhibitor 17-dimethylaminoethylaminogeldanamycin (17DMAG) on tumor necrosis factor alpha (TNFalpha) mediated apopotosis in cancer cells and the underlying molecular mechanisms.	17DMAG	120-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
21826987-1	2011	OBJECTIVE: To investigate the effect of heat shock protein 90 (HSP90) inhibitor 17-dimethylaminoethylaminogeldanamycin (17DMAG) on tumor necrosis factor alpha (TNFalpha) mediated apopotosis in cancer cells and the underlying molecular mechanisms.	17DMAG	120-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
21414251-9	2011	In eukaryotes, cytosolic co-chaperones regulate the in vivo dynamic behavior of Hsp90 by shifting conformational equilibria and affecting the kinetics of structural changes and ATP hydrolysis.	Adenosine Triphosphate	177-180	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
21439943-1	2011	Previously, we found that treatment of cells with the Hsp90 inhibitor geldanamycin (GA) leads to a substantial reduction in the number of processing bodies (P-bodies), and also alters the size and subcellular localization of stress granules.	geldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
21439943-1	2011	Previously, we found that treatment of cells with the Hsp90 inhibitor geldanamycin (GA) leads to a substantial reduction in the number of processing bodies (P-bodies), and also alters the size and subcellular localization of stress granules.	geldanamycin	84-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
21439943-3	2011	To verify these observations, we examined whether another Hsp90 inhibitor radicicol (RA) affected P-bodies and stress granules.	monorden	74-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
21420297-1	2011	A novel series of macrocyclic ortho-aminobenzamide Hsp90 inhibitors is reported.	anthranilamide	30-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21372220-5	2011	The antitumor activity of specific heat shock protein 90 (Hsp90) inhibitors was investigated by an analysis of cell viability, cell cycle, and apoptosis using MTT-assays and flow cytometry.	monooxyethylene trimethylolpropane tristearate	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-56
21459002-1	2011	A number of compounds from different chemical classes are known to bind competitively to the ATP-pocket of Hsp90 and inhibit its chaperone function.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
21459002-2	2011	The natural product geldanamycin was the first reported inhibitor of Hsp90 and since then synthetic inhibitors from purine, isoxazole and indazol-4-one chemical classes have been discovered and are currently or soon to be in clinical trials for the treatment of cancer.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
21372220-5	2011	The antitumor activity of specific heat shock protein 90 (Hsp90) inhibitors was investigated by an analysis of cell viability, cell cycle, and apoptosis using MTT-assays and flow cytometry.	monooxyethylene trimethylolpropane tristearate	159-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
21330372-12	2011	Geldanamycin (GA), a specific Hsp90 inhibitor, disrupts the Hsp90-PI4KIIbeta interaction and destabilizes PI4KIIbeta, reducing its half-life by 40% and increasing its susceptibility to ubiquitylation and proteasomal degradation.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
21346199-0	2011	Heat shock protein 90-mediated inactivation of nuclear factor-kappaB switches autophagy to apoptosis through becn1 transcriptional inhibition in selenite-induced NB4 cells.	Selenious Acid	145-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
21346199-3	2011	Here, we report that selenite treatment triggers opposite patterns of autophagy in the NB4, HL60, and Jurkat leukemia cell lines during apoptosis and provide evidence that the suppressive effect of selenite on autophagy in NB4 cells is due to the decreased expression of the chaperone protein Hsp90 (heat shock protein 90), suggesting a novel regulatory function of Hsp90 in apoptosis and autophagy.	Selenious Acid	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	293-298
21346199-3	2011	Here, we report that selenite treatment triggers opposite patterns of autophagy in the NB4, HL60, and Jurkat leukemia cell lines during apoptosis and provide evidence that the suppressive effect of selenite on autophagy in NB4 cells is due to the decreased expression of the chaperone protein Hsp90 (heat shock protein 90), suggesting a novel regulatory function of Hsp90 in apoptosis and autophagy.	Selenious Acid	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	300-321
21346199-3	2011	Here, we report that selenite treatment triggers opposite patterns of autophagy in the NB4, HL60, and Jurkat leukemia cell lines during apoptosis and provide evidence that the suppressive effect of selenite on autophagy in NB4 cells is due to the decreased expression of the chaperone protein Hsp90 (heat shock protein 90), suggesting a novel regulatory function of Hsp90 in apoptosis and autophagy.	Selenious Acid	21-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	366-371
21346199-4	2011	Excessive or insufficient expression indicates that Hsp90 protects NB4 cells from selenite-induced apoptosis, and selenite-induced decreases in the expression of Hsp90, especially in NB4 cells, inhibit the activities of the IkappaB kinase/nuclear factor-kappaB (IKK/NF-kappaB) signaling pathway, leading to less nuclear translocation and inactivation of NF-kappaB and the subsequent weak binding of the becn1 promoter, which facilitates the transition from autophagy to apoptosis.	Selenious Acid	114-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
21346199-5	2011	Taken together, our observations provide novel insights into the mechanisms underlying the balance between apoptosis and autophagy, and we also identified Hsp90-NF-kappaB-Beclin1 as a potential biological pathway for signaling the switch from autophagy to apoptosis in selenite-treated NB4 cells.	Selenious Acid	269-277	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
21330372-12	2011	Geldanamycin (GA), a specific Hsp90 inhibitor, disrupts the Hsp90-PI4KIIbeta interaction and destabilizes PI4KIIbeta, reducing its half-life by 40% and increasing its susceptibility to ubiquitylation and proteasomal degradation.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
21330372-12	2011	Geldanamycin (GA), a specific Hsp90 inhibitor, disrupts the Hsp90-PI4KIIbeta interaction and destabilizes PI4KIIbeta, reducing its half-life by 40% and increasing its susceptibility to ubiquitylation and proteasomal degradation.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
21474071-5	2011	FRET measurements show that Delta131Delta accelerates the nucleotide-driven open/closed transition and stimulates ATP hydrolysis by Hsp90.	Adenosine Triphosphate	114-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
21330372-12	2011	Geldanamycin (GA), a specific Hsp90 inhibitor, disrupts the Hsp90-PI4KIIbeta interaction and destabilizes PI4KIIbeta, reducing its half-life by 40% and increasing its susceptibility to ubiquitylation and proteasomal degradation.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
21330372-15	2011	Stimuli such as PDGF receptor activation that also induce recruitment of the kinase to membranes disrupt the Hsp90-PI4KIIbeta interaction to a similar extent as GA treatment.	geldanamycin	161-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
21508365-0	2011	Antitumor effect of novel HSP90 inhibitor NVP-AUY922 against oral squamous cell carcinoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	46-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21508365-5	2011	NVP-AUY922 (Novartis) is a novel 4,5-diaryloxazole adenosine triphosphate-binding site HSP90 inhibitor.	4,5-diaryloxazole adenosine triphosphate	33-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
21050069-2	2011	Our previous studies have shown that Gyrase, Hsp90, MutL (GHL) inhibitors bind to the ATP-binding pocket of HK and may provide lead compounds for the design of novel antibiotics targeting these kinases.	Adenosine Triphosphate	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
21210767-0	2011	Cyclic lipopeptide antibiotics bind to the N-terminal domain of the prokaryotic Hsp90 to inhibit the chaperone activity.	cyclic lipopeptide antibiotics	0-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
21352196-7	2011	We demonstrate that the HSP90 inhibitor 17-DMAG exhibited synergy with dasatinib in vitro, and moreover, induced apoptosis of CLL cells in the CD154L/IL-4 system.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	40-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
21352196-7	2011	We demonstrate that the HSP90 inhibitor 17-DMAG exhibited synergy with dasatinib in vitro, and moreover, induced apoptosis of CLL cells in the CD154L/IL-4 system.	Dasatinib	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
21353544-0	2011	Synthesis and biological evaluation of 2,4-diaminoquinazoline derivatives as novel heat shock protein 90 inhibitors.	2,4-diaminoquinazoline	39-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
21542685-4	2011	The matrices were also loaded with the heat-shock protein (HSP)90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17-AAG), currently in clinical trials for different malignancies, in order to deliver a combination of hyperthermia and chemotherapy.	tanespimycin	76-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-65
21353544-1	2011	Novel 2,4-diaminoquinazoline derivatives originating from a virtual screening approach were designed, synthesized and their biological activities as heat shock protein 90 (Hsp90) inhibitors were evaluated.	2,4-diaminoquinazoline	6-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-170
21353544-1	2011	Novel 2,4-diaminoquinazoline derivatives originating from a virtual screening approach were designed, synthesized and their biological activities as heat shock protein 90 (Hsp90) inhibitors were evaluated.	2,4-diaminoquinazoline	6-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
21360678-5	2011	Mutation of PP5, replacing key basic amino acids (K97A and R101A) in the tetratricopeptide repeat (TPR) region known to be necessary for the interactions with Hsp90, abolished both the known interaction of PP5 with cell division cycle 37 homolog and the novel interaction of PP5 with stress-induced phosphoprotein 1.	Amino Acids, Basic	31-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
21278242-1	2011	PURPOSE: A phase I study to define toxicity and recommend a phase II dose of the HSP90 inhibitor alvespimycin (17-DMAG; 17-dimethylaminoethylamino-17-demethoxygeldanamycin).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	97-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
21334891-0	2011	Synthesis and in vitro anti-HSV-1 activity of a novel Hsp90 inhibitor BJ-B11.	2-(4-acetyloxycyclohexylamino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indazol-1-yl)-benzamide	70-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
21368131-1	2011	Geldanamycin and its derivative 17AAG [17-(Allylamino)-17-demethoxygeldanamycin, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
21368131-1	2011	Geldanamycin and its derivative 17AAG [17-(Allylamino)-17-demethoxygeldanamycin, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function.	tanespimycin	32-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
21368131-1	2011	Geldanamycin and its derivative 17AAG [17-(Allylamino)-17-demethoxygeldanamycin, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function.	tanespimycin	39-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
21368131-1	2011	Geldanamycin and its derivative 17AAG [17-(Allylamino)-17-demethoxygeldanamycin, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function.	telatinib	81-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
21368131-5	2011	In contrast, the HSP90 inhibitor radicicol, lacking a bezoquinone moiety, has no measurable effect on cationic current and is less effective in influencing intercellular Ca(2+) concentration.	monorden	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
21408192-0	2011	High-content, high-throughput analysis of cell cycle perturbations induced by the HSP90 inhibitor XL888.	XL 888	98-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
21278242-1	2011	PURPOSE: A phase I study to define toxicity and recommend a phase II dose of the HSP90 inhibitor alvespimycin (17-DMAG; 17-dimethylaminoethylamino-17-demethoxygeldanamycin).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	111-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
21278242-1	2011	PURPOSE: A phase I study to define toxicity and recommend a phase II dose of the HSP90 inhibitor alvespimycin (17-DMAG; 17-dimethylaminoethylamino-17-demethoxygeldanamycin).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	120-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
21446842-5	2011	CDH(2) is demonstrated ab initio using a previously well-characterized Hsp90/Cdc37 complex.	cdh	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
21306907-1	2011	Structure based drug design (SBDD) was used to discover heat shock protein 90 (HSP90) inhibitors useful in the treatment of cancer.	sbdd	29-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-77
21306907-1	2011	Structure based drug design (SBDD) was used to discover heat shock protein 90 (HSP90) inhibitors useful in the treatment of cancer.	sbdd	29-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
20966961-0	2011	Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90.	pidd	14-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
20966961-4	2011	In this study, we screened for novel PIDD regulators and identified heat shock protein 90 (Hsp90) as a major effector in both PIDD protein maturation and activation.	pidd	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
20966961-4	2011	In this study, we screened for novel PIDD regulators and identified heat shock protein 90 (Hsp90) as a major effector in both PIDD protein maturation and activation.	pidd	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
20966961-5	2011	Hsp90, together with p23, binds PIDD and inhibition of Hsp90 activity with geldanamycin efficiently disrupts this association and impairs PIDD auto-processing.	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20966961-5	2011	Hsp90, together with p23, binds PIDD and inhibition of Hsp90 activity with geldanamycin efficiently disrupts this association and impairs PIDD auto-processing.	geldanamycin	75-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
21249311-0	2011	Enhancement of radiation sensitivity in lung cancer cells by celastrol is mediated by inhibition of Hsp90.	celastrol	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
21249311-4	2011	Celastrol inhibited the ATP-binding activity of Hsp90.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
21249311-4	2011	Celastrol inhibited the ATP-binding activity of Hsp90.	Adenosine Triphosphate	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
21249311-5	2011	Furthermore, celastrol treatment dissociated an Hsp90 client protein, EGFR, and this in turn resulted in degradation of the client protein.	celastrol	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
21249311-8	2011	Celastrol may be considered an effective radiosensitizer acting as an inhibitor of Hsp90 and a p53 activator.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
21156818-5	2011	After treatment with 17AAG, biomarkers of Hsp90 inhibition, including markers of cell-cycle arrest, were more pronounced in NQO1-expressing cells compared with NQO1-null cells.	tanespimycin	21-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
21417768-9	2011	An Hsp90 inhibitor, 17-DMAG, was able to inhibit the eNOS and Hsp90 interaction, decrease the level of eNOS, and significantly inhibit cord formation to 38% of the level observed in the control.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
21417768-9	2011	An Hsp90 inhibitor, 17-DMAG, was able to inhibit the eNOS and Hsp90 interaction, decrease the level of eNOS, and significantly inhibit cord formation to 38% of the level observed in the control.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
21347335-7	2011	Furthermore, HSP90 was involved in mediating Lexa and CHX combination treatment-induced ROS increase and apoptotic death.	Reactive Oxygen Species	88-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
21127066-5	2011	In the presence of EGF, U87 cells showed HSP90alpha-induced Ca(2+) oscillations, which were reduced by the ATP/ADPase, apyrase, and inhibited by the purinergic P(2) inhibitor, suramin, suggesting that ATP release is requested.	Adenosine Triphosphate	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-51
21127066-6	2011	Disruption of lipid rafts with methyl beta-cyclodextrin impaired the Ca(2+) rise induced by extracellular HSP90alpha combined with EGF.	methyl-beta-cyclodextrin	31-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
21127066-10	2011	Extracellular HSP90alpha induced EGFR phosphorylation at Tyr-1068, and this event was prevented by both the protein kinase Cdelta inhibitor, rottlerin, and the c-Src inhibitor, PP2.	Tyrosine	57-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-24
21127066-10	2011	Extracellular HSP90alpha induced EGFR phosphorylation at Tyr-1068, and this event was prevented by both the protein kinase Cdelta inhibitor, rottlerin, and the c-Src inhibitor, PP2.	rottlerin	141-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-24
21127066-11	2011	Altogether, our results suggest that extracellular HSP90alpha transactivates EGFR/ErbB1 through TLR4 and a PKCdelta/c-Src pathway, which induces ATP release and cytosolic Ca(2+) increase and finally favors cell migration.	Adenosine Triphosphate	145-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-61
21145921-4	2011	Treatment with three distinct HSP90 inhibitors, radicicol, macbecin and 17-DMAG significantly enhanced alpha(2C)-AR cell surface levels at 37 C, but these inhibitors had no effect at 30 C. Similar results were obtained after decreasing the HSP90 cellular levels using specific siRNA.	monorden	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
21145921-4	2011	Treatment with three distinct HSP90 inhibitors, radicicol, macbecin and 17-DMAG significantly enhanced alpha(2C)-AR cell surface levels at 37 C, but these inhibitors had no effect at 30 C. Similar results were obtained after decreasing the HSP90 cellular levels using specific siRNA.	Macbecin	59-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
21145921-4	2011	Treatment with three distinct HSP90 inhibitors, radicicol, macbecin and 17-DMAG significantly enhanced alpha(2C)-AR cell surface levels at 37 C, but these inhibitors had no effect at 30 C. Similar results were obtained after decreasing the HSP90 cellular levels using specific siRNA.	Macbecin	59-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
21145921-4	2011	Treatment with three distinct HSP90 inhibitors, radicicol, macbecin and 17-DMAG significantly enhanced alpha(2C)-AR cell surface levels at 37 C, but these inhibitors had no effect at 30 C. Similar results were obtained after decreasing the HSP90 cellular levels using specific siRNA.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
21145921-4	2011	Treatment with three distinct HSP90 inhibitors, radicicol, macbecin and 17-DMAG significantly enhanced alpha(2C)-AR cell surface levels at 37 C, but these inhibitors had no effect at 30 C. Similar results were obtained after decreasing the HSP90 cellular levels using specific siRNA.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
21219297-3	2011	Tanespimycin, an HSP90 inhibitor, reduces tumour cell survival in vitro.	tanespimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
21219297-8	2011	HSP90 inhibition is a promising strategy in MM especially in combination with bortezomib; additional studies will further evaluate optimal dosings of candidate drugs and schedules, as well as confirm efficacy in comparative phase III trials.	Bortezomib	78-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
21454186-2	2011	Like its parent compound geldanamycin, tanespimycin binds to HSP90 and causes antineoplastic effects in vitro and in vivo.	tanespimycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
20585984-0	2011	Targeting PI3K/Akt/HSP90 signaling sensitizes gastric cancer cells to deoxycholate-induced apoptosis.	Deoxycholic Acid	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
20585984-11	2011	Although, deoxycholate at low concentration (50 microM) slightly inhibited the expression of pAkt and cleaved HSP90 to 55 KDa fragment, no significant effect on apoptosis induction, up to 4 h (as assessed by caspase-3 activation) was observed.	Deoxycholic Acid	10-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
20585984-12	2011	The higher concentrations of DC (100 microM-300 microM) resulted in progressive inhibition of pAkt, activation of PTEN, and specific cleavage of HSP90 to approximately 45 KDa fragments with significant induction of apoptosis.	Deoxycholic Acid	29-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
20585984-15	2011	CONCLUSIONS: These results demonstrate that down-regulation of PI3K/Akt pathway with specific cleavage of HSP90 to 45 KDa modulates the pro-apoptotic effects of DC in gastric cells.	Deoxycholic Acid	161-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
21268072-9	2011	In addition, GA prevented Hsp90/mutant p53 complex formation and enhanced interaction of mutant p53 with Hsp70.	gambogic acid	13-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21082217-0	2011	Carbamazepine promotes Her-2 protein degradation in breast cancer cells by modulating HDAC6 activity and acetylation of Hsp90.	Carbamazepine	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
21082217-3	2011	Therefore, in this study we examined the effect of carbamazepine, which could inhibit HDAC on Hsp90 acetylation and Her-2 stability.	Carbamazepine	51-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
21082217-4	2011	The results of this study demonstrate that while carbamazepine had no effect on the Her-2 mRNA level, it induced Her-2 protein degradation via the proteasome pathway by disrupting the chaperone function of Hsp90 in SK-BR-3 cells.	Carbamazepine	49-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
20955164-4	2011	The chaperone activity of Hsc70/Hsp70 and Hsp90 occurs in coordinated cycles of ATP hydrolysis and substrate binding, and is regulated by a number of co-chaperone proteins.	Adenosine Triphosphate	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
21106982-4	2011	In bortezomib-resistant cells, both BiP/Grp78 knockdown and cell pretreatment with the Hsp90 inhibitor of the ansamycin class, IPI-504, led to synergistic induction of apoptotic cell death when combined with bortezomib.	Bortezomib	3-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
21106982-0	2011	The Hsp90 inhibitor IPI-504 overcomes bortezomib resistance in mantle cell lymphoma in vitro and in vivo by down-regulation of the prosurvival ER chaperone BiP/Grp78.	tanespimycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21156818-0	2011	Role for NAD(P)H:quinone oxidoreductase 1 and manganese-dependent superoxide dismutase in 17-(allylamino)-17-demethoxygeldanamycin-induced heat shock protein 90 inhibition in pancreatic cancer cells.	tanespimycin	90-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-160
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	tanespimycin	128-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	tanespimycin	128-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	tanespimycin	170-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	tanespimycin	170-175	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	hydroquinone	198-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	hydroquinone	198-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	17aagh2	212-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
21156818-1	2011	Previous work demonstrated that NAD(P)H:quinone oxidoreductase 1 (NQO1) metabolized the heat shock protein 90 (Hsp90) inhibitor 17-(allylamino)-17-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone (17AAGH2).	17aagh2	212-219	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
21156818-2	2011	The formation of 17AAGH2 by NQO1 results in a molecule that binds with greater affinity to Hsp90 compared with the parent quinone.	quinone	122-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
21283735-8	2011	On top of the list, three HSP90 inhibitors, i.e. 17-AAG (also known as tanespimycin), monorden, and alvespimycin, showed significant negative enrichment scores.	tanespimycin	49-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21283735-8	2011	On top of the list, three HSP90 inhibitors, i.e. 17-AAG (also known as tanespimycin), monorden, and alvespimycin, showed significant negative enrichment scores.	tanespimycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21283735-8	2011	On top of the list, three HSP90 inhibitors, i.e. 17-AAG (also known as tanespimycin), monorden, and alvespimycin, showed significant negative enrichment scores.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
21106982-0	2011	The Hsp90 inhibitor IPI-504 overcomes bortezomib resistance in mantle cell lymphoma in vitro and in vivo by down-regulation of the prosurvival ER chaperone BiP/Grp78.	Bortezomib	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21106982-4	2011	In bortezomib-resistant cells, both BiP/Grp78 knockdown and cell pretreatment with the Hsp90 inhibitor of the ansamycin class, IPI-504, led to synergistic induction of apoptotic cell death when combined with bortezomib.	Rifabutin	110-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
21106982-4	2011	In bortezomib-resistant cells, both BiP/Grp78 knockdown and cell pretreatment with the Hsp90 inhibitor of the ansamycin class, IPI-504, led to synergistic induction of apoptotic cell death when combined with bortezomib.	tanespimycin	127-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
21106982-4	2011	In bortezomib-resistant cells, both BiP/Grp78 knockdown and cell pretreatment with the Hsp90 inhibitor of the ansamycin class, IPI-504, led to synergistic induction of apoptotic cell death when combined with bortezomib.	Bortezomib	208-218	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
21106982-5	2011	Cell exposure to the IPI-504-bortezomib combination provoked the dissociation of Hsp90/BiP complexes, leading to BiP/Grp78 depletion, inhibition of unfolded protein response, and promotion of NOXA-mediated mitochondrial depolarization.	ipi-504-bortezomib	21-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
21106982-7	2011	These results suggest that targeting unfolded protein response activation by the inhibition of Hsp90 may be an attractive model for the design of a new bortezomib-based combination therapy for MCL.	Bortezomib	152-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
21183720-3	2011	The chaperoning mechanism of Hsp90 is controlled by ATP and various cochaperones, but is poorly understood and controversial.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
21183720-9	2011	The p23-dependent NMR shifts mapped to both the lid and the adenine end of Hsp90"s ATP binding pocket, but also to large parts of the middle domain.	Adenosine Triphosphate	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
21183720-4	2011	Here, we characterized the Apo and ATP states of the 170-kDa human Hsp90 full-length protein by NMR spectroscopy in solution, and we elucidated the mechanism of the inhibition of its ATPase by its cochaperone p23.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
21183720-6	2011	We found that ATP caused exclusively local changes in Hsp90"s N-terminal nucleotide-binding domain.	Adenosine Triphosphate	14-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
21183720-9	2011	The p23-dependent NMR shifts mapped to both the lid and the adenine end of Hsp90"s ATP binding pocket, but also to large parts of the middle domain.	Adenine	60-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
20883729-2	2011	Inhibition of HSP90 by inhibitors such as 17-allylamino-demethoxy-geldanamycin (17AAG) is known to induce apoptosis in various cancer cells by decreasing the activation or expression of pro-survival molecules such as protein kinase B (Akt).	17-allylamino-demethoxy-geldanamycin	42-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
21144839-5	2011	The present work reports a bio-computational study carried out with the aim of exploring the dual inhibition of Hsp90/Cdc37 chaperone/co-chaperone association complex by the naturally occurring drug candidates withaferin A and 17-DMAG along with their possible modes of action.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	227-234	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
20883729-2	2011	Inhibition of HSP90 by inhibitors such as 17-allylamino-demethoxy-geldanamycin (17AAG) is known to induce apoptosis in various cancer cells by decreasing the activation or expression of pro-survival molecules such as protein kinase B (Akt).	tanespimycin	80-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20883729-10	2011	Our work provides the molecular mechanism by which HSP90 inhibition delays cell migration and should be useful in developing cancer treatment strategies with known anti-cancer drugs such as cisplatin in combination with HSP90 inhibitors.	Cisplatin	190-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
21088503-3	2011	The triterpene natural product Celastrol inhibits HSP90 and several pathways relevant to ErbB2-dependent oncogenesis including the NFkappaB pathway and the proteasome, and has shown promising activity in other cancer models.	Triterpenes	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
21111762-0	2011	Calpain digestion and HSP90-based chaperone protection modulate the level of plasma membrane F508del-CFTR.	f508del	93-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
21088503-3	2011	The triterpene natural product Celastrol inhibits HSP90 and several pathways relevant to ErbB2-dependent oncogenesis including the NFkappaB pathway and the proteasome, and has shown promising activity in other cancer models.	celastrol	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
21088503-7	2011	Mechanistically, Celastrol not only induced the expected ubiquitinylation and degradation of ErbB2 and other HSP90 client proteins, but it also increased the levels of reactive oxygen species (ROS).	celastrol	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
21111762-8	2011	The recovery of HSP90 binding capacity in F508del-CFTR, following digestion, explains the large accumulation of the 100 kDa CFTR form in circulating PBMC from CF patients.	f508del	42-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
21129982-1	2011	Several Hsp90 modulators have been identified including the N-terminal ligand geldanamycin (GDA), the C-terminal ligand novobiocin (NB), and the co-chaperone disruptor celastrol.	geldanamycin	78-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21129982-1	2011	Several Hsp90 modulators have been identified including the N-terminal ligand geldanamycin (GDA), the C-terminal ligand novobiocin (NB), and the co-chaperone disruptor celastrol.	geldanamycin	92-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21129982-1	2011	Several Hsp90 modulators have been identified including the N-terminal ligand geldanamycin (GDA), the C-terminal ligand novobiocin (NB), and the co-chaperone disruptor celastrol.	Novobiocin	120-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21129982-1	2011	Several Hsp90 modulators have been identified including the N-terminal ligand geldanamycin (GDA), the C-terminal ligand novobiocin (NB), and the co-chaperone disruptor celastrol.	celastrol	168-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
21129982-3	2011	For example, the natural product gedunin and the synthetic anti-spermatogenic agent H2-gamendazole, recently identified Hsp90 modulators, manifest biological activity through undefined mechanisms.	h2-gamendazole	84-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
21129982-5	2011	Such studies provided evidence that gedunin and H2-gamendazole both modulate Hsp90 via a mechanism similar to celastrol, and unlike NB or GDA.	h2-gamendazole	48-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
21821931-0	2011	SNX-2112, a novel Hsp90 inhibitor, induces G2/M cell cycle arrest and apoptosis in MCF-7 cells.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
21821931-1	2011	SNX-2112 is a heat shock protein 90 (Hsp90) inhibitor with anticancer properties currently in clinical trials.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
21821931-1	2011	SNX-2112 is a heat shock protein 90 (Hsp90) inhibitor with anticancer properties currently in clinical trials.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
20981255-3	2011	We demonstrate that Hsp90 inhibition by geldanamycin can effectively suppress proteasome inhibitor, MG-132-induced protein aggregation in a way that is independent of HDAC inhibition or the tubulin acetylation levels in ARPE-19 cells.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
21208906-0	2011	Antitumor activity of SNX-2112, a synthetic heat shock protein-90 inhibitor, in MET-amplified tumor cells with or without resistance to selective MET Inhibition.	SNX 2112	22-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-65
21208906-4	2011	EXPERIMENTAL DESIGN: The aim of our study was to assess the efficacy of SNX-2112, a synthetic HSP-90 inhibitor, in 3 different MET-amplified tumor cell lines (GTL-16, MKN-45, and EBC-1) as well as PR-GTL-16 cells, a GTL-16 subline selected for resistance to the highly selective MET kinase inhibitor PHA-665752.	SNX 2112	72-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-100
21568884-7	2011	We will illustrate the review with some of our results concerning the effects of oxidative stress on Hsp90 using various oxidative stress-generating systems based on different quinones in combination with a well-known reducing agent (i.e., ascorbate).	Ascorbic Acid	240-249	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
20937381-7	2011	The heat-shock proteins Hsp70/Hsp40, Hsp90 and a proposed pharmacological PAH chaperone (3-amino-2-benzyl-7-nitro-4-(2-quinolyl)-1,2-dihydroisoquinolin-1-one) partly inhibit the self-association process.	3-amino-2-benzyl-7-nitro-4-(2-quinolyl)-1,2-dihydroisoquinolin-1-one	89-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
22087060-1	2011	Inhibiting Hsp90 chaperone roles using 17AAG induces cytostasis or apoptosis in tumor cells through destabilization of several mutated cancer promoting proteins.	tanespimycin	39-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
22087060-3	2011	Here, we show that Hsp90 inhibition with 17AAG first affects mitochondrial integrity in different human tumor cells, neuroblastoma, cervical cancer and glial cells.	tanespimycin	41-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
20981255-3	2011	We demonstrate that Hsp90 inhibition by geldanamycin can effectively suppress proteasome inhibitor, MG-132-induced protein aggregation in a way that is independent of HDAC inhibition or the tubulin acetylation levels in ARPE-19 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	100-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
21875325-0	2011	Sulforaphane potentiates the efficacy of 17-allylamino 17-demethoxygeldanamycin against pancreatic cancer through enhanced abrogation of Hsp90 chaperone function.	sulforaphane	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
21756040-5	2011	Administration of the specific Hsp90 inhibitor geldanamycin as well as RNAi directed against HSP90 effectively inhibited EGFR activation, suggesting an essential role for Hsp90 in hyperthermia-induced EGFR activation.	geldanamycin	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
21756040-5	2011	Administration of the specific Hsp90 inhibitor geldanamycin as well as RNAi directed against HSP90 effectively inhibited EGFR activation, suggesting an essential role for Hsp90 in hyperthermia-induced EGFR activation.	geldanamycin	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
21756040-6	2011	In addition, cells treated with geldanamycin were sensitised to heat treatment, suggesting that adding Hsp90 inhibitors to hyperthermia regimens might have a beneficial effect for cancer treatment.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
21875325-0	2011	Sulforaphane potentiates the efficacy of 17-allylamino 17-demethoxygeldanamycin against pancreatic cancer through enhanced abrogation of Hsp90 chaperone function.	tanespimycin	41-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
21875325-5	2011	ATP binding assay and coimmunoprecipitation revealed that sulforaphane disrupted Hsp90-p50(Cdc37) interaction, whereas 17-AAG inhibited ATP binding to Hsp90.	sulforaphane	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
21245936-6	2011	Multi-RTK inhibition by the HSP90 inhibitor 17-allyloamino-17-demethoxygeldanamycin (17-AAG) had a substantially greater effect on mesothelioma proliferation and survival compared with inhibition of individual activated RTKs.	17-allyloamino-17-demethoxygeldanamycin	44-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
21245936-6	2011	Multi-RTK inhibition by the HSP90 inhibitor 17-allyloamino-17-demethoxygeldanamycin (17-AAG) had a substantially greater effect on mesothelioma proliferation and survival compared with inhibition of individual activated RTKs.	tanespimycin	85-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
21875325-5	2011	ATP binding assay and coimmunoprecipitation revealed that sulforaphane disrupted Hsp90-p50(Cdc37) interaction, whereas 17-AAG inhibited ATP binding to Hsp90.	Adenosine Triphosphate	136-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
21875325-6	2011	Concomitant use of sulforaphane and 17-AAG synergistically downregulated Hsp90 client proteins in Mia Paca-2 cells.	sulforaphane	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
21875325-8	2011	Our data suggest that sulforaphane potentiates the efficacy of 17-AAG against pancreatic cancer through enhanced abrogation of Hsp90 function.	sulforaphane	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
22073242-0	2011	Phase I evaluation of STA-1474, a prodrug of the novel HSP90 inhibitor ganetespib, in dogs with spontaneous cancer.	STA 9090	71-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
22073242-1	2011	BACKGROUND: The novel water soluble compound STA-1474 is metabolized to ganetespib (formerly STA-9090), a potent HSP90 inhibitor previously shown to kill canine tumor cell lines in vitro and inhibit tumor growth in the setting of murine xenografts.	Water	22-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
22073242-1	2011	BACKGROUND: The novel water soluble compound STA-1474 is metabolized to ganetespib (formerly STA-9090), a potent HSP90 inhibitor previously shown to kill canine tumor cell lines in vitro and inhibit tumor growth in the setting of murine xenografts.	STA 9090	72-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
21949862-0	2011	The soluble recombinant Neisseria meningitidis adhesin NadA(Delta351-405) stimulates human monocytes by binding to extracellular Hsp90.	N-acetyldopamine	55-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
21949677-0	2011	Degradation of HIF-1alpha under hypoxia combined with induction of Hsp90 polyubiquitination in cancer cells by hypericin: a unique cancer therapy.	hypericin	111-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
21949677-2	2011	Hypericin is the only known exogenous reagent that can induce forced poly-ubiquitination and accelerated degradation of heat shock protein 90 (Hsp90) in cancer cells.	hypericin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-141
21949677-2	2011	Hypericin is the only known exogenous reagent that can induce forced poly-ubiquitination and accelerated degradation of heat shock protein 90 (Hsp90) in cancer cells.	hypericin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
21647436-9	2011	The crystal structure of MC-HSP90 reveals that, in addition to the C-terminal dimerization domain, the residue W320 in the M domain plays a critical role in its oligomerization.	Methylcholanthrene	25-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
21950128-1	2011	rTNFalpha-induced programmed death of Jurkat tumor cells cultured with 17-AAG, a selective inhibitor of heat shock protein (Hsp90), was studied by fluorescent microscopy with the use of FITC-labeled annexin V and propidium iodide.	rtnfalpha	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
20880838-1	2010	Hsp90 is an ATP-dependent molecular chaperone, which facilitates the activation and stabilization of hundreds of client proteins in cooperation with a defined set of cofactors.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20940293-3	2010	To investigate the relationship between Hsp90 inhibition and cellular effects, we developed a method that measures drug occupancy on Hsp90 after treatment with the Hsp90 inhibitor IPI-504 in living cells and in tumor xenografts.	tanespimycin	180-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
20940293-3	2010	To investigate the relationship between Hsp90 inhibition and cellular effects, we developed a method that measures drug occupancy on Hsp90 after treatment with the Hsp90 inhibitor IPI-504 in living cells and in tumor xenografts.	tanespimycin	180-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
20940293-3	2010	To investigate the relationship between Hsp90 inhibition and cellular effects, we developed a method that measures drug occupancy on Hsp90 after treatment with the Hsp90 inhibitor IPI-504 in living cells and in tumor xenografts.	tanespimycin	180-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
20940293-6	2010	For sensitive Hsp90 clients (e.g. HER2 (human epidermal growth factor receptor 2), client protein levels directly mirror Hsp90 occupancy at all time points after IPI-504 administration.	tanespimycin	162-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20940293-6	2010	For sensitive Hsp90 clients (e.g. HER2 (human epidermal growth factor receptor 2), client protein levels directly mirror Hsp90 occupancy at all time points after IPI-504 administration.	tanespimycin	162-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
21074517-0	2010	Gambogic acid inhibits Hsp90 and deregulates TNF-alpha/NF-kappaB in HeLa cells.	gambogic acid	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
21074517-2	2010	This study is the first to show that GB inhibits heat shock protein 90 (Hsp90) and down-regulates TNF-alpha/NF-kappaB in HeLa cells.	gambogic acid	37-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-70
21074517-2	2010	This study is the first to show that GB inhibits heat shock protein 90 (Hsp90) and down-regulates TNF-alpha/NF-kappaB in HeLa cells.	gambogic acid	37-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
21074517-3	2010	The effects of GB on Hsp90 were studied by characterizing its physical interactions with Hsp90 upon binding, the noncompetitive inhibition of Hsp90 ATPase activity, and the degradation of Hsp90 client proteins (i.e., Akt, IKK) in HeLa cells.	gambogic acid	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
21074517-3	2010	The effects of GB on Hsp90 were studied by characterizing its physical interactions with Hsp90 upon binding, the noncompetitive inhibition of Hsp90 ATPase activity, and the degradation of Hsp90 client proteins (i.e., Akt, IKK) in HeLa cells.	gambogic acid	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
21074517-3	2010	The effects of GB on Hsp90 were studied by characterizing its physical interactions with Hsp90 upon binding, the noncompetitive inhibition of Hsp90 ATPase activity, and the degradation of Hsp90 client proteins (i.e., Akt, IKK) in HeLa cells.	gambogic acid	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
21074517-3	2010	The effects of GB on Hsp90 were studied by characterizing its physical interactions with Hsp90 upon binding, the noncompetitive inhibition of Hsp90 ATPase activity, and the degradation of Hsp90 client proteins (i.e., Akt, IKK) in HeLa cells.	gambogic acid	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
21074517-4	2010	GB seems to bind to the N-terminal ATP-binding domain of Hsp90.	gambogic acid	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
21074517-4	2010	GB seems to bind to the N-terminal ATP-binding domain of Hsp90.	Adenosine Triphosphate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
21074517-6	2010	Thus, GB represents a promising therapeutic agent for cancer; it may also be useful as a probe to increase understanding of the biological functions of Hsp90.	gambogic acid	6-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
21030459-5	2010	A chemically distinct ALK inhibitor, TAE684, and the HSP90 inhibitor 17-AAG are both effective in models harboring the F1174L ALK mutation.	tanespimycin	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
21106457-0	2010	N-aryl-benzimidazolones as novel small molecule HSP90 inhibitors.	n-aryl-benzimidazolones	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
21106457-1	2010	We describe the development of a novel series of N-aryl-benzimidazolone HSP90 inhibitors (9) targeting the N-terminal ATP-ase site.	n-aryl-benzimidazolone	49-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
20810927-4	2010	PS-induced acetylation of the heat shock protein (hsp) 90 reduced the chaperone association between CXCR4 and hsp90, directing CXCR4 to degradation by the 20S proteasome.	Panobinostat	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-57
20810927-4	2010	PS-induced acetylation of the heat shock protein (hsp) 90 reduced the chaperone association between CXCR4 and hsp90, directing CXCR4 to degradation by the 20S proteasome.	Panobinostat	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
21151603-8	2010	GlcN had only minor effects on the expression of Hsp90, Grp78, and transcription factor CHOP/GADD 153 markers of nonspecific stress in the endoplasmic reticulum.	Glucosamine	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
20937816-6	2010	Further investigation reveals that this stabilization effect is isoform-specific, ATP-independent, and mediated by the interaction between the Hsp90alpha middle domain and the MMP-2 C-terminal hemopexin domain.	Adenosine Triphosphate	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-153
21949862-4	2011	We show that NadA(Delta351-405) (against which we obtained polyclonal antibodies in rabbits), binds to hsp90, but not to other extracellular homologous heat shock proteins grp94 and hsp70, in vitro and on the surface of monocytes, in a temperature dependent way.	N-acetyldopamine	13-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
21949862-7	2011	Consistently, polymixin B interfered with NadA(Delta351-405) /hsp90 association, abrogated the decrease of anti-hsp90 antibodies binding to the cell surface due to NadA(Delta351-405) and inhibited adhesin-induced cytokine/chemokine secretion without affecting monocyte-adhesin binding.	N-acetyldopamine	164-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
21949862-10	2011	Finally, the activation of monocytes by NadA(Delta351-405) alone or in the presence of anti-hsp90 antibodies were both inhibited by neutralizing anti-TLR4 antibodies, but not by anti-TLR2 antibodies.	N-acetyldopamine	40-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
21949862-11	2011	We propose that hsp90-dependent recruitment into an hsp90/hsp70/TLR4 transducing signal complex is necessary for the immune-stimulating activity of NadA(Delta351-405) anti-MenB vaccine candidate.	N-acetyldopamine	148-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
20861078-4	2010	17-Allylamino-17-demethoxygeldanamycin (17-AAG) is a benzoquinone ansamycin antibiotic that binds to Hsp90 and alters its function.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
20861078-4	2010	17-Allylamino-17-demethoxygeldanamycin (17-AAG) is a benzoquinone ansamycin antibiotic that binds to Hsp90 and alters its function.	benzoquinone ansamycin	53-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
21154128-3	2010	STA-9090 binds to the ATP-binding domain at the N-terminus of Hsp90 and acts as a potent Hsp90 inhibitor by inducing degradation of multiple oncogenic Hsp90 client proteins including HER2/neu, mutated EGFR, Akt, c-Kit, IGF-1R, PDGFRalpha, Jak1, Jak2, STAT3, STAT5, HIF-1alpha, CDC2, c-Met, and Wilms" tumor 1.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
21949862-11	2011	We propose that hsp90-dependent recruitment into an hsp90/hsp70/TLR4 transducing signal complex is necessary for the immune-stimulating activity of NadA(Delta351-405) anti-MenB vaccine candidate.	N-acetyldopamine	148-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
20940188-0	2010	Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer.	tanespimycin	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-50
20940188-1	2010	PURPOSE: IPI-504 is a novel, water-soluble, potent inhibitor of heat-shock protein 90 (Hsp90).	tanespimycin	9-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
20940188-1	2010	PURPOSE: IPI-504 is a novel, water-soluble, potent inhibitor of heat-shock protein 90 (Hsp90).	tanespimycin	9-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
20940188-1	2010	PURPOSE: IPI-504 is a novel, water-soluble, potent inhibitor of heat-shock protein 90 (Hsp90).	Water	29-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
20940188-1	2010	PURPOSE: IPI-504 is a novel, water-soluble, potent inhibitor of heat-shock protein 90 (Hsp90).	Water	29-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
21092132-5	2010	Exposure of SP-CI73T cells to drugs currently used empirically in ILD therapy, cyclophosphamide, azathioprine, hydroxychloroquine or methylprednisolone, enhanced expression of the chaperones HSP90, HSP70, calreticulin and calnexin.	Hydroxychloroquine	111-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
20924358-5	2010	Upon mild oxidative stress, SENP3 undergoes thiol modification, which recruits Hsp90.	Sulfhydryl Compounds	44-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
21191765-0	2010	6-Alkylsalicylic acid analogues inhibit in vitro ATPase activity of heat shock protein 90.	6-alkylsalicylic acid	0-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
21191765-3	2010	In an effort to identify new Hsp90 inhibitors from natural sources using an in vitro ATPase inhibition assay, two 6-alkylsalicylic acid analogues, salaceyin A and B were identified from the culture extract of Streptomyces.	6-alkylsalicylic acid	114-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
21191765-3	2010	In an effort to identify new Hsp90 inhibitors from natural sources using an in vitro ATPase inhibition assay, two 6-alkylsalicylic acid analogues, salaceyin A and B were identified from the culture extract of Streptomyces.	salaceyin a and b	147-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
21191765-5	2010	Binding of salaceyins to human Hsp90alpha was examined by competition binding experiments with ATP-Sepharose beads.	Adenosine Triphosphate	95-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-41
21191765-5	2010	Binding of salaceyins to human Hsp90alpha was examined by competition binding experiments with ATP-Sepharose beads.	Sepharose	99-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-41
20951100-1	2010	A simple, rapid and sensitive liquid chromatography/tandem mass spectrometric (LC/MS/MS) analytical method was developed for quantification of Hsp90 inhibitor PF-04928473 in human plasma, following administration of its prodrug, PF-04929113.	pyrazofurin	159-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
20951100-1	2010	A simple, rapid and sensitive liquid chromatography/tandem mass spectrometric (LC/MS/MS) analytical method was developed for quantification of Hsp90 inhibitor PF-04928473 in human plasma, following administration of its prodrug, PF-04929113.	pyrazofurin	229-231	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
20943306-0	2010	Thermodynamics of radicicol binding to human Hsp90 alpha and beta isoforms.	monorden	18-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-56
20651072-7	2010	Furthermore, Hsp90 inhibitors 17-AAG [17-(allylamino)-17-demethoxygeldanamycin] and STA-9090 significantly reduced the growth of myeloid leukemia xenografts in vivo and effectively down-regulated the expression of WT1 and its downstream target proteins, c-Myc and Bcl-2.	tanespimycin	30-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
20651072-7	2010	Furthermore, Hsp90 inhibitors 17-AAG [17-(allylamino)-17-demethoxygeldanamycin] and STA-9090 significantly reduced the growth of myeloid leukemia xenografts in vivo and effectively down-regulated the expression of WT1 and its downstream target proteins, c-Myc and Bcl-2.	tanespimycin	38-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
20841485-4	2010	Both LATS1 and LATS2 were depleted from cells treated with the HSP90 inhibitors 17-allylamino-17-demethoxygeldanamycin (17-AAG), radicicol, and PU-H71.	tanespimycin	80-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
20841485-4	2010	Both LATS1 and LATS2 were depleted from cells treated with the HSP90 inhibitors 17-allylamino-17-demethoxygeldanamycin (17-AAG), radicicol, and PU-H71.	tanespimycin	120-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
20841485-4	2010	Both LATS1 and LATS2 were depleted from cells treated with the HSP90 inhibitors 17-allylamino-17-demethoxygeldanamycin (17-AAG), radicicol, and PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	144-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
20841485-5	2010	Moreover, these kinases interacted with HSP90, and LATS1 isolated from 17-AAG-treated cells had reduced catalytic activity, thus showing that the kinase is a bona fide HSP90 client.	tanespimycin	71-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
20841485-5	2010	Moreover, these kinases interacted with HSP90, and LATS1 isolated from 17-AAG-treated cells had reduced catalytic activity, thus showing that the kinase is a bona fide HSP90 client.	tanespimycin	71-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
20943306-1	2010	Radicicol is a natural antibiotic that specifically inhibits chaperone Hsp90 activity and binds to its active site with nanomolar affinity.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
20943306-3	2010	Here we present a detailed thermodynamic description of radicicol binding to human Hsp90 and yeast Hsc82 studied by isothermal titration calorimetry and thermal shift assay.	monorden	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20943306-8	2010	The intrinsic enthalpy of radicicol binding to Hsc82 was -46.7 kJ/mol, to Hsp90alpha -70.7 kJ/mol, and to Hsp90beta was -66.8 kJ/mol.	monorden	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-84
20925690-2	2010	The information obtained by molecular dynamics (MD) simulations is combined with NMR data to provide a cross-validated atomic resolution model of the complementary interactions of heat shock protein 90 with a peptidic (shepherdin) and a non-peptidic (5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside, AICAR) inhibitor, showing antiproliferative and proapoptotic activity in multiple tumor cell lines.	acadesine	251-305	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-201
20925690-4	2010	In 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside bound state, one conformation of those present in solution is selected, where imidazolic, H4 and H5 protons have a key role in defining a non-polar region contacting heat shock protein 90 surface.	acadesine	3-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-245
20692357-7	2010	Inhibition of Hsp90 function by geldanamycin derivatives and novobiocin elicited a pattern of HSF1 activation and BAG3 expression that was similar to PDTC.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20480272-0	2010	Celastrol regulates multiple nuclear transcription factors belonging to HSP90"s clients in a dose- and cell type-dependent way.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
20480272-1	2010	Celastrol, a novel HSP90 inhibitor, has recently attracted much attention due to its potential in multiple applications, such as anti-inflammation use, degenerative neuron disease relief, and tumor management.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
20480272-2	2010	At present, the studies in celastrol"s effects on HSP90"s clients have focused on the kinase sub-population, while another key sub-population, nuclear transcription factors (TFs), is not being well-explored.	celastrol	27-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
20480272-3	2010	In this study, we observe the effects of celastrol on 18 TFs (belonging to HSP90 clients) in three human cell lines: MCF-7 (breast cancer), HepG2 (hepatoma), and THP-1 (monocytic leukemia).	celastrol	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
20480272-6	2010	Celastrol"s capability to affect multiple TFs was consistent with its altering HSP90/TFs interactions and disrupting HSP90/Hop interaction, in addition to the reported damaging HSP90/Cdc37 interaction.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
20480272-6	2010	Celastrol"s capability to affect multiple TFs was consistent with its altering HSP90/TFs interactions and disrupting HSP90/Hop interaction, in addition to the reported damaging HSP90/Cdc37 interaction.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
20480272-6	2010	Celastrol"s capability to affect multiple TFs was consistent with its altering HSP90/TFs interactions and disrupting HSP90/Hop interaction, in addition to the reported damaging HSP90/Cdc37 interaction.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
20480272-7	2010	This work confirms, for the first time, that celastrol has broad effects on TFs belonging to HSP90"s clients, casts new light on understanding these reported actions, and suggests new possible applications for celastrol, such as diabetes management.	celastrol	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
20717760-8	2010	Exposing these cells to the Hsp90 inhibitor geldanamycin caused a rapid reduction of luciferase and kinase activities and depletion of detergent-soluble v-Src::luciferase fusion protein.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
20692357-9	2010	Cell treatment with PDTC increased significantly the level of Hsp90alpha thiol oxidation, a posttranslational modification known to inhibit its chaperone function.	Sulfhydryl Compounds	73-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-72
20667592-1	2010	The Hsp90 inhibitor 17DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) is currently undergoing clinical trials as an antitumor drug.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
20667592-1	2010	The Hsp90 inhibitor 17DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) is currently undergoing clinical trials as an antitumor drug.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	28-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
20980790-5	2010	An HSP90 inhibitor, geldanamycin (GA), significantly suppressed angiotensin II-induced [3H]leucine incorporation and atrial natriuretic factor expression in cardiac cells.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
20980790-5	2010	An HSP90 inhibitor, geldanamycin (GA), significantly suppressed angiotensin II-induced [3H]leucine incorporation and atrial natriuretic factor expression in cardiac cells.	geldanamycin	34-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
20980790-5	2010	An HSP90 inhibitor, geldanamycin (GA), significantly suppressed angiotensin II-induced [3H]leucine incorporation and atrial natriuretic factor expression in cardiac cells.	Tritium	88-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
20980790-5	2010	An HSP90 inhibitor, geldanamycin (GA), significantly suppressed angiotensin II-induced [3H]leucine incorporation and atrial natriuretic factor expression in cardiac cells.	Leucine	91-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
20980790-8	2010	We also found that GA prevented HSP90-IKKs complex induced by angiotensin II in cardiac cells.	geldanamycin	19-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
20688913-0	2010	ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
20688913-1	2010	Hsp90 is a ubiquitous, ATP-dependent chaperone, essential for eukaryotes.	Adenosine Triphosphate	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20688913-3	2010	Here, we elucidate the role of the adenine nucleotide in the Hsp90 chaperone cycle, by taking advantage of a unique in vitro assay measuring Hsp90-dependent p53 binding to the promoter sequence.	Adenine Nucleotides	35-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
20688913-3	2010	Here, we elucidate the role of the adenine nucleotide in the Hsp90 chaperone cycle, by taking advantage of a unique in vitro assay measuring Hsp90-dependent p53 binding to the promoter sequence.	Adenine Nucleotides	35-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
20688913-6	2010	Surprisingly, in the case of WT, but also E42A Hsp90beta, the presence of ATP stimulates dissociation of Hsp90-p53 complexes and results in p53 binding to the promoter sequence.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
20688913-9	2010	The ATP-dependent dissociation of p53-Hsp90 complex allows further folding of p53 protein to an active conformation, able to bind to the promoter sequence.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
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
20977755-0	2010	The anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1.	purine	37-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
20977755-0	2010	The anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1.	purine	37-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-108
20977755-0	2010	The anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
20977755-0	2010	The anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-108
20977755-3	2010	We evaluated the in vitro anti-tumor activity and mechanism of action of PU-H71, a novel purine scaffold HSP90 inhibitor in human multiple myeloma cell lines.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	73-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
20977755-11	2010	Our finding further suggests that PU-H71 and the geldanamycin analogues work in part by inhibiting the endoplasmic reticulum gp96 along with the cytosolic HSP90.	Plutonium	34-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
20977755-11	2010	Our finding further suggests that PU-H71 and the geldanamycin analogues work in part by inhibiting the endoplasmic reticulum gp96 along with the cytosolic HSP90.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
20667832-5	2010	Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20667832-5	2010	Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
20667832-5	2010	Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20667832-5	2010	Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
20667832-5	2010	Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.	geldanamycin	81-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20667832-5	2010	Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.	geldanamycin	81-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
20669973-2	2010	The purpose of this study is to evaluate the antitumor activity of MEK inhibitor U0126 in combination with Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) in pancreatic cancer cells.	tanespimycin	123-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
20669973-10	2010	Taken together, these data demonstrate that MEK inhibitor U0126 potentiates the activity of Hsp90 inhibitor 17-AAG against pancreatic cancer cells.	U 0126	58-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
20920318-2	2010	In fact, the HSP90 inhibitor, 17AAG, currently has entered in phase II clinical trials as an anticancer agent in breast and other tumors.	tanespimycin	30-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
20693398-2	2010	We tested the hypotheses that 1) the interaction between Hsp90 and its known client protein, endothelial nitric oxide synthase (eNOS), is impaired in pulmonary resistance arteries (PRAs) from piglets with pulmonary hypertension caused by exposure to 3 or 10 days of hypoxia and 2) Hsp90 interacts with the prostanoid pathway proteins prostacyclin synthase (PGIS) and/or thromboxane synthase (TXAS).	Prostaglandins	306-316	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
20693398-3	2010	We also determined whether Hsp90 antagonism with geldanamycin alters the agonist-induced synthesis of prostacyclin and thromboxane or alters PRA responses to these prostaglandin metabolites.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
20693398-5	2010	Despite reduced Hsp90-eNOS interactions, dilation to ACh was enhanced in geldanamycin-treated PRAs from hypoxic, but not normoxic, piglets.	geldanamycin	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
20693398-9	2010	Our findings indicate that Hsp90 influences both prostanoid and eNOS signaling in the pulmonary circulation of newborn piglets and that the impact of pharmacological inhibition of Hsp90 on these signaling pathways is altered during exposure to chronic hypoxia.	Prostaglandins	49-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
21061222-5	2010	It was observed that tephrosin induced ROS generation and Hsp90 expression inhibition.	tephrosin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
20738310-0	2010	The novel Hsp-90 inhibitor SNX7081 is significantly more potent  than 17-AAG against primary CLL cells and a range of  haematological cell lines, irrespective of lesions in the TP53  pathway.	SNX-7081	27-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-16
20738310-2	2010	We investigated the activity of a novel Hsp90 inhibitor, SNX7081, against a panel of eight haematological cell lines and 23 CLL patient samples.	SNX-7081	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
20626591-4	2010	Moreover, we have recently shown that melatonin stimulates production of two major anti-apoptotic heat shock proteins, HSP27 and HSP 90, in pancreatic carcinoma cells.	Melatonin	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-135
20635416-0	2010	Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.	Adenosine Triphosphate	17-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
20635416-2	2010	The Hsp90 protein from the parasite Plasmodium falciparum, the causative agent of malaria, is critical for this organism"s survival; the anti-Hsp90 drug geldanamycin is toxic to P. falciparum growth.	geldanamycin	153-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
20635416-2	2010	The Hsp90 protein from the parasite Plasmodium falciparum, the causative agent of malaria, is critical for this organism"s survival; the anti-Hsp90 drug geldanamycin is toxic to P. falciparum growth.	geldanamycin	153-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
20635416-3	2010	We have solved the structure of the N-terminal ATP-binding domain of P. falciparum Hsp90, which contains a principal drug-binding pocket, in both apo and ADP-bound states at 2.3 A resolution.	Adenosine Triphosphate	47-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20635416-3	2010	We have solved the structure of the N-terminal ATP-binding domain of P. falciparum Hsp90, which contains a principal drug-binding pocket, in both apo and ADP-bound states at 2.3 A resolution.	Adenosine Diphosphate	154-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20635416-4	2010	The structure shows that P. falciparum Hsp90 is highly similar to human Hsp90, and likely binds agents such as geldanamycin in an identical manner.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
20635416-4	2010	The structure shows that P. falciparum Hsp90 is highly similar to human Hsp90, and likely binds agents such as geldanamycin in an identical manner.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
20885985-7	2010	Data further shows that MGO decreases the levels of the molecular chaperones Hsc70 and Hsp90 and leads to accumulation of CHIP-, Hsp40- and ubiquitin-containing aggregates.	Pyruvaldehyde	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
20708938-0	2010	Design and synthesis of Hsp90 inhibitors: exploring the SAR of Sansalvamide A derivatives.	sansalvamide A	63-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
20708938-1	2010	Utilizing the structure-activity relationship we have developed during the synthesis of the first two generations and mechanism of action studies that point to the interaction of these molecules with the key oncogenic protein Hsp90, we report here the design of 32 new Sansalvamide A derivatives and their synthesis.	sansalvamide A	269-283	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
20828379-0	2010	17-Allylamino-17-demethoxygeldanamycin induces downregulation of critical Hsp90 protein clients and results in cell cycle arrest and apoptosis of human urinary bladder cancer cells.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
20828379-1	2010	BACKGROUND: 17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinone ansamycin antibiotic, specifically targets heat shock protein 90 (Hsp90) and interferes with its function as a molecular chaperone that maintains the structural and functional integrity of various protein clients involved in cellular signaling.	tanespimycin	12-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-140
20828379-1	2010	BACKGROUND: 17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinone ansamycin antibiotic, specifically targets heat shock protein 90 (Hsp90) and interferes with its function as a molecular chaperone that maintains the structural and functional integrity of various protein clients involved in cellular signaling.	tanespimycin	12-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
20828379-1	2010	BACKGROUND: 17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinone ansamycin antibiotic, specifically targets heat shock protein 90 (Hsp90) and interferes with its function as a molecular chaperone that maintains the structural and functional integrity of various protein clients involved in cellular signaling.	benzoquinone ansamycin	63-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-140
20828379-1	2010	BACKGROUND: 17-Allylamino-17-demethoxygeldanamycin (17-AAG), a benzoquinone ansamycin antibiotic, specifically targets heat shock protein 90 (Hsp90) and interferes with its function as a molecular chaperone that maintains the structural and functional integrity of various protein clients involved in cellular signaling.	benzoquinone ansamycin	63-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
20536386-7	2010	HK-PPK activation was inhibited by cysteine, BK and protamine, and by novobiocin, a heat shock protein 90 (HSP90) inhibitor.	Novobiocin	70-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-105
20536386-7	2010	HK-PPK activation was inhibited by cysteine, BK and protamine, and by novobiocin, a heat shock protein 90 (HSP90) inhibitor.	Novobiocin	70-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
20656483-2	2010	Disrupting the ability of ATP to bind and facilitate the operation of Hsp90 has emerged as a promising approach toward cancer chemotherapeutic development.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
20035426-2	2010	Arsenic trioxide (ATO) synergizes with the heat shock protein (HSP) 90 inhibitor, 17-DMAG, to down-regulate STAT3 activity.	Arsenic Trioxide	0-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-70
20035426-2	2010	Arsenic trioxide (ATO) synergizes with the heat shock protein (HSP) 90 inhibitor, 17-DMAG, to down-regulate STAT3 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	82-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-70
20043217-4	2010	We observed that endocytosis of transferrin, which is involved in the delivery of iron to the cell, was increased after stress induced by heat shock or after incubation with inhibitors of Hsp90 function.	Iron	82-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
19948165-6	2010	Radicicol and 17-allylamino-17-demethoxygeldanamycin (17-AAG) at non-cytotoxic doses targeted cell-surface HSP90 in OPCs.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
19948165-6	2010	Radicicol and 17-allylamino-17-demethoxygeldanamycin (17-AAG) at non-cytotoxic doses targeted cell-surface HSP90 in OPCs.	tanespimycin	14-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
19948165-7	2010	Thus, 0.01 nM 17-AAG or 10 nM radicicol competed with the anti-HSP90 antibodies for binding to cell-surface HSP90.	monorden	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19948165-7	2010	Thus, 0.01 nM 17-AAG or 10 nM radicicol competed with the anti-HSP90 antibodies for binding to cell-surface HSP90.	monorden	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
19948165-10	2010	The present results show that, despite OPCs being very sensitive to HSP90 inhibitors, low and non-cytotoxic doses of 17-AAG and radicicol protect oligodendrocytes from anti-HSP90 antibody attack.	monorden	128-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
20084478-6	2010	Cellular studies indicate that, similar to EGFR, the geldanamycin (GA) sensitivity of ERBB3 and HSP90 binding resides in the nascent state and is dependent on the presence of the kinase domain of ERBB3.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
20084478-6	2010	Cellular studies indicate that, similar to EGFR, the geldanamycin (GA) sensitivity of ERBB3 and HSP90 binding resides in the nascent state and is dependent on the presence of the kinase domain of ERBB3.	geldanamycin	67-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
20084478-8	2010	Geldanamycin disrupts the interaction of ERBB3 and HSP90 and inhibits ERBB3 maturation at an early stage of synthesis, prior to export from the ER.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
20084478-9	2010	Studies with a photo-convertible fusion protein of ERBB3 suggest geldanamycin sensitivity at a later stage in maturation, possibly through the putative role of HSP90 in structural proofreading.	geldanamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
20662534-0	2010	Discovery of (2,4-dihydroxy-5-isopropylphenyl)-[5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl]methanone (AT13387), a novel inhibitor of the molecular chaperone Hsp90 by fragment based drug design.	(2,4-dihydroxy-5-isopropylphenyl)-(5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl)methanone	117-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
20718493-6	2010	This fragment was optimized using structure based design into a resorcinol lead which has subnanomolar affinity for Hsp90, excellent cell potency, and good ligand efficiency.	resorcinol	64-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
20471294-8	2010	At the C2 position of the benzene ring, the HER2 model favored steric bulkier substitutes more than HSP90.	Benzene	26-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
20655237-0	2010	Natural and semisynthetic azaphilones as a new scaffold for Hsp90 inhibitors.	azaphilone	26-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
20655237-1	2010	A series of mold metabolites of Ascomycetes, structurally belonging to the class of azaphilones, were found to inhibit the heat shock protein Hsp90.	azaphilone	84-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
20655237-2	2010	In particular, bulgarialactone B was tested for its binding to Hsp90 using surface plasmon resonance and limited proteolysis assays and for its effects on Hsp90 client proteins expression in a series of human tumor cell lines.	bulgarialactone	15-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
20655237-2	2010	In particular, bulgarialactone B was tested for its binding to Hsp90 using surface plasmon resonance and limited proteolysis assays and for its effects on Hsp90 client proteins expression in a series of human tumor cell lines.	bulgarialactone	15-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
20655237-5	2010	Preliminary results indicated in vivo activity of bulgarialactone B against an ascitic ovarian carcinoma xenograft, thus supporting the therapeutic potential of this novel series of Hsp90 inhibitors.	BULGARIALACTONE B	50-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
20619278-0	2010	15-Hydroxyeicosatetraenoic acid (15-HETE) protects pulmonary artery smooth muscle cells against apoptosis via HSP90.	Eicosatetraenoic acid, 15-hydroxy-	0-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
20619278-0	2010	15-Hydroxyeicosatetraenoic acid (15-HETE) protects pulmonary artery smooth muscle cells against apoptosis via HSP90.	15-Hete	33-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
20619278-7	2010	SIGNIFICANCE: This study establishes the factor involved in 15-HETE-protecting PASMC from apoptosis and the regulation of HSP90 by 15-HETE may be an important mechanism underlying the treatment of pulmonary artery hypertension and provide a novel therapeutic target in future.	15-Hete	60-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
20619278-7	2010	SIGNIFICANCE: This study establishes the factor involved in 15-HETE-protecting PASMC from apoptosis and the regulation of HSP90 by 15-HETE may be an important mechanism underlying the treatment of pulmonary artery hypertension and provide a novel therapeutic target in future.	pasmc	79-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
20619278-7	2010	SIGNIFICANCE: This study establishes the factor involved in 15-HETE-protecting PASMC from apoptosis and the regulation of HSP90 by 15-HETE may be an important mechanism underlying the treatment of pulmonary artery hypertension and provide a novel therapeutic target in future.	15-Hete	131-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
20705236-3	2010	In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families.	Adenosine Triphosphate	69-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
20618337-1	2010	Tanespimycin, a heat shock protein 90 (HSP90) inhibitor, induces apoptosis in drug-sensitive and -resistant MM cell lines and in tumour cells from patients with relapsed MM.	tanespimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
20618337-1	2010	Tanespimycin, a heat shock protein 90 (HSP90) inhibitor, induces apoptosis in drug-sensitive and -resistant MM cell lines and in tumour cells from patients with relapsed MM.	tanespimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
20618338-1	2010	Tanespimycin (17-allylamino-17-demethoxygeldanamycin, 17-AAG) disrupts heat shock protein 90 (HSP90), a key molecular chaperone for signal transduction proteins critical to myeloma growth, survival and drug resistance.	tanespimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-92
20618338-1	2010	Tanespimycin (17-allylamino-17-demethoxygeldanamycin, 17-AAG) disrupts heat shock protein 90 (HSP90), a key molecular chaperone for signal transduction proteins critical to myeloma growth, survival and drug resistance.	tanespimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
20618338-1	2010	Tanespimycin (17-allylamino-17-demethoxygeldanamycin, 17-AAG) disrupts heat shock protein 90 (HSP90), a key molecular chaperone for signal transduction proteins critical to myeloma growth, survival and drug resistance.	tanespimycin	14-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-92
20618338-1	2010	Tanespimycin (17-allylamino-17-demethoxygeldanamycin, 17-AAG) disrupts heat shock protein 90 (HSP90), a key molecular chaperone for signal transduction proteins critical to myeloma growth, survival and drug resistance.	tanespimycin	14-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
20493187-2	2010	GA and its analogs, including 17-allylamino-demethoxy geldanamycin (17-AAG), are also known to block the function of a molecular chaperone, heat shock protein 90 (Hsp90).	17-allylamino-demethoxy geldanamycin	30-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
20493187-2	2010	GA and its analogs, including 17-allylamino-demethoxy geldanamycin (17-AAG), are also known to block the function of a molecular chaperone, heat shock protein 90 (Hsp90).	17-allylamino-demethoxy geldanamycin	30-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
20493187-2	2010	GA and its analogs, including 17-allylamino-demethoxy geldanamycin (17-AAG), are also known to block the function of a molecular chaperone, heat shock protein 90 (Hsp90).	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
20493187-2	2010	GA and its analogs, including 17-allylamino-demethoxy geldanamycin (17-AAG), are also known to block the function of a molecular chaperone, heat shock protein 90 (Hsp90).	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
20721818-2	2010	This conference report highlights selected presentations on Hsp90 inhibitors and Hsp70 inducers, such as KU-32 and KU-174 (University of Kansas); natural products in drug design, such as minnelide (University of Minnesota) and tylocrebrine; novel compounds from Merck for metabolic and cardiovascular diseases, such as MK-7725, a series of DDP4 inhibitors and KV1.5 ion channel antagonists; and the discovery of the VEGFR2 kinase inhibitor AMG-429 (Amgen Inc).	KU-32	105-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
20721818-2	2010	This conference report highlights selected presentations on Hsp90 inhibitors and Hsp70 inducers, such as KU-32 and KU-174 (University of Kansas); natural products in drug design, such as minnelide (University of Minnesota) and tylocrebrine; novel compounds from Merck for metabolic and cardiovascular diseases, such as MK-7725, a series of DDP4 inhibitors and KV1.5 ion channel antagonists; and the discovery of the VEGFR2 kinase inhibitor AMG-429 (Amgen Inc).	ku-174	115-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
20492351-4	2010	Heat shock protein 90 (HSP90) regulates nNOSalpha activity by facilitating heme insertion into the nNOSalpha monomer, resulting in increased NO production.	Heme	75-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
20492351-4	2010	Heat shock protein 90 (HSP90) regulates nNOSalpha activity by facilitating heme insertion into the nNOSalpha monomer, resulting in increased NO production.	Heme	75-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
20492351-6	2010	Here, we show in vitro that inhibition of HSP90 with geldanamycin increases nNOS mobility and induces formation of aggresome-like inclusions containing both nNOSalpha and nNOSbeta in primary cortical neurons.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
20663926-3	2010	In the present study, we show the chaperone association of TrkA with heat shock protein 90 (hsp90) and the inhibitory effect of the hsp90 inhibitor, 17-DMAG, on TrkA levels and signaling in cultured and primary myeloid leukemia cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	149-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
20670895-1	2010	Hsp90-mediated function of NLR receptors in plant and animal innate immunity depends on the cochaperone Sgt1 and, at least in plants, on a cysteine- and histidine-rich domains (CHORD)-containing protein Rar1.	Cysteine	139-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20670895-3	2010	Both CHORD and CS domains are independently capable of interacting with the molecular chaperone Hsp90 and can coexist in complexes with Hsp90.	Cesium	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
20670895-3	2010	Both CHORD and CS domains are independently capable of interacting with the molecular chaperone Hsp90 and can coexist in complexes with Hsp90.	Cesium	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
20668552-7	2010	The bcl-2-induced HIF-1alpha stabilization in response to low oxygen tension conditions was achieved through the impairment of ubiquitin-dependent HIF-1alpha degradation involving the molecular chaperone HSP90, but it was not dependent on the prolyl hydroxylation of HIF-1alpha protein.	Oxygen	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
20605501-0	2010	Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
20659681-5	2010	The approach, which also provides broad target selectivity information, was used to drive the identification of a potent and orally active Hsp90 inhibitor, SNX-5422, which is currently in phase 1 clinical studies.	SNX-5422	156-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
20540933-10	2010	We also found that hispolon induced increased association of Hsp70, Hsc70, Hsp90 and LAMP2A with MDM2.	hispolon	19-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
20540933-11	2010	This association was inhibited in cells pretreated with geldanamycin (GA), an Hsp90 inhibitor.	geldanamycin	56-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
20540933-11	2010	This association was inhibited in cells pretreated with geldanamycin (GA), an Hsp90 inhibitor.	geldanamycin	70-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
20525756-1	2010	PURPOSE: Heat shock protein (Hsp) 90 inhibition affects the Raf kinase signaling pathway and could enhance antitumor effects of sorafenib, a Raf kinase inhibitor.	Sorafenib	128-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-36
20616224-1	2010	In this issue of Blood, Hertlein and colleagues present compelling in vitro and in vivo evidence that the novel HSP90 inhibitor 17-DMAG is a potent and selective killer of CLL cells that mediates its effects through the targeted inhibition of NF-B.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	128-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
20570149-0	2010	Click chemistry to probe Hsp90: Synthesis and evaluation of a series of triazole-containing novobiocin analogues.	Triazoles	72-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
20570149-0	2010	Click chemistry to probe Hsp90: Synthesis and evaluation of a series of triazole-containing novobiocin analogues.	Novobiocin	92-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
20394503-0	2010	Geldanamycin-induced PCNA degradation in isolated Hsp90 complex from cancer cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
20394503-3	2010	An Hsp90-specific inhibitor, geldanamycin, is shown to bind to the ATP binding site of the chaperone to induce degradation of many client proteins, and results in antitumor activities.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
20394503-3	2010	An Hsp90-specific inhibitor, geldanamycin, is shown to bind to the ATP binding site of the chaperone to induce degradation of many client proteins, and results in antitumor activities.	Adenosine Triphosphate	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	3-8
20394503-7	2010	After geldanamycin treatment, both PCNA and Hsp90 were shown to be degraded.	geldanamycin	6-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
20444924-3	2010	HSP90 is specifically inhibited by 17-allyl-amino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	35-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20444924-3	2010	HSP90 is specifically inhibited by 17-allyl-amino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20444924-4	2010	OBJECTIVE: Our aim was to investigate whether RET protein half-life depends on HSP90 and to dissect the molecular pathway responsible for the degradation of RET upon HSP90 inhibition by 17-AAG.	tanespimycin	186-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
20444924-11	2010	CONCLUSION: RET and MEN2-associated RET mutants rely on HSP90 for protein stability, and HSP90 blockade by 17-AAG promotes RET degradation.	tanespimycin	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
20219895-6	2010	In the HepG2 cell, geldanamycin (GA), an HSP90-specific inhibitor, blocked intracellular transportation of p239, but had no effect on the binding and cellular entry of p239, suggesting that HSP90 was important for HEV capsid intracellular transportation.	geldanamycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
20219895-6	2010	In the HepG2 cell, geldanamycin (GA), an HSP90-specific inhibitor, blocked intracellular transportation of p239, but had no effect on the binding and cellular entry of p239, suggesting that HSP90 was important for HEV capsid intracellular transportation.	geldanamycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
20219895-6	2010	In the HepG2 cell, geldanamycin (GA), an HSP90-specific inhibitor, blocked intracellular transportation of p239, but had no effect on the binding and cellular entry of p239, suggesting that HSP90 was important for HEV capsid intracellular transportation.	geldanamycin	33-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
20219895-6	2010	In the HepG2 cell, geldanamycin (GA), an HSP90-specific inhibitor, blocked intracellular transportation of p239, but had no effect on the binding and cellular entry of p239, suggesting that HSP90 was important for HEV capsid intracellular transportation.	geldanamycin	33-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	190-195
20219895-7	2010	RT-PCR results showed that the efficiency of wild-type HEV infection was inhibited significantly by GA treatment, suggesting the importance of HSP90 in virus infectivity.	geldanamycin	100-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
20138989-4	2010	Geldanamycin (GA), an Hsp90 inhibitor, is able to suppress 1,25-induced differentiation of HL60 cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
20138989-4	2010	Geldanamycin (GA), an Hsp90 inhibitor, is able to suppress 1,25-induced differentiation of HL60 cells.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
21037799-0	2010	Modulation of melanoma cell phospholipid metabolism in response to heat shock protein 90 inhibition.	Phospholipids	28-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-88
21037799-4	2010	We show that, concomitant with growth inhibition and re-differentiation, Hsp90 inhibition in human melanoma cells is associated with increased glycerophosphocholine content.	Glycerylphosphorylcholine	143-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
21037799-5	2010	This was seen with both the clinical geldanamycin-based Hsp90 drug 17-AAG and the structurally dissimilar Hsp90 inhibitor CCT018159.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
21037799-5	2010	This was seen with both the clinical geldanamycin-based Hsp90 drug 17-AAG and the structurally dissimilar Hsp90 inhibitor CCT018159.	tanespimycin	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
21037799-5	2010	This was seen with both the clinical geldanamycin-based Hsp90 drug 17-AAG and the structurally dissimilar Hsp90 inhibitor CCT018159.	CCT018159	122-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
21037799-8	2010	Importantly, the phospholipase A2 inhibitor bromoenol lactone prevented the rise in glycerophosphocholine seen with 17-AAG, suggesting a role for phospholipase A2 activation in the Hsp90 inhibitor-induced metabolic response.	6-(bromomethylene)tetrahydro-3-(1-naphthaleneyl)-2H-pyran-2-one	44-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
21037799-8	2010	Importantly, the phospholipase A2 inhibitor bromoenol lactone prevented the rise in glycerophosphocholine seen with 17-AAG, suggesting a role for phospholipase A2 activation in the Hsp90 inhibitor-induced metabolic response.	Glycerylphosphorylcholine	84-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
21037799-8	2010	Importantly, the phospholipase A2 inhibitor bromoenol lactone prevented the rise in glycerophosphocholine seen with 17-AAG, suggesting a role for phospholipase A2 activation in the Hsp90 inhibitor-induced metabolic response.	tanespimycin	116-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
20818581-2	2010	To identify important chemical features for Hsp90 inhibitory activity, a 3D-QSAR pharmacophore model was developed using a set of 61 inhibitors (a training set of 31 and a test set of 30 compounds) belonging to a series of 2-amino-6-halopurine and 7"-substituted benzothiazolothio- and pyridinothiazolothio-purines.	2-amino-6-halopurine	223-243	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
20418907-11	2010	Finally, we report that the Hsp90 inhibitors, 17-AAG and 17-DMAG, can suppress the proliferation of KSHV-positive PEL cell lines and exhibited IC(50) values of 50 nM and below.	tanespimycin	46-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
20418907-11	2010	Finally, we report that the Hsp90 inhibitors, 17-AAG and 17-DMAG, can suppress the proliferation of KSHV-positive PEL cell lines and exhibited IC(50) values of 50 nM and below.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
20427569-6	2010	Pharmacologic inhibition of Hsp90 function by geldanamycin reduces, whereas overexpression of Hsp90 increases surface expression of wild-type K(ATP) channels.	geldanamycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
20550649-0	2010	The new platinum(IV) derivative LA-12 shows stronger inhibitory effect on Hsp90 function compared to cisplatin.	UNII-37WM0V5E17	32-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
20550649-5	2010	Similarly to cisplatin, an interaction of LA-12 with molecular chaperone Hsp90 was proposed.	UNII-37WM0V5E17	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
20550649-6	2010	Binding of LA-12 to Hsp90 was demonstrated by Hsp90 immunoprecipitation followed by platinum measurement using atomic absorption spectrometry (AAS).	UNII-37WM0V5E17	11-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
20550649-6	2010	Binding of LA-12 to Hsp90 was demonstrated by Hsp90 immunoprecipitation followed by platinum measurement using atomic absorption spectrometry (AAS).	UNII-37WM0V5E17	11-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
20550649-6	2010	Binding of LA-12 to Hsp90 was demonstrated by Hsp90 immunoprecipitation followed by platinum measurement using atomic absorption spectrometry (AAS).	Platinum	84-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
20550649-7	2010	An inhibitory effect of LA-12 on Hsp90 chaperoning function was shown by decrease of Hsp90-assisted wild-type p53 binding to p21WAF1 promoter sequence in vitro and by accelerated ubiqutination and degradation of primarily unfolded mutant p53 proteins in cells exposed to LA-12.	UNII-37WM0V5E17	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
20550649-7	2010	An inhibitory effect of LA-12 on Hsp90 chaperoning function was shown by decrease of Hsp90-assisted wild-type p53 binding to p21WAF1 promoter sequence in vitro and by accelerated ubiqutination and degradation of primarily unfolded mutant p53 proteins in cells exposed to LA-12.	UNII-37WM0V5E17	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
20550649-7	2010	An inhibitory effect of LA-12 on Hsp90 chaperoning function was shown by decrease of Hsp90-assisted wild-type p53 binding to p21WAF1 promoter sequence in vitro and by accelerated ubiqutination and degradation of primarily unfolded mutant p53 proteins in cells exposed to LA-12.	UNII-37WM0V5E17	271-276	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
20550649-7	2010	An inhibitory effect of LA-12 on Hsp90 chaperoning function was shown by decrease of Hsp90-assisted wild-type p53 binding to p21WAF1 promoter sequence in vitro and by accelerated ubiqutination and degradation of primarily unfolded mutant p53 proteins in cells exposed to LA-12.	UNII-37WM0V5E17	271-276	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
20550649-8	2010	CONCLUSIONS: To generalize our findings, LA-12 induced degradation of other Hsp90 client proteins such as Cyclin D1 and estrogen receptor was shown and proved as more efficient in comparison with cisplatin.	UNII-37WM0V5E17	41-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
20550649-9	2010	This newly characterised molecular mechanism of action opens opportunities to design new cancer treatment strategy profitable from unique LA-12 properties, which combine DNA damaging and Hsp90 inhibitory effects.	UNII-37WM0V5E17	138-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	187-192
20559560-4	2010	The assay was originally developed to identify inhibitors of Hsp90 in tumor cells, and relies upon the ability of small molecules to inhibit the binding of fluorescently labelled geldanamycin to Hsp90.	geldanamycin	179-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
20559560-4	2010	The assay was originally developed to identify inhibitors of Hsp90 in tumor cells, and relies upon the ability of small molecules to inhibit the binding of fluorescently labelled geldanamycin to Hsp90.	geldanamycin	179-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	195-200
20559560-6	2010	The assay was validated using known inhibitors of Hsp90 that compete with geldanamycin for binding to Hsp90, including members of the synthetic purine-scaffold series of compounds.	geldanamycin	74-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
20559560-6	2010	The assay was validated using known inhibitors of Hsp90 that compete with geldanamycin for binding to Hsp90, including members of the synthetic purine-scaffold series of compounds.	geldanamycin	74-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
20559560-6	2010	The assay was validated using known inhibitors of Hsp90 that compete with geldanamycin for binding to Hsp90, including members of the synthetic purine-scaffold series of compounds.	purine	144-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
20559560-6	2010	The assay was validated using known inhibitors of Hsp90 that compete with geldanamycin for binding to Hsp90, including members of the synthetic purine-scaffold series of compounds.	purine	144-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
20413784-8	2010	Promotion of CHIP function by heat shock protein (Hsp)90 inhibitor, 17-allylamino-17-demethoxy geldanamycin (17-AAG), also prevented p53 accumulation and cardiomyocyte apoptosis both in vitro and in vivo.	tanespimycin	68-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-56
20413784-8	2010	Promotion of CHIP function by heat shock protein (Hsp)90 inhibitor, 17-allylamino-17-demethoxy geldanamycin (17-AAG), also prevented p53 accumulation and cardiomyocyte apoptosis both in vitro and in vivo.	tanespimycin	109-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-56
20537126-0	2010	Epigallocatechin-3-gallate suppresses the expression of HSP70 and HSP90 and exhibits anti-tumor activity in vitro and in vivo.	epigallocatechin gallate	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
20537126-8	2010	EGCG specifically inhibited the expression of HSP70 and HSP90 by inhibiting the promoter activity of HSP70 and HSP90.	epigallocatechin gallate	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
20537126-8	2010	EGCG specifically inhibited the expression of HSP70 and HSP90 by inhibiting the promoter activity of HSP70 and HSP90.	epigallocatechin gallate	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
20537126-10	2010	Moreover, treatment with EGCG (10 mg/kg) in a xenograft model resulted in delayed tumor incidence and reduced tumor size, as well as the inhibition of HSP70 and HSP90 expression.	epigallocatechin gallate	25-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
20537126-11	2010	CONCLUSIONS: Overall, these findings demonstrate that HSP70 and HSP90 are potent molecular targets of EGCG and suggest EGCG as a drug candidate for the treatment of human cancer.	epigallocatechin gallate	102-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
20552022-5	2010	METHODOLOGY/PRINCIPAL FINDINGS: In MTT assays, small cell lung cancer cells showed a biphasic response to the Hsp90 inhibitors geldanamycin and radicicol, with low concentrations causing proliferation arrest and high concentrations causing cell death.	monooxyethylene trimethylolpropane tristearate	35-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
20552022-5	2010	METHODOLOGY/PRINCIPAL FINDINGS: In MTT assays, small cell lung cancer cells showed a biphasic response to the Hsp90 inhibitors geldanamycin and radicicol, with low concentrations causing proliferation arrest and high concentrations causing cell death.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
20552022-5	2010	METHODOLOGY/PRINCIPAL FINDINGS: In MTT assays, small cell lung cancer cells showed a biphasic response to the Hsp90 inhibitors geldanamycin and radicicol, with low concentrations causing proliferation arrest and high concentrations causing cell death.	monorden	144-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
20552022-6	2010	Assessment of Hsp90 intracellular activity using loss of client protein expression showed that geldanamycin concentrations that inhibited Hsp90 correlated closely with those causing proliferation arrest but not cell death.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20552022-6	2010	Assessment of Hsp90 intracellular activity using loss of client protein expression showed that geldanamycin concentrations that inhibited Hsp90 correlated closely with those causing proliferation arrest but not cell death.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
20138026-8	2010	We have used this strain to demonstrate that significant levels of resistance to the Hsp90 inhibitors radicicol and 17-allylamino-demethoxygeldanamycin (17-AAG) are generated as a result of the same single point mutation within the native Hsp90 of yeast (A107N), the human Hsp90alpha (A121N) and the human Hsp90beta (A116N).	monorden	102-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	273-283
20138026-8	2010	We have used this strain to demonstrate that significant levels of resistance to the Hsp90 inhibitors radicicol and 17-allylamino-demethoxygeldanamycin (17-AAG) are generated as a result of the same single point mutation within the native Hsp90 of yeast (A107N), the human Hsp90alpha (A121N) and the human Hsp90beta (A116N).	17-allylamino-demethoxygeldanamycin	116-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	273-283
20138026-8	2010	We have used this strain to demonstrate that significant levels of resistance to the Hsp90 inhibitors radicicol and 17-allylamino-demethoxygeldanamycin (17-AAG) are generated as a result of the same single point mutation within the native Hsp90 of yeast (A107N), the human Hsp90alpha (A121N) and the human Hsp90beta (A116N).	tanespimycin	153-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	273-283
20068362-9	2010	Dex increased cardiac oxidative stress (protein expression: 4-HNE +20%, Hsp90 -42% and eNOS -54%), induced left ventricle (LV) wall thinning (LV wall volume: Ctrl: 47.2 +/- 1.2 mm(3) vs. Dex: 38.9 +/- 1.7 mm(3)) and decreased the ratio of the aortic lumen:total vessel area (Ctrl: 0.74 +/- 0.01 vs. Dex: 0.66 +/- 0.02), all p &lt; 0.05.	Dexamethasone	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
20068362-10	2010	DexCE restored towards control values survival, growth symmetry the aortic lumen:total vessel area, and increased the cardiac expression of Hsp90 relative to Dex.	dexce	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
20068362-10	2010	DexCE restored towards control values survival, growth symmetry the aortic lumen:total vessel area, and increased the cardiac expression of Hsp90 relative to Dex.	Dexamethasone	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
20428801-3	2010	HSP90 proteins are ATP-dependent chaperones and the binding and hydrolysis of ATP are coupled to conformation changes of HSP90, which facilitate client protein folding and maturation.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20428801-3	2010	HSP90 proteins are ATP-dependent chaperones and the binding and hydrolysis of ATP are coupled to conformation changes of HSP90, which facilitate client protein folding and maturation.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
20428801-3	2010	HSP90 proteins are ATP-dependent chaperones and the binding and hydrolysis of ATP are coupled to conformation changes of HSP90, which facilitate client protein folding and maturation.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20428801-3	2010	HSP90 proteins are ATP-dependent chaperones and the binding and hydrolysis of ATP are coupled to conformation changes of HSP90, which facilitate client protein folding and maturation.	Adenosine Triphosphate	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
20428801-4	2010	Many natural and synthetic molecular compounds have been proposed as promising cancer therapy via disrupting the formation of complex ATP-HSP90-client proteins.	Adenosine Triphosphate	134-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
20534344-3	2010	Unique proteome patterns were observed in HeLa cells treated with the HSP90 inhibitor geldanamycin, and were similar to the patterns induced by radicicol, a structurally different HSP90 inhibitor.	geldanamycin	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
20534344-3	2010	Unique proteome patterns were observed in HeLa cells treated with the HSP90 inhibitor geldanamycin, and were similar to the patterns induced by radicicol, a structurally different HSP90 inhibitor.	geldanamycin	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
20534344-3	2010	Unique proteome patterns were observed in HeLa cells treated with the HSP90 inhibitor geldanamycin, and were similar to the patterns induced by radicicol, a structurally different HSP90 inhibitor.	monorden	144-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
20534344-3	2010	Unique proteome patterns were observed in HeLa cells treated with the HSP90 inhibitor geldanamycin, and were similar to the patterns induced by radicicol, a structurally different HSP90 inhibitor.	monorden	144-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	180-185
20348093-5	2010	First, we demonstrate that methylene blue inhibits the ability of the purified Hsp90/Hsp70-based chaperone machinery to enable ligand binding by the glucocorticoid receptor and show that this effect is due to specific inhibition of Hsp70.	Methylene Blue	27-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
20348093-7	2010	Finally, we demonstrate that methylene blue impairs degradation of the polyglutamine expanded androgen receptor, an Hsp90 client mutated in spinal and bulbar muscular atrophy.	Methylene Blue	29-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
20406843-0	2010	New molecular and biological mechanism of antitumor activities of KW-2478, a novel nonansamycin heat shock protein 90 inhibitor, in multiple myeloma cells.	KW-2478	66-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-117
20406843-3	2010	EXPERIMENTAL DESIGN: We evaluated the antitumor activities of KW-2478, a nonansamycin Hsp90 inhibitor, in MM cells with various chromosomal translocations of immunoglobulin heavy chain (IgH) loci both in vitro and in vivo.	KW-2478	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
20349996-3	2010	A robotic high throughput screen (HTS) was performed using 4000 small molecules from a natural compound (Spectrum), pharmacologically active (Lopac), and Food and Drug Administration (FDA) approved drug library (Prestwick) for competitive inhibition of the ATP-binding (GHKL) domain of Plasmodium falciparum (Pf) Hsp90, a highly conserved chaperone.	Adenosine Triphosphate	257-260	heat shock protein 90 alpha family class A member 1	Homo sapiens	313-318
20149843-0	2010	Hydrogen sulfide protects neurons against hypoxic injury via stimulation of ATP-sensitive potassium channel/protein kinase C/extracellular signal-regulated kinase/heat shock protein 90 pathway.	Hydrogen Sulfide	0-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-184
20149843-8	2010	Western blots showed that NaHS significantly stimulated ERK1/2 activation and Hsp90 expression.	sodium bisulfide	26-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
20149843-9	2010	In conclusion, H(2)S exerts a protective effect against cerebral hypoxia induced neuronal cell death via K(ATP)/PKC/ERK1/2/Hsp90 pathway.	Hydrogen Sulfide	15-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
20149843-9	2010	In conclusion, H(2)S exerts a protective effect against cerebral hypoxia induced neuronal cell death via K(ATP)/PKC/ERK1/2/Hsp90 pathway.	Adenosine Triphosphate	107-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
20154064-2	2010	HSP90 inhibitors [17-allylamino-17-demethoxygeldamycin (17-AAG)/17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride (17-DMAG)] bind to and inactivate HSP90, increasing the heat shock response and suppressing different signalling pathways.	17-allylamino-17-demethoxygeldamycin	18-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20154064-2	2010	HSP90 inhibitors [17-allylamino-17-demethoxygeldamycin (17-AAG)/17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride (17-DMAG)] bind to and inactivate HSP90, increasing the heat shock response and suppressing different signalling pathways.	17-allylamino-17-demethoxygeldamycin	18-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
20154064-2	2010	HSP90 inhibitors [17-allylamino-17-demethoxygeldamycin (17-AAG)/17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride (17-DMAG)] bind to and inactivate HSP90, increasing the heat shock response and suppressing different signalling pathways.	tanespimycin	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20154064-2	2010	HSP90 inhibitors [17-allylamino-17-demethoxygeldamycin (17-AAG)/17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride (17-DMAG)] bind to and inactivate HSP90, increasing the heat shock response and suppressing different signalling pathways.	17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride	64-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20154064-2	2010	HSP90 inhibitors [17-allylamino-17-demethoxygeldamycin (17-AAG)/17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride (17-DMAG)] bind to and inactivate HSP90, increasing the heat shock response and suppressing different signalling pathways.	17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride	64-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
20154064-2	2010	HSP90 inhibitors [17-allylamino-17-demethoxygeldamycin (17-AAG)/17-dimethyl aminothylamino-17-demethoxygeldanamycin hydrochloride (17-DMAG)] bind to and inactivate HSP90, increasing the heat shock response and suppressing different signalling pathways.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	131-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20546334-10	2010	CONCLUSIONS: Overexpression of HSP90 is predictive of adverse behaviour in GISTs and may provide a therapeutic solution to the challenge of imatinib-resistant GISTs and other mesenchymal sarcomas.	Imatinib Mesylate	140-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
20395337-5	2010	The aim of this study was to investigate (89)Zr-bevacizumab PET for early antiangiogenic tumor response evaluation of treatment with the new HSP90 inhibitor NVP-AUY922.	Zirconium	45-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
20237157-3	2010	Here we have shown that geldanamycin, a well-characterized HSP90 inhibitor, abolishes P-bodies and significantly reduces Argonaute and GW182 protein levels but does not affect the miRNA level and the efficiency of miRNA-mediated gene repression; however, it significantly impairs siRNA loading and the efficacy of exogenous siRNA.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
20457619-0	2010	Mechanistic evaluation of the novel HSP90 inhibitor NVP-AUY922 in adult and pediatric glioblastoma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
20457619-3	2010	Here, we explored the mechanistic potential of the potent synthetic diarylisoxazole amide resorcinol HSP90 inhibitor, NVP-AUY922, in adult and pediatric GB.	diarylisoxazole amide resorcinol	68-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
20416086-0	2010	Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin inhibits the proliferation of ARPE-19 cells.	tanespimycin	16-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20416086-1	2010	BACKGROUND: The antiproliferative effect of the Hsp90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) on human retinal pigment epithelial cells is investigated.	tanespimycin	64-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
20416086-1	2010	BACKGROUND: The antiproliferative effect of the Hsp90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) on human retinal pigment epithelial cells is investigated.	tanespimycin	72-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
20416086-9	2010	Real-time PCR results indicated that Hsp90 and Hsp70, which were not identified by proteomic analysis, were both upregulated upon 17-AAG treatment.	tanespimycin	130-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
20159978-5	2010	Experimental manipulation of Hsp90 function by the inhibitor novobiocin, but not 17-AAG, results in redistribution of AF9 from a primarily nuclear to cytoplasmic location.	Novobiocin	61-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
20159978-6	2010	Knockdown of Hsp90 with siRNA mimics the effect elicited by novobiocin.	Novobiocin	60-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
20398364-0	2010	HSP90 inhibitor, celastrol, arrests human monocytic leukemia cell U937 at G0/G1 in thiol-containing agents reversible way.	celastrol	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20398364-0	2010	HSP90 inhibitor, celastrol, arrests human monocytic leukemia cell U937 at G0/G1 in thiol-containing agents reversible way.	Sulfhydryl Compounds	83-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20398364-2	2010	Recently, celastrol is identified both as a novel inhibitor of HSP90 and as a potential anti-tumor agent.	celastrol	10-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
20398364-8	2010	CONCLUSIONS: Our results disclose a novel action of celastrol-- causing cell cycle arrest at G0/G1 phase based upon thiol-related HSP90 inhibition.	celastrol	52-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
20398364-8	2010	CONCLUSIONS: Our results disclose a novel action of celastrol-- causing cell cycle arrest at G0/G1 phase based upon thiol-related HSP90 inhibition.	Sulfhydryl Compounds	116-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
20398291-3	2010	Since the molecular chaperone Hsp90 binds and stabilizes survivin, it is widely believed that down-regulation of survivin is one of the important therapeutic functions of Hsp90 inhibitors such as the phase III clinically trialed compound 17-AAG.	tanespimycin	238-244	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
20398291-3	2010	Since the molecular chaperone Hsp90 binds and stabilizes survivin, it is widely believed that down-regulation of survivin is one of the important therapeutic functions of Hsp90 inhibitors such as the phase III clinically trialed compound 17-AAG.	tanespimycin	238-244	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
20398291-6	2010	RESULTS: Here, we demonstrated that Hsp90 inhibitors, geldanamycin and 17-AAG, induced the over-expression of survivin in three different human cancer cell lines as shown by Western blotting.	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
20398291-6	2010	RESULTS: Here, we demonstrated that Hsp90 inhibitors, geldanamycin and 17-AAG, induced the over-expression of survivin in three different human cancer cell lines as shown by Western blotting.	tanespimycin	71-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
20226165-4	2010	Celastrol (i) inhibits directly the IKKalpha and beta kinases, (ii) inactivates the Cdc37 and p23 proteins which are co-chaperones of HSP90, (iii) inhibits the function of proteasomes, and (iv) activates the HSF1 and subsequently triggers the heat shock response.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
19751963-0	2010	Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT.	Curcumin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
19751963-7	2010	In contrast, the treatment of the Hsp90 inhibitor geldanamycin promotes dissociation of both Hsp90 and p23 proteins from hTERT.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19751963-7	2010	In contrast, the treatment of the Hsp90 inhibitor geldanamycin promotes dissociation of both Hsp90 and p23 proteins from hTERT.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
19850405-1	2010	Geldanamycin is a benzoquinone ansamycin antibiotic that manifests anti-cancer activity through the inhibition of HSP90-chaperone function.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
19850405-1	2010	Geldanamycin is a benzoquinone ansamycin antibiotic that manifests anti-cancer activity through the inhibition of HSP90-chaperone function.	benzoquinone ansamycin	18-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
20423228-2	2010	In this work, the binding property of 17-allylamino-17-demethoxygeldanamycin (17-AAG), an HSP90 inhibitor now in phase II clinical trials, was used by labeling with radioisotope iodine-131 ((131)I), to observe the potential therapeutic effects on nonsmall-cell lung carcinoma (NSCLC) xenografts.	tanespimycin	38-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
20423228-2	2010	In this work, the binding property of 17-allylamino-17-demethoxygeldanamycin (17-AAG), an HSP90 inhibitor now in phase II clinical trials, was used by labeling with radioisotope iodine-131 ((131)I), to observe the potential therapeutic effects on nonsmall-cell lung carcinoma (NSCLC) xenografts.	Iodine-131	178-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
20028416-0	2010	Synergistic action of the novel HSP90 inhibitor NVP-AUY922 with histone deacetylase inhibitors, melphalan, or doxorubicin in multiple myeloma.	Doxorubicin	110-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
20028416-9	2010	These data show impressive synergistic action of the novel HSP90 inhibitor NVP-AUY922 with melphalan, doxorubicin, NVP-LBH589, and SAHA in multiple myeloma and build the frame work for clinical trials.	Melphalan	91-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
20028416-9	2010	These data show impressive synergistic action of the novel HSP90 inhibitor NVP-AUY922 with melphalan, doxorubicin, NVP-LBH589, and SAHA in multiple myeloma and build the frame work for clinical trials.	Doxorubicin	102-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
20028416-9	2010	These data show impressive synergistic action of the novel HSP90 inhibitor NVP-AUY922 with melphalan, doxorubicin, NVP-LBH589, and SAHA in multiple myeloma and build the frame work for clinical trials.	Panobinostat	119-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
20028416-9	2010	These data show impressive synergistic action of the novel HSP90 inhibitor NVP-AUY922 with melphalan, doxorubicin, NVP-LBH589, and SAHA in multiple myeloma and build the frame work for clinical trials.	Vorinostat	131-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
21083459-5	2010	The current study demonstrates that HSP90 forms a complex with BCL6, and inhibition of HSP90 with the drug PU-H71 selectively kills BCL6-positive DLBCL in animal models.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
21083459-5	2010	The current study demonstrates that HSP90 forms a complex with BCL6, and inhibition of HSP90 with the drug PU-H71 selectively kills BCL6-positive DLBCL in animal models.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	107-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
20521618-0	2010	Hsp90 mediates activation of the heme regulated eIF-2 alpha kinase during oxidative stress.	Heme	33-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20521618-5	2010	The results indicate a significant increase in both Hsp70 and Hsp90 expression during AAPH (2,2"-azobis (2-amidinopropane) dihydrochloride)-induced oxidative stress.	2,2'-azobis(2-amidinopropane)	92-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
20111068-0	2010	Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-42
20111068-2	2010	The small-molecule Hsp90 inhibitor alvespimycin, a geldanamycin derivative, is being developed for various malignancies.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
20111068-2	2010	The small-molecule Hsp90 inhibitor alvespimycin, a geldanamycin derivative, is being developed for various malignancies.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19540014-4	2010	Stress and heat shock proteins such as HSP90, HSP70 and HSP27 are induced in response to a wide variety of physiological environmental insults including heat, reactive oxygen species or anticancer drugs.	Reactive Oxygen Species	159-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
20371713-3	2010	NVP-BEP800 is a novel, fully synthetic, orally bioavailable inhibitor that binds to the NH(2)-terminal ATP-binding pocket of Hsp90.	Adenosine Triphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
20376192-0	2010	Tamoxifen enhances the Hsp90 molecular chaperone ATPase activity.	Tamoxifen	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
20376192-3	2010	METHODOLOGY/PRINCIPAL FINDINGS: Using a virtual screening approach, 4-hydroxytamoxifen, the active metabolite of the anti-estrogen drug tamoxifen, was identified as a putative Hsp90 ligand.	hydroxytamoxifen	68-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
20376192-3	2010	METHODOLOGY/PRINCIPAL FINDINGS: Using a virtual screening approach, 4-hydroxytamoxifen, the active metabolite of the anti-estrogen drug tamoxifen, was identified as a putative Hsp90 ligand.	Tamoxifen	77-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
20376192-4	2010	Surprisingly, while all drugs targeting Hsp90 inhibit the chaperone ATPase activity, it was found experimentally that 4-hydroxytamoxifen and tamoxifen enhance rather than inhibit Hsp90 ATPase.	hydroxytamoxifen	118-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
20376192-4	2010	Surprisingly, while all drugs targeting Hsp90 inhibit the chaperone ATPase activity, it was found experimentally that 4-hydroxytamoxifen and tamoxifen enhance rather than inhibit Hsp90 ATPase.	Tamoxifen	127-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
20376192-5	2010	CONCLUSIONS/SIGNIFICANCE: Hence, tamoxifen and its metabolite are the first members of a new pharmacological class of Hsp90 activators.	Tamoxifen	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
20416171-2	2010	The HSP90 mRNA expression and migration change of human multiple myeloma cell line (U266) were detected by RT-PCR and Transwell chamber respectively after treatment of U266 cells with final concentration 50, 100, 150, 200 nmol/L of bortezomib (proteosome inhibitor) for 4 hours.	Bortezomib	232-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
20416171-3	2010	The results indicated that along with the increasing of bortezomib concentration, the expression level of HSP90alpha mRNA in U266 cells was enhanced, while no obvious increase of HSP90beta mRNA expression was observed in spite of statistical difference as a whole (p&lt;0.05), but with the increasing of drug concentration in cells, their migration ability gradually decreased (p&lt;0.05).	Bortezomib	56-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-116
20110359-9	2010	This protection does not require ATP binding and hydrolysis by Hsp90, but it is counteracted by geldanamycin, a specific inhibitor of Hsp90.	geldanamycin	96-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
20146531-9	2010	Formation of a complex with intact Hsp70 and Hsp90 or their respective C-terminal octapeptides induced folding of the TPR domain to a defined, highly stabilized structure with protected amide hydrogens.	Amides	186-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
20146531-9	2010	Formation of a complex with intact Hsp70 and Hsp90 or their respective C-terminal octapeptides induced folding of the TPR domain to a defined, highly stabilized structure with protected amide hydrogens.	Hydrogen	192-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
19685492-4	2010	Our results indicated that Sp17 protein levels in esophageal squamous cancer cell lines decreased in response to treatment with (i) the HSP90 activity inhibitor geldanamycin, (ii) the tyrosine kinase inhibitor erlotinib and (iii) cisplatin (chemotherapeutic agent commonly used in management of ESCC).	geldanamycin	161-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
20089831-2	2010	To elucidate the structural basis for ATPase stimulation of human Hsp90 by human Aha1, we have developed novel mass spectrometry approaches that demonstrate that the N- and C-terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90 to modulate the ATP hydrolysis cycle and client activity in vivo.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
20089831-2	2010	To elucidate the structural basis for ATPase stimulation of human Hsp90 by human Aha1, we have developed novel mass spectrometry approaches that demonstrate that the N- and C-terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90 to modulate the ATP hydrolysis cycle and client activity in vivo.	Adenosine Triphosphate	38-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	249-254
19686041-7	2010	The carbonyl scavenger bisulfite suppressed acrolein toxicity, intermediate filament adduction, vimentin cross-linking, Hsp90 redistribution, and loss of cellular adhesive strength, while also suppressing vimentin hyperphosphorylation.	hydrogen sulfite	23-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
19995547-2	2010	In this study, we investigated the mechanism of inhibition of TGF-beta signaling by the Hsp90 inhibitor geldanamycin (GA).	geldanamycin	104-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
19995547-2	2010	In this study, we investigated the mechanism of inhibition of TGF-beta signaling by the Hsp90 inhibitor geldanamycin (GA).	geldanamycin	118-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
20039095-0	2010	The enhancement of antiproliferative and proapoptotic activity of HDAC inhibitors by curcumin is mediated by Hsp90 inhibition.	Curcumin	85-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
20039095-2	2010	In this study, we observed that curcumin inhibited Hsp90 activity causing depletion of client proteins implicated in survival pathways.	Curcumin	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
20039095-3	2010	Based on this observation, this study was designed to investigate the cellular effects of curcumin combination with the pan-HDAC inhibitors, vorinostat and panobinostat, which induce hyperacetylation of Hsp90, resulting in inhibition of its chaperone function.	Curcumin	90-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
20039095-3	2010	Based on this observation, this study was designed to investigate the cellular effects of curcumin combination with the pan-HDAC inhibitors, vorinostat and panobinostat, which induce hyperacetylation of Hsp90, resulting in inhibition of its chaperone function.	Vorinostat	141-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
20039095-3	2010	Based on this observation, this study was designed to investigate the cellular effects of curcumin combination with the pan-HDAC inhibitors, vorinostat and panobinostat, which induce hyperacetylation of Hsp90, resulting in inhibition of its chaperone function.	Panobinostat	156-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
20087915-0	2010	Targeting the Hsp90 chaperone: synthesis of novel resorcylic acid macrolactone inhibitors of Hsp90.	resorcylic acid macrolactone	50-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20087915-0	2010	Targeting the Hsp90 chaperone: synthesis of novel resorcylic acid macrolactone inhibitors of Hsp90.	resorcylic acid macrolactone	50-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
20087915-1	2010	A series of benzo-macrolactones has been prepared by chemical synthesis, and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents.	benzo-macrolactones	12-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-125
20087915-1	2010	A series of benzo-macrolactones has been prepared by chemical synthesis, and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents.	benzo-macrolactones	12-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
20231121-5	2010	Hsp90 inhibitors, derived from the natural compound geldanamycin, are attractive targets for anticancer drug development.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20425593-5	2010	The N-terminal inhibitors, geldanamycin and radiciol, were the first two described inhibitors of Hsp90, but were not clinically useful.	geldanamycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
19662650-2	2010	The ansamycin-based Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in Phase III clinical testing.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
19662650-2	2010	The ansamycin-based Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in Phase III clinical testing.	tanespimycin	36-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
19676042-1	2010	17-AAG, the first-generation clinical Hsp90 inhibitor, exhibits promising antitumor activity in clinical studies, but is limited by poor solubility and hepatotoxicity.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
20409220-0	2010	Effect of the hsp90 inhibitor geldanamycin on androgen response of prostate cancer under hypoxic conditions.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20039369-3	2010	In this study, we further found that novobiocin, a HSP90 inhibitor, could decrease the expression of SMYD3 and dose dependently inhibit the proliferation and migration of MDA-MB-231 human breast cancer cells.	Novobiocin	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
20147598-0	2010	Detection of the ATPase activity of the molecular chaperones Hsp90 and Hsp72 using the TranscreenerTM ADP assay kit.	Adenosine Diphosphate	102-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
20147598-7	2010	The authors have evaluated the use of commercial reagents (Transcreener ADP) for the measurement of ATPase activity of both yeast and human Hsp90 (ATP K(m) approximately 500 microM) and human Hsp72 (ATP K(m) ~1 microM).	Adenosine Diphosphate	72-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
20147598-7	2010	The authors have evaluated the use of commercial reagents (Transcreener ADP) for the measurement of ATPase activity of both yeast and human Hsp90 (ATP K(m) approximately 500 microM) and human Hsp72 (ATP K(m) ~1 microM).	Adenosine Triphosphate	100-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
20147598-7	2010	The authors have evaluated the use of commercial reagents (Transcreener ADP) for the measurement of ATPase activity of both yeast and human Hsp90 (ATP K(m) approximately 500 microM) and human Hsp72 (ATP K(m) ~1 microM).	Adenosine Triphosphate	147-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
19934398-3	2010	We have previously shown that direct expression of Hsp70 and pharmacological up-regulation of Hsp70 by geldanamycin, an Hsp90 inhibitor, are protective against alphasyn-induced toxicity and prevent aggregation in culture.	geldanamycin	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
20007406-2	2010	Celastrol, isolated from a Chinese medicinal herb, is a novel heat shock protein 90 (Hsp90) inhibitor with potent anticancer activity against glioma in vitro and in vivo.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
20007406-2	2010	Celastrol, isolated from a Chinese medicinal herb, is a novel heat shock protein 90 (Hsp90) inhibitor with potent anticancer activity against glioma in vitro and in vivo.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
20007406-8	2010	Combined treatment of glioma cells with sulfasalazine and celastrol led to chemosensitization, as suggested by increased celastrol-induced cell cycle arrest, apoptosis, and down-regulation of the Hsp90 client protein, epidermal growth factor receptor.	Sulfasalazine	40-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-201
20007406-8	2010	Combined treatment of glioma cells with sulfasalazine and celastrol led to chemosensitization, as suggested by increased celastrol-induced cell cycle arrest, apoptosis, and down-regulation of the Hsp90 client protein, epidermal growth factor receptor.	celastrol	58-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-201
20007406-8	2010	Combined treatment of glioma cells with sulfasalazine and celastrol led to chemosensitization, as suggested by increased celastrol-induced cell cycle arrest, apoptosis, and down-regulation of the Hsp90 client protein, epidermal growth factor receptor.	celastrol	121-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-201
20038533-5	2010	The whole MR-hsp90-based heterocomplex was transiently recovered in the soluble fraction of the nucleus after 10 min of incubation with aldosterone.	Aldosterone	136-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
19856130-1	2010	UNLABELLED: Hsp90 is an ATP-dependent molecular chaperone that regulates key signaling proteins and thereby impacts cell growth and development.	Adenosine Triphosphate	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
19856130-2	2010	Chaperone cycle of Hsp90 is regulated by ATP binding and hydrolysis through its intrinsic ATPase activities, which is in turn modulated by interaction with its co-chaperones.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19856130-10	2010	This analysis provides mechanistic insights into the links between increased Hsp90 ATPase activity, tumor phenotype and the hypersensitivity of tumor Hsp90 to inhibition by ATP analogs.	Adenosine Triphosphate	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19856130-10	2010	This analysis provides mechanistic insights into the links between increased Hsp90 ATPase activity, tumor phenotype and the hypersensitivity of tumor Hsp90 to inhibition by ATP analogs.	Adenosine Triphosphate	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
20005756-1	2010	Heat Shock Protein 90 (HSP90), an ATP-dependent molecular chaperone, has emerged as a promising target in the treatment of cancer.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
20005756-1	2010	Heat Shock Protein 90 (HSP90), an ATP-dependent molecular chaperone, has emerged as a promising target in the treatment of cancer.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
20005756-3	2010	Many HSP90 inhibitors bind to the ATP-binding pocket, inhibit chaperone function, resulting in cell death.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
20133715-7	2010	Either disruption of the LIS1-Hsp90 interaction with the C terminus of NudCL2 or inhibition of Hsp90 chaperone function by geldanamycin decreased LIS1 stability.	geldanamycin	123-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
20100459-0	2010	Inhibition of heat shock protein 90 attenuates adenylate cyclase sensitization after chronic morphine treatment.	Morphine	93-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
20100459-3	2010	Here, we report that treatment of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90), led to effective attenuation of morphine-induced adenylate cyclase sensitization.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
20100459-3	2010	Here, we report that treatment of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90), led to effective attenuation of morphine-induced adenylate cyclase sensitization.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
20100459-3	2010	Here, we report that treatment of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90), led to effective attenuation of morphine-induced adenylate cyclase sensitization.	Morphine	138-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
20100459-3	2010	Here, we report that treatment of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90), led to effective attenuation of morphine-induced adenylate cyclase sensitization.	Morphine	138-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
20100459-8	2010	These results indicate that Hsp90 is a new pharmacological target for the suppression of adenylate cyclase sensitization induced by chronic morphine treatment.	Morphine	140-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
20170530-2	2010	Heat shock protein 90 alpha (HSP90alpha) isoform is an ATP-dependent molecular chaperone that maintains the active conformation of client oncoproteins in cancer cells, which is abundantly expressed in HCC, especially in hepatitis B virus (HBV)-related tumors, might be involved in tumor progression.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-39
19769945-1	2010	The purpose of this study is to investigate the efficacy and the mechanism of Hsp90 inhibition of Withaferin A (WA), a steroidal lactone occurring in Withania somnifera, in pancreatic cancer in vitro and in vivo.	withaferin A	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
19769945-1	2010	The purpose of this study is to investigate the efficacy and the mechanism of Hsp90 inhibition of Withaferin A (WA), a steroidal lactone occurring in Withania somnifera, in pancreatic cancer in vitro and in vivo.	Lactones	129-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
19769945-4	2010	Western blotting demonstrated that WA inhibited Hsp90 chaperone activity to induce degradation of Hsp90 client proteins (Akt, Cdk4 and glucocorticoid receptor), which was reversed by the proteasomal inhibitor, MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	210-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
19769945-4	2010	Western blotting demonstrated that WA inhibited Hsp90 chaperone activity to induce degradation of Hsp90 client proteins (Akt, Cdk4 and glucocorticoid receptor), which was reversed by the proteasomal inhibitor, MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	210-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	Biotin	3-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	Biotin	3-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	Biotin	3-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	withaferin A	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	withaferin A	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	withaferin A	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	Biotin	102-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	Biotin	102-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19769945-5	2010	WA-biotin pull down assay of Hsp90 using Panc-1 cancer cell lysates and purified Hsp90 showed that WA-biotin binds to C-terminus of Hsp90 which was competitively blocked by unlabeled WA.	Biotin	102-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19769945-8	2010	These data demonstrate that Withaferin A binds Hsp90, inhibits Hsp90 chaperone activity through an ATP-independent mechanism, results in Hsp90 client protein degradation, and exhibits in vivo anticancer activity against pancreatic cancer.	withaferin A	28-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19769945-8	2010	These data demonstrate that Withaferin A binds Hsp90, inhibits Hsp90 chaperone activity through an ATP-independent mechanism, results in Hsp90 client protein degradation, and exhibits in vivo anticancer activity against pancreatic cancer.	withaferin A	28-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19769945-8	2010	These data demonstrate that Withaferin A binds Hsp90, inhibits Hsp90 chaperone activity through an ATP-independent mechanism, results in Hsp90 client protein degradation, and exhibits in vivo anticancer activity against pancreatic cancer.	withaferin A	28-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19914055-0	2010	Hsp90-functionalized polypyrrole nanotube FET sensor for anti-cancer agent detection.	polypyrrole	21-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19914055-1	2010	A rapid and efficient strategy to detect novel heat shock protein 90 (Hsp90) inhibitors as anti-cancer agents was developed with field-effect transistor (FET) sensor based on carboxylated polypyrrole nanotubes (CPNTs).	polypyrrole nanotubes	188-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-68
19914055-1	2010	A rapid and efficient strategy to detect novel heat shock protein 90 (Hsp90) inhibitors as anti-cancer agents was developed with field-effect transistor (FET) sensor based on carboxylated polypyrrole nanotubes (CPNTs).	polypyrrole nanotubes	188-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
19914055-1	2010	A rapid and efficient strategy to detect novel heat shock protein 90 (Hsp90) inhibitors as anti-cancer agents was developed with field-effect transistor (FET) sensor based on carboxylated polypyrrole nanotubes (CPNTs).	cpnts	211-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-68
19914055-1	2010	A rapid and efficient strategy to detect novel heat shock protein 90 (Hsp90) inhibitors as anti-cancer agents was developed with field-effect transistor (FET) sensor based on carboxylated polypyrrole nanotubes (CPNTs).	cpnts	211-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
19914055-5	2010	Subsequently, Hsp90 was attached to the CPNTs surface through condensation reactions between the terminal amino groups in Hsp90 amino acid residues and the carboxyl groups on the CPNTs.	cpnts	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19914055-5	2010	Subsequently, Hsp90 was attached to the CPNTs surface through condensation reactions between the terminal amino groups in Hsp90 amino acid residues and the carboxyl groups on the CPNTs.	cpnts	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
19914055-5	2010	Subsequently, Hsp90 was attached to the CPNTs surface through condensation reactions between the terminal amino groups in Hsp90 amino acid residues and the carboxyl groups on the CPNTs.	cpnts	179-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
20159548-0	2010	Phosphotyrosine confers client specificity to Hsp90.	Phosphotyrosine	0-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
20159548-2	2010	(2010) report a new tyrosine phosphorylation site in Hsp90, which is essential for Hsp90"s interaction with a subset of its client proteins, notably protein kinases.	Tyrosine	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
20159548-2	2010	(2010) report a new tyrosine phosphorylation site in Hsp90, which is essential for Hsp90"s interaction with a subset of its client proteins, notably protein kinases.	Tyrosine	20-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20159554-1	2010	The chaperone Hsp90 is an ATP-dependent, dimeric molecular machine regulated by several cochaperones, including inhibitors and the unique ATPase activator Aha1.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19996313-0	2010	Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19996313-1	2010	Hsp90 is an ATP-dependent molecular chaperone.	Adenosine Triphosphate	12-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19996313-2	2010	The best characterized inhibitors of Hsp90 target its ATP binding pocket, causing nonselective degradation of Hsp90 client proteins.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19996313-2	2010	The best characterized inhibitors of Hsp90 target its ATP binding pocket, causing nonselective degradation of Hsp90 client proteins.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
19996313-3	2010	Here, we show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperone p23, resulting in a more selective destabilization of steroid receptors compared with kinase clients.	celastrol	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
20036116-0	2010	(89)Zr-trastuzumab PET visualises HER2 downregulation by the HSP90 inhibitor NVP-AUY922 in a human tumour xenograft.	Zirconium	4-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
19875381-0	2010	A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.	Adenosine Diphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
19875381-0	2010	A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.	Adenosine Diphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
19875381-2	2010	Here we use tandem affinity purification and LC-MS/MS to investigate the proteome-wide effects of ATP, ADP, and geldanamycin on the constituents of the human HSP90 interactome.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
19875381-2	2010	Here we use tandem affinity purification and LC-MS/MS to investigate the proteome-wide effects of ATP, ADP, and geldanamycin on the constituents of the human HSP90 interactome.	Adenosine Diphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
19875381-2	2010	Here we use tandem affinity purification and LC-MS/MS to investigate the proteome-wide effects of ATP, ADP, and geldanamycin on the constituents of the human HSP90 interactome.	geldanamycin	112-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
19875381-4	2010	Interestingly, our results also show that geldanamycin treatment causes HSP90 complexes to become significantly enriched for core transcription machinery, suggesting that HSP90 inhibition may have broad based effects on transcription and RNA processing.	geldanamycin	42-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
19875381-4	2010	Interestingly, our results also show that geldanamycin treatment causes HSP90 complexes to become significantly enriched for core transcription machinery, suggesting that HSP90 inhibition may have broad based effects on transcription and RNA processing.	geldanamycin	42-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
19875381-5	2010	We further characterized a novel ADP-dependent HSP90 interaction with the cysteine- and histidine-rich domain (CHORD)-containing protein CHORDC1.	Adenosine Diphosphate	33-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19875381-5	2010	We further characterized a novel ADP-dependent HSP90 interaction with the cysteine- and histidine-rich domain (CHORD)-containing protein CHORDC1.	Cysteine	74-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19875381-5	2010	We further characterized a novel ADP-dependent HSP90 interaction with the cysteine- and histidine-rich domain (CHORD)-containing protein CHORDC1.	Histidine	88-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
20142037-4	2010	Almost all known Hsp90 inhibitors have been reported to bind to the Hsp90 N-terminal ATP-binding site and to simultaneously induce degradation and activation of its multiple client proteins.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
20142037-4	2010	Almost all known Hsp90 inhibitors have been reported to bind to the Hsp90 N-terminal ATP-binding site and to simultaneously induce degradation and activation of its multiple client proteins.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
19632771-1	2010	The Hsp90 inhibitor 17DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) is undergoing clinical trials as an antitumor drug.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
19632771-1	2010	The Hsp90 inhibitor 17DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) is undergoing clinical trials as an antitumor drug.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	28-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
21904660-1	2010	Structural modifications to the coumarin core and benzamide side chain of novobiocin have successfully transformed the natural product from a selective DNA gyrase inhibitor into a potent inhibitor of the Hsp90 C-terminus.	coumarin	32-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
21904660-1	2010	Structural modifications to the coumarin core and benzamide side chain of novobiocin have successfully transformed the natural product from a selective DNA gyrase inhibitor into a potent inhibitor of the Hsp90 C-terminus.	benzamide	50-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
21904660-1	2010	Structural modifications to the coumarin core and benzamide side chain of novobiocin have successfully transformed the natural product from a selective DNA gyrase inhibitor into a potent inhibitor of the Hsp90 C-terminus.	Novobiocin	74-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	204-209
21904660-3	2010	Therefore, a series of sugar mimics and non-sugar derivatives were synthesized and evaluated to identify simplified compounds that exhibit Hsp90 inhibition.	Sugars	23-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
19833175-11	2010	Hyperalgesia (allodynia was not tested) and in vitro M3G-induced TLR4 signaling were both blocked by 17-DMAG, an inhibitor of heat shock protein 90 (HSP90) that can contribute to TLR4 signaling.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	101-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
19833175-11	2010	Hyperalgesia (allodynia was not tested) and in vitro M3G-induced TLR4 signaling were both blocked by 17-DMAG, an inhibitor of heat shock protein 90 (HSP90) that can contribute to TLR4 signaling.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	101-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
19908836-0	2010	Dihydroxyphenylisoindoline amides as orally bioavailable inhibitors of the heat shock protein 90 (hsp90) molecular chaperone.	dihydroxyphenylisoindoline amides	0-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-96
19908836-0	2010	Dihydroxyphenylisoindoline amides as orally bioavailable inhibitors of the heat shock protein 90 (hsp90) molecular chaperone.	dihydroxyphenylisoindoline amides	0-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
19908836-1	2010	The discovery and optimization of potency and metabolic stability of a novel class of dihyroxyphenylisoindoline amides as Hsp90 inhibitors are presented.	dihyroxyphenylisoindoline amides	86-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
19908836-2	2010	Optimization of a screening hit using structure-based design and modification of log D and chemical structural features led to the identification of a class of orally bioavailable non-quinone-containing Hsp90 inhibitors.	quinone	184-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	203-208
20090934-11	2010	17-allylamino-17-demethoxygeldanamycin (17AAG), a drug that inhibits Hsp90 chaperone and degrades its client protein Akt concomitantly elevated Hsp70 levels by promoting nuclear translocation of HSF1 from the cytosol.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
20090934-11	2010	17-allylamino-17-demethoxygeldanamycin (17AAG), a drug that inhibits Hsp90 chaperone and degrades its client protein Akt concomitantly elevated Hsp70 levels by promoting nuclear translocation of HSF1 from the cytosol.	tanespimycin	40-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
20090934-17	2010	Additionally, Resveratrol can be used in combination with chemotherapeutic agents such as 17AAG, an Hsp90 inhibitor reported to induce Hsp70 and hence compromise its chemotherapeutic potential.	Resveratrol	14-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
20090934-17	2010	Additionally, Resveratrol can be used in combination with chemotherapeutic agents such as 17AAG, an Hsp90 inhibitor reported to induce Hsp70 and hence compromise its chemotherapeutic potential.	tanespimycin	90-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
20730035-0	2010	Mechanistic studies of Sansalvamide A-amide: an allosteric modulator of Hsp90.	CHEMBL192264	23-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
20730035-1	2010	Herein we show that San A-amide, a structurally unique molecule, influences a subset of cancer-related pathways involving Hsp90.	sansalvamide A	20-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
20730035-2	2010	We show that San A-amide specifically binds to the N-middle domain of Hsp90 allosterically disrupts the binding of proteins thought to interact with the Hsp90 C-terminal domain, while having no effect on an N-terminal domain client protein.	sansalvamide A	13-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
20730035-2	2010	We show that San A-amide specifically binds to the N-middle domain of Hsp90 allosterically disrupts the binding of proteins thought to interact with the Hsp90 C-terminal domain, while having no effect on an N-terminal domain client protein.	sansalvamide A	13-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
20730035-3	2010	This unique mechanism suggests that San A-amide is a potential tool for studying C-terminal binding proteins of Hsp90 as well as a promising lead in the development of new cancer therapeutics.	sansalvamide A	36-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
19948822-5	2010	Targeting TRAP-1 with a novel class of mitochondria-directed Hsp90 inhibitors, ie, Gamitrinibs, caused rapid and complete killing of androgen-dependent or -independent prostate cancer, but not BPH-1 cells, whereas reintroduction of TRAP-1 in BPH-1 cells conferred sensitivity to Gamitrinib-induced cell death.	gamitrinibs	83-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
19948822-5	2010	Targeting TRAP-1 with a novel class of mitochondria-directed Hsp90 inhibitors, ie, Gamitrinibs, caused rapid and complete killing of androgen-dependent or -independent prostate cancer, but not BPH-1 cells, whereas reintroduction of TRAP-1 in BPH-1 cells conferred sensitivity to Gamitrinib-induced cell death.	Gamitrinib	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
19932969-1	2010	The natural products novobiocin and derrubone have both demonstrated Hsp90 inhibition and structure-activity relationships have been established for each scaffold.	Novobiocin	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
19932969-4	2010	These studies confirmed that the functionality present at the 3-position of the isoflavone plays a critical role in determining Hsp90 inhibition and suggests that the bicyclic ring system present in both novobiocin and derrubone do not share similar modes of binding.	Isoflavones	80-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
19932969-4	2010	These studies confirmed that the functionality present at the 3-position of the isoflavone plays a critical role in determining Hsp90 inhibition and suggests that the bicyclic ring system present in both novobiocin and derrubone do not share similar modes of binding.	Novobiocin	204-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
20057149-5	2010	Herbimycin A induced down-regulation of the AhR protein by inhibiting its molecular chaperone heat shock protein 90 (HSP90).	herbimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-115
20057149-5	2010	Herbimycin A induced down-regulation of the AhR protein by inhibiting its molecular chaperone heat shock protein 90 (HSP90).	herbimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
20946630-1	2010	INTRODUCTION: 17-allyamino-17-demethoxygeldanamycin (17-AAG), a small molecule inhibitor of Hsp90, is currently in clinical trials in breast cancer.	17-allyamino-17-demethoxygeldanamycin	14-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
20946630-10	2010	CONCLUSIONS: This study determined that in the MCF-7 breast cancer model inhibition of Hsp90 by 17-AAG results in a significant MRS-detectable increase in choline, PC and GPC, which is likely due to an increase in choline transport into the cell and phospholipase activation.	Choline	155-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
20946630-10	2010	CONCLUSIONS: This study determined that in the MCF-7 breast cancer model inhibition of Hsp90 by 17-AAG results in a significant MRS-detectable increase in choline, PC and GPC, which is likely due to an increase in choline transport into the cell and phospholipase activation.	Choline	214-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
20946630-12	2010	As Hsp90 inhibitors enter routine clinical use, t-Cho could thus provide an easily detectable, noninvasive metabolic biomarker of Hsp90 inhibition in breast cancer patients.	t-cho	48-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
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
21063103-0	2010	Opposite effect of Hsp90alpha and Hsp90beta on eNOS ability to produce nitric oxide or superoxide anion in human embryonic kidney cells.	Nitric Oxide	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-29
21063103-0	2010	Opposite effect of Hsp90alpha and Hsp90beta on eNOS ability to produce nitric oxide or superoxide anion in human embryonic kidney cells.	Superoxides	87-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-29
21063103-8	2010	The Hsp90alpha over-expression induced a significant increase in NO(2)/NO(3) levels, an effect that was associated with increased phosphorylation of eNOS Ser 1177 and Akt/PKB Ser473, as well as with a greater Hsp90alpha dimerization.	Serine	154-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-14
22615596-4	2010	After intradermal injection of confirmed purified band of protein to rabbits and isolation of the serum IgG antibody, for its affinity purification, the rabbit"s purified Hsp90 specific IgG was coupled to the cyanogen bromide-activated Sepharose 4B.	Cyanogen Bromide	209-225	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
22615596-4	2010	After intradermal injection of confirmed purified band of protein to rabbits and isolation of the serum IgG antibody, for its affinity purification, the rabbit"s purified Hsp90 specific IgG was coupled to the cyanogen bromide-activated Sepharose 4B.	Sepharose	236-245	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
19945858-1	2010	PURPOSE: Phase I dose-escalation study to determine the toxicity and maximum tolerated dose (MTD) of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein 90 (Hsp90) inhibitor, administered on a twice weekly schedule in patients with advanced cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	101-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-187
19945858-1	2010	PURPOSE: Phase I dose-escalation study to determine the toxicity and maximum tolerated dose (MTD) of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein 90 (Hsp90) inhibitor, administered on a twice weekly schedule in patients with advanced cancer.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	101-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-194
19157829-4	2010	Moreover, the carotenoid strongly prevented the increase of NOX-4, hsp70 and hsp90 expressions as well as the phosphorylation of the redox-sensitive p38, JNK and ERK1/2 induced by the oxysterol.	Carotenoids	14-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19157829-4	2010	Moreover, the carotenoid strongly prevented the increase of NOX-4, hsp70 and hsp90 expressions as well as the phosphorylation of the redox-sensitive p38, JNK and ERK1/2 induced by the oxysterol.	Oxysterols	184-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19408974-5	2010	METHODS: The authors examined the cytotoxicity of an hsp90 inhibitor, 17-(allylamino)-17-demethoxygeldanamycin (17-AAG), both alone and in combination with 1 of 3 DNA-damaging agents (cisplatin, 1,3-bis(2-chloroethyl)-1-nitrosourea, and TMZ) in human glioma cell lines.	tanespimycin	70-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
19408974-11	2010	Similar effects were observed when cells were treated with radicicol, another hsp90 inhibitor.	monorden	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
21253549-2	2010	GA derivatives are being evaluated as anti-neoplastic agents, but their utility against parasites whose heat shock proteins (Hsps) have homology with human Hsp90 is unknown.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
19956882-0	2010	p53 independent radio-sensitization of human lymphoblastoid cell lines by Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	90-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
19956882-2	2010	Recent studies presented that an Hsp90 inhibitor, 17AAG (17-allylamino-17-demethoxygeldanamycin), enhanced tumor radio-sensitivity, while this was not observed in normal cells.	tanespimycin	50-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
19956882-2	2010	Recent studies presented that an Hsp90 inhibitor, 17AAG (17-allylamino-17-demethoxygeldanamycin), enhanced tumor radio-sensitivity, while this was not observed in normal cells.	tanespimycin	57-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
19739131-2	2010	Previously, we reported the development of novobiocin analogues designed to inhibit the C-terminal portion of Hsp90, which demonstrated the ability to decrease client protein expression.	Novobiocin	43-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
19890989-8	2010	Hsp90 adopts an additional ligand-specific conformation in the presence of ATP and we find that osmolytes do not significantly affect this conformational change.	Adenosine Triphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
20373211-1	2010	An adenosine tri-phosphate (ATP)-dependent molecular chaperone heat shock protein (Hsp90) is of current interest as a potential anticancer drug target.	Adenosine Triphosphate	3-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20373211-1	2010	An adenosine tri-phosphate (ATP)-dependent molecular chaperone heat shock protein (Hsp90) is of current interest as a potential anticancer drug target.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20373211-3	2010	In order to identify essential chemical functional features for Hsp90 inhibition, a pharmacophore model consisting of one hydrogen bond donor, two hydrogen bond acceptor lipid and one hydrophobic feature has been developed using Hypogen (Catalyst 2.0 software) on a total set of 103 inhibitors consisting of 16 and 87 compounds in the training and the test set, respectively.	Hydrogen	122-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
19850929-0	2009	The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
19850929-3	2009	We found that treatment with the Hsp90 inhibitor geldanamycin leads to a substantial reduction in the number of HeLa cells that contain processing bodies.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
19858214-0	2009	Characterization of celastrol to inhibit hsp90 and cdc37 interaction.	celastrol	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
19858214-5	2009	The GST pull-down assay and ELISA assay show that Cdc37 binds to ADP-bound/nucleotide-free Hsp90 but not ATP-bound Hsp90.	Adenosine Diphosphate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
19858214-6	2009	Celastrol disrupts Hsp90-Cdc37 complex formation, whereas the classical Hsp90 inhibitors (e.g. geldanamycin) have no effect.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19858214-7	2009	Celastrol inhibits Hsp90 ATPase activity without blocking ATP binding.	celastrol	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19858214-7	2009	Celastrol inhibits Hsp90 ATPase activity without blocking ATP binding.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19858214-8	2009	Proteolytic fingerprinting indicates celastrol binds to Hsp90 C-terminal domain to protect it from trypsin digestion.	celastrol	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
19858214-9	2009	These data suggest that celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex.	celastrol	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19858214-9	2009	These data suggest that celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex.	celastrol	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
19858214-9	2009	These data suggest that celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex.	celastrol	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
19965370-4	2009	We also demonstrate that secretion of Hsp90alpha is determined by the phosphorylation status at residue Thr-90, regulated by protein kinase A and protein phosphatase 5.	Threonine	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-48
20156737-0	2009	Nuclear HSP90 and HSP70 in COPD patients treated with formoterol or formoterol and corticosteroids.	Formoterol Fumarate	54-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
20156737-0	2009	Nuclear HSP90 and HSP70 in COPD patients treated with formoterol or formoterol and corticosteroids.	Formoterol Fumarate	68-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
19828702-5	2009	Treatment with PS also disrupted the chaperone association of JAK2V617F with hsp90, promoting proteasomal degradation of JAK2V617F.	Panobinostat	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
20201223-4	2009	To begin to address this issue, we developed novel long-acting biocompatible and biodegradable phospholipid micelles (size, approximately 15 nm) to inhibit triggering receptor expressed on myeloid cells 1 (TREM-1), reactive oxygen species and Hsp90, key effectors thought to underlie ALI, in vivo.	Phospholipids	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	243-248
19952119-0	2009	The antiproliferative activity of the heat shock protein 90 inhibitor IPI-504 is not dependent on NAD(P)H:quinone oxidoreductase 1 activity in vivo.	tanespimycin	70-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-59
19952119-1	2009	IPI-504, a water-soluble ansamycin analogue currently being investigated in clinical trials, is a potent inhibitor of the protein chaperone heat shock protein 90 (Hsp90).	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
19952119-1	2009	IPI-504, a water-soluble ansamycin analogue currently being investigated in clinical trials, is a potent inhibitor of the protein chaperone heat shock protein 90 (Hsp90).	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
19952119-1	2009	IPI-504, a water-soluble ansamycin analogue currently being investigated in clinical trials, is a potent inhibitor of the protein chaperone heat shock protein 90 (Hsp90).	Water	11-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
19952119-1	2009	IPI-504, a water-soluble ansamycin analogue currently being investigated in clinical trials, is a potent inhibitor of the protein chaperone heat shock protein 90 (Hsp90).	Rifabutin	25-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-161
19952119-1	2009	IPI-504, a water-soluble ansamycin analogue currently being investigated in clinical trials, is a potent inhibitor of the protein chaperone heat shock protein 90 (Hsp90).	Rifabutin	25-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
19952119-2	2009	Inhibition of Hsp90 by IPI-504 triggers the degradation of important oncogenic client proteins.	tanespimycin	23-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19952119-3	2009	In cells, the free base of IPI-504 hydroquinone exists in a dynamic redox equilibrium with its corresponding quinone (17-AAG); the hydroquinone form binding 50 times more tightly to Hsp90.	ipi-504 hydroquinone	27-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
19952119-3	2009	In cells, the free base of IPI-504 hydroquinone exists in a dynamic redox equilibrium with its corresponding quinone (17-AAG); the hydroquinone form binding 50 times more tightly to Hsp90.	quinone	40-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
19952119-3	2009	In cells, the free base of IPI-504 hydroquinone exists in a dynamic redox equilibrium with its corresponding quinone (17-AAG); the hydroquinone form binding 50 times more tightly to Hsp90.	hydroquinone	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
19952121-0	2009	Targeting heat shock protein 90 with CUDC-305 overcomes erlotinib resistance in non-small cell lung cancer.	CUDC 305	37-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-31
19741006-3	2009	Here, we investigated the extent to which a novel novobiocin-derived C-terminal Hsp90 inhibitor, designated KU135, induced antiproliferative effects in Jurkat T-lymphocytes.	Novobiocin	50-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
19741006-3	2009	Here, we investigated the extent to which a novel novobiocin-derived C-terminal Hsp90 inhibitor, designated KU135, induced antiproliferative effects in Jurkat T-lymphocytes.	KU135	108-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
19741006-4	2009	The results indicated that KU135 bound directly to Hsp90, caused the degradation of known Hsp90 client proteins, and induced more potent antiproliferative effects than the established N-terminal Hsp90 inhibitor 17-allylamino-demethoxygeldanamycin (17-AAG).	KU135	27-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19741006-4	2009	The results indicated that KU135 bound directly to Hsp90, caused the degradation of known Hsp90 client proteins, and induced more potent antiproliferative effects than the established N-terminal Hsp90 inhibitor 17-allylamino-demethoxygeldanamycin (17-AAG).	KU135	27-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
19741006-4	2009	The results indicated that KU135 bound directly to Hsp90, caused the degradation of known Hsp90 client proteins, and induced more potent antiproliferative effects than the established N-terminal Hsp90 inhibitor 17-allylamino-demethoxygeldanamycin (17-AAG).	KU135	27-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
19741006-5	2009	Closer examination of the cellular response to KU135 and 17-AAG revealed that only 17-AAG induced a strong up-regulation of Hsp70 and Hsp90.	tanespimycin	83-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
19741006-8	2009	Together, these data suggest that KU135 inhibits cell proliferation by regulating signaling pathways that are mechanistically different from those targeted by 17-AAG and as such represents a novel opportunity for Hsp90 inhibition.	KU135	34-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	213-218
19966776-0	2009	A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas.	purine	2-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
19966776-6	2009	We examined the pharmacokinetics, toxicity and efficacy of PU-H71, a recently developed purine-derived Hsp90 inhibitor.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	59-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
19966776-6	2009	We examined the pharmacokinetics, toxicity and efficacy of PU-H71, a recently developed purine-derived Hsp90 inhibitor.	purine	88-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
19913553-3	2010	Here, we study one facet of this CHIP-mediated turnover by determining the lysine residues on human Hsp70 and Hsp90 ubiquitinated by CHIP.	Lysine	75-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
19913553-5	2010	Six such ubiquitination sites were identified on Hsp70 (K325, K451, K524, K526, K559, and K561) and 13 ubiquitinated lysine residues were found on Hsp90 (K107, K204, K219, K275, K284, K347, K399, K477, K481, K538, K550, K607, and K623).	Lysine	117-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
19952121-0	2009	Targeting heat shock protein 90 with CUDC-305 overcomes erlotinib resistance in non-small cell lung cancer.	Erlotinib Hydrochloride	56-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-31
19952121-1	2009	CUDC-305 is a heat shock protein 90 (HSP90) inhibitor of the novel imidazopyridine class.	CUDC 305	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
19856365-1	2009	The pochoximes, based on the radicicol pharmacophore, are potent inhibitors of heat shock protein 90 (HSP90) that retain their activity in vivo.	monorden	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-100
19856365-1	2009	The pochoximes, based on the radicicol pharmacophore, are potent inhibitors of heat shock protein 90 (HSP90) that retain their activity in vivo.	monorden	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
19856365-4	2009	Cocrystal structures of pochoximes A and B with HSP90 show that pochoximes bind to a different conformation of HSP90 than radicicol and provide a rationale for the enhanced affinity of the pochoximes relative to radicicol and the pochonins.	monorden	122-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
19856365-4	2009	Cocrystal structures of pochoximes A and B with HSP90 show that pochoximes bind to a different conformation of HSP90 than radicicol and provide a rationale for the enhanced affinity of the pochoximes relative to radicicol and the pochonins.	monorden	212-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
19856365-4	2009	Cocrystal structures of pochoximes A and B with HSP90 show that pochoximes bind to a different conformation of HSP90 than radicicol and provide a rationale for the enhanced affinity of the pochoximes relative to radicicol and the pochonins.	monorden	212-221	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
19734938-0	2009	The neuroblastoma tumour-suppressor TrkAI and its oncogenic alternative TrkAIII splice variant exhibit geldanamycin-sensitive interactions with Hsp90 in human neuroblastoma cells.	geldanamycin	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
19952121-1	2009	CUDC-305 is a heat shock protein 90 (HSP90) inhibitor of the novel imidazopyridine class.	CUDC 305	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19952121-1	2009	CUDC-305 is a heat shock protein 90 (HSP90) inhibitor of the novel imidazopyridine class.	imidazopyridine	67-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
19952121-1	2009	CUDC-305 is a heat shock protein 90 (HSP90) inhibitor of the novel imidazopyridine class.	imidazopyridine	67-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19952121-3	2009	We show that CUDC-305 binds strongly to HSP90 extracted from erlotinib-resistant NSCLC cells (IC50 70 nmol/L).	CUDC 305	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19952121-3	2009	We show that CUDC-305 binds strongly to HSP90 extracted from erlotinib-resistant NSCLC cells (IC50 70 nmol/L).	Erlotinib Hydrochloride	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19703551-2	2009	Hsp90 inhibitor geldanamycin (GA) cytotoxicity has been attributed to the disruption of Hsp90 binding, and the contribution of oxidative stress generated by its quinone group has not been studied in this context.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19703551-2	2009	Hsp90 inhibitor geldanamycin (GA) cytotoxicity has been attributed to the disruption of Hsp90 binding, and the contribution of oxidative stress generated by its quinone group has not been studied in this context.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
19703551-2	2009	Hsp90 inhibitor geldanamycin (GA) cytotoxicity has been attributed to the disruption of Hsp90 binding, and the contribution of oxidative stress generated by its quinone group has not been studied in this context.	geldanamycin	30-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19703551-2	2009	Hsp90 inhibitor geldanamycin (GA) cytotoxicity has been attributed to the disruption of Hsp90 binding, and the contribution of oxidative stress generated by its quinone group has not been studied in this context.	geldanamycin	30-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
19703551-5	2009	At 24 h, NAC prevented cytotoxicity and Hsp90 complex disruption.	Acetylcysteine	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19703551-8	2009	GA and MEN decreased Hsp90-binding protein expression, and proteasomal inhibition prevented MEN-, but not GA-induced degradation.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
19703551-9	2009	In conclusion, whereas MEN cytotoxicity is mediated by ROS and proteasomal degradation, GA-induced cytotoxicity requires ROS but induces Hsp90 complex dissociation and proteasome-independent protein degradation.	geldanamycin	88-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
19734938-1	2009	Hsp90 chaperones stabilize many tyrosine kinases including several oncogenes, which are inhibited or induced to degrade by the Hsp90 inhibitor geldanamycin (GA).	geldanamycin	143-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19734938-1	2009	Hsp90 chaperones stabilize many tyrosine kinases including several oncogenes, which are inhibited or induced to degrade by the Hsp90 inhibitor geldanamycin (GA).	geldanamycin	143-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
19734938-1	2009	Hsp90 chaperones stabilize many tyrosine kinases including several oncogenes, which are inhibited or induced to degrade by the Hsp90 inhibitor geldanamycin (GA).	geldanamycin	157-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19734938-1	2009	Hsp90 chaperones stabilize many tyrosine kinases including several oncogenes, which are inhibited or induced to degrade by the Hsp90 inhibitor geldanamycin (GA).	geldanamycin	157-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
19734938-6	2009	TrkAI exhibits GA-sensitive interaction with Hsp90 required for receptor endoplasmic reticulum export, maturation, cell surface stabilization and ligand-mediated activation, whereas TrkAIII exhibits GA-sensitive interactions with Hsp90 required for spontaneous activity and to a lesser extent stability.	geldanamycin	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
19734938-8	2009	Our data suggest that GA-sensitive interactions with Hsp90 are critical for both TrkAI tumour suppressor and TrkAIII oncogenic function in NB and that TrkAIII expression exerts a negative impact on GA-induced NB cell eradication, which can be counteracted by a novel TrkAIII-specific peptide nucleic acid inhibitor.	geldanamycin	22-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
19861537-3	2009	We examined whether the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) can inhibit the growth of aromatase inhibitor-resistant breast cancers and the mechanisms by which 17-DMAG affects proliferation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	64-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
19861537-3	2009	We examined whether the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) can inhibit the growth of aromatase inhibitor-resistant breast cancers and the mechanisms by which 17-DMAG affects proliferation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	64-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19861537-3	2009	We examined whether the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) can inhibit the growth of aromatase inhibitor-resistant breast cancers and the mechanisms by which 17-DMAG affects proliferation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	119-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
19861537-3	2009	We examined whether the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) can inhibit the growth of aromatase inhibitor-resistant breast cancers and the mechanisms by which 17-DMAG affects proliferation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	119-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19861537-3	2009	We examined whether the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) can inhibit the growth of aromatase inhibitor-resistant breast cancers and the mechanisms by which 17-DMAG affects proliferation.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	227-234	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19861537-8	2009	Moreover, detailed mechanistic studies suggested that 17-DMAG inhibits cell growth via degradation of HSP90 client proteins AKT and HER2.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
19759002-6	2009	This suggests that Hsp90 modulates the assembly of alpha-synuclein in an ATP-dependent manner.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
19844167-5	2009	We found such genetic lesions to predict activity of geldanamycin-derived Hsp90 inhibitors as well as of the clinically approved SRC/ABL-inhibitor dasatinib.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
19809428-0	2009	Inhibition of constitutive and cxc-chemokine-induced NF-kappaB activity potentiates ansamycin-based HSP90-inhibitor cytotoxicity in castrate-resistant prostate cancer cells.	[[(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(azanyl)purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
19740745-7	2009	Serine phosphorylation of Hsp90 was significantly reduced in cells expressing high levels of Delta p23 compared with those expressing full-length p23.	Serine	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
19740745-8	2009	Mutation analyses revealed that two serine residues (Ser-231 and Ser-263) in Hsp90 are important for activation of telomerase, and down-regulation of telomerase activity by Delta p23 was associated with inhibition of cell growth and sensitization of cells to cisplatin.	Serine	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19740745-8	2009	Mutation analyses revealed that two serine residues (Ser-231 and Ser-263) in Hsp90 are important for activation of telomerase, and down-regulation of telomerase activity by Delta p23 was associated with inhibition of cell growth and sensitization of cells to cisplatin.	Serine	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19740745-8	2009	Mutation analyses revealed that two serine residues (Ser-231 and Ser-263) in Hsp90 are important for activation of telomerase, and down-regulation of telomerase activity by Delta p23 was associated with inhibition of cell growth and sensitization of cells to cisplatin.	Serine	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19740745-8	2009	Mutation analyses revealed that two serine residues (Ser-231 and Ser-263) in Hsp90 are important for activation of telomerase, and down-regulation of telomerase activity by Delta p23 was associated with inhibition of cell growth and sensitization of cells to cisplatin.	Cisplatin	259-268	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19481753-2	2009	METHODS AND RESULTS: The presence of HSP90 on 26 cryostat and 6 paraffin embedded sections of carotid atherosclerotic plaques was determined by immunohistochemistry and immunofluorescence.	Paraffin	64-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19686236-0	2009	Anti-myeloma activity of the novel 2-aminothienopyrimidine Hsp90 inhibitor NVP-BEP800.	2-aminothienopyrimidine	35-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
19686236-3	2009	The present study preclinically tested the effects of the novel 2-aminothienopyrimidine class Hsp90 inhibitor NVP-BEP800, which is suitable for oral formulations, on multiple myeloma cells from established cell lines and on a larger cohort (n = 40) of primary myeloma samples.	2-aminothienopyrimidine	64-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	17-allylamino	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	17-allylamino	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	17-allylamino	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	17-demethoxygeldanamycin	15-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	17-demethoxygeldanamycin	15-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	17-demethoxygeldanamycin	15-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	tanespimycin	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	tanespimycin	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19780165-1	2009	17-Allylamino, 17-demethoxygeldanamycin (17-AAG), an effective inhibitor of the heat shock protein hsp90, preferentially inhibiting tumor hsp90 compared to hsp90 from normal cells, has shown promising results against several cancers, including hormone-resistant prostate cancer.	tanespimycin	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19464103-2	2009	For Hsp90 inhibition, we used geldanamycin derivates, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and 17-DMAG (17-(dimethylaminoethylamino) 17-demethoxygeldanamycin) in this study.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
19809428-0	2009	Inhibition of constitutive and cxc-chemokine-induced NF-kappaB activity potentiates ansamycin-based HSP90-inhibitor cytotoxicity in castrate-resistant prostate cancer cells.	Rifabutin	84-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
19809428-1	2009	BACKGROUND: We determined how CXC-chemokine signalling and necrosis factor-kappaB (NF-kappaB) activity affected heat-shock protein 90 (Hsp90) inhibitor (geldanamycin (GA) and 17-allylamino-demethoxygeldanamycin (17-AAG)) cytotoxicity in castrate-resistant prostate cancer (CRPC).	geldanamycin	153-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
19809428-1	2009	BACKGROUND: We determined how CXC-chemokine signalling and necrosis factor-kappaB (NF-kappaB) activity affected heat-shock protein 90 (Hsp90) inhibitor (geldanamycin (GA) and 17-allylamino-demethoxygeldanamycin (17-AAG)) cytotoxicity in castrate-resistant prostate cancer (CRPC).	geldanamycin	153-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
19809428-1	2009	BACKGROUND: We determined how CXC-chemokine signalling and necrosis factor-kappaB (NF-kappaB) activity affected heat-shock protein 90 (Hsp90) inhibitor (geldanamycin (GA) and 17-allylamino-demethoxygeldanamycin (17-AAG)) cytotoxicity in castrate-resistant prostate cancer (CRPC).	geldanamycin	167-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
19809428-1	2009	BACKGROUND: We determined how CXC-chemokine signalling and necrosis factor-kappaB (NF-kappaB) activity affected heat-shock protein 90 (Hsp90) inhibitor (geldanamycin (GA) and 17-allylamino-demethoxygeldanamycin (17-AAG)) cytotoxicity in castrate-resistant prostate cancer (CRPC).	geldanamycin	167-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
19809428-1	2009	BACKGROUND: We determined how CXC-chemokine signalling and necrosis factor-kappaB (NF-kappaB) activity affected heat-shock protein 90 (Hsp90) inhibitor (geldanamycin (GA) and 17-allylamino-demethoxygeldanamycin (17-AAG)) cytotoxicity in castrate-resistant prostate cancer (CRPC).	17-allylamino-demethoxygeldanamycin	175-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
19809428-1	2009	BACKGROUND: We determined how CXC-chemokine signalling and necrosis factor-kappaB (NF-kappaB) activity affected heat-shock protein 90 (Hsp90) inhibitor (geldanamycin (GA) and 17-allylamino-demethoxygeldanamycin (17-AAG)) cytotoxicity in castrate-resistant prostate cancer (CRPC).	tanespimycin	212-218	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
19631219-0	2009	Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
19631219-1	2009	Despite its importance as a target in anti-cancer therapeutics and the numerous rational-based inhibitor design efforts aimed at it, there are only limited data available on structural-thermodynamic relationships of interactions of the N-terminal ATP-binding domain of Hsp90 (N-Hsp90).	Adenosine Triphosphate	247-250	heat shock protein 90 alpha family class A member 1	Homo sapiens	269-274
19631219-1	2009	Despite its importance as a target in anti-cancer therapeutics and the numerous rational-based inhibitor design efforts aimed at it, there are only limited data available on structural-thermodynamic relationships of interactions of the N-terminal ATP-binding domain of Hsp90 (N-Hsp90).	Adenosine Triphosphate	247-250	heat shock protein 90 alpha family class A member 1	Homo sapiens	276-283
19631219-3	2009	Interactions of nucleotides with N-Hsp90 are relatively weak (&gt;10 microM) and are strongly enthalpy driven over the temperature range 10-25 degrees C. Geldanamycin (GA) and its analogues 17-AAG [17-(allylamino)-17-demethoxy-GA] and 17-DMAG (17-N,N-dimethylaminoethylamino-17-demethoxy-GA) bind more strongly and have a dominant favourable enthalpic contribution over the temperature range investigated.	geldanamycin	154-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-40
19821460-1	2009	The resorcylic acid lactones (RAL) are endowed with diverse biological activity ranging from transcription factor modulators (zearalenone and zearalenol) to HSP90 inhibitors (radicicol and pochonin D) and reversible (aigialomycin D) as well as irreversible kinase inhibitors (hypothemycin and other RAL containing a cis-enone).	resorcylic acid lactones	4-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
19682504-5	2009	However, geldanamycin (GA)-mediated inhibition of Hsp90 did not disrupt their interaction or result in NDRG1 protein destabilization.	geldanamycin	9-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
19682504-5	2009	However, geldanamycin (GA)-mediated inhibition of Hsp90 did not disrupt their interaction or result in NDRG1 protein destabilization.	geldanamycin	23-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
19662498-5	2009	This is supported by the following observations: (1) phospho-Thr308 decreases when Ser129 is mutated to alanine, (2) this decrease is abolished by cell treatment with okadaic acid (to inactivate PP2A) or geldanamycin (to inactivate Hsp90), (3) phosphorylation of Ser129 neither enhances the activity of PDK1 nor hampers the in vitro activity of PP2A on Thr308, but increases the Hsp90 association to Akt.	Okadaic Acid	167-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
19662498-5	2009	This is supported by the following observations: (1) phospho-Thr308 decreases when Ser129 is mutated to alanine, (2) this decrease is abolished by cell treatment with okadaic acid (to inactivate PP2A) or geldanamycin (to inactivate Hsp90), (3) phosphorylation of Ser129 neither enhances the activity of PDK1 nor hampers the in vitro activity of PP2A on Thr308, but increases the Hsp90 association to Akt.	Okadaic Acid	167-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	379-384
19662498-5	2009	This is supported by the following observations: (1) phospho-Thr308 decreases when Ser129 is mutated to alanine, (2) this decrease is abolished by cell treatment with okadaic acid (to inactivate PP2A) or geldanamycin (to inactivate Hsp90), (3) phosphorylation of Ser129 neither enhances the activity of PDK1 nor hampers the in vitro activity of PP2A on Thr308, but increases the Hsp90 association to Akt.	geldanamycin	204-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	232-237
19662498-5	2009	This is supported by the following observations: (1) phospho-Thr308 decreases when Ser129 is mutated to alanine, (2) this decrease is abolished by cell treatment with okadaic acid (to inactivate PP2A) or geldanamycin (to inactivate Hsp90), (3) phosphorylation of Ser129 neither enhances the activity of PDK1 nor hampers the in vitro activity of PP2A on Thr308, but increases the Hsp90 association to Akt.	geldanamycin	204-216	heat shock protein 90 alpha family class A member 1	Homo sapiens	379-384
19696785-1	2009	Heat shock protein 90 (Hsp90) is an abundant, dimeric ATP-dependent molecular chaperone, and ATPase activity is essential for its in vivo functions.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
19696785-1	2009	Heat shock protein 90 (Hsp90) is an abundant, dimeric ATP-dependent molecular chaperone, and ATPase activity is essential for its in vivo functions.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
19696785-4	2009	Here, we show that this residue is a conserved, strong regulator of Hsp90 functions, including ATP hydrolysis and chaperone activity.	Adenosine Triphosphate	95-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
19763143-0	2009	Just say NO: nitric oxide regulation of Hsp90.	Nitric Oxide	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19631219-3	2009	Interactions of nucleotides with N-Hsp90 are relatively weak (&gt;10 microM) and are strongly enthalpy driven over the temperature range 10-25 degrees C. Geldanamycin (GA) and its analogues 17-AAG [17-(allylamino)-17-demethoxy-GA] and 17-DMAG (17-N,N-dimethylaminoethylamino-17-demethoxy-GA) bind more strongly and have a dominant favourable enthalpic contribution over the temperature range investigated.	geldanamycin	168-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-40
19631219-3	2009	Interactions of nucleotides with N-Hsp90 are relatively weak (&gt;10 microM) and are strongly enthalpy driven over the temperature range 10-25 degrees C. Geldanamycin (GA) and its analogues 17-AAG [17-(allylamino)-17-demethoxy-GA] and 17-DMAG (17-N,N-dimethylaminoethylamino-17-demethoxy-GA) bind more strongly and have a dominant favourable enthalpic contribution over the temperature range investigated.	tanespimycin	190-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-40
19631219-3	2009	Interactions of nucleotides with N-Hsp90 are relatively weak (&gt;10 microM) and are strongly enthalpy driven over the temperature range 10-25 degrees C. Geldanamycin (GA) and its analogues 17-AAG [17-(allylamino)-17-demethoxy-GA] and 17-DMAG (17-N,N-dimethylaminoethylamino-17-demethoxy-GA) bind more strongly and have a dominant favourable enthalpic contribution over the temperature range investigated.	tanespimycin	198-229	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-40
19631219-3	2009	Interactions of nucleotides with N-Hsp90 are relatively weak (&gt;10 microM) and are strongly enthalpy driven over the temperature range 10-25 degrees C. Geldanamycin (GA) and its analogues 17-AAG [17-(allylamino)-17-demethoxy-GA] and 17-DMAG (17-N,N-dimethylaminoethylamino-17-demethoxy-GA) bind more strongly and have a dominant favourable enthalpic contribution over the temperature range investigated.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	235-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-40
19631219-3	2009	Interactions of nucleotides with N-Hsp90 are relatively weak (&gt;10 microM) and are strongly enthalpy driven over the temperature range 10-25 degrees C. Geldanamycin (GA) and its analogues 17-AAG [17-(allylamino)-17-demethoxy-GA] and 17-DMAG (17-N,N-dimethylaminoethylamino-17-demethoxy-GA) bind more strongly and have a dominant favourable enthalpic contribution over the temperature range investigated.	17-n,n-dimethylaminoethylamino-17-demethoxy-ga	244-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-40
19748980-3	2009	In this study, we tested the effect of 17-allylaminogeldanamycin and radicicol, drugs targeting the heat shock protein-90 (HSP-90) chaperone protein and displaying antimyeloma activity, on the expression of NKG2D and DNAM-1 ligands in human myeloma cell lines.	tanespimycin	39-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-121
19748980-3	2009	In this study, we tested the effect of 17-allylaminogeldanamycin and radicicol, drugs targeting the heat shock protein-90 (HSP-90) chaperone protein and displaying antimyeloma activity, on the expression of NKG2D and DNAM-1 ligands in human myeloma cell lines.	tanespimycin	39-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-129
19748980-3	2009	In this study, we tested the effect of 17-allylaminogeldanamycin and radicicol, drugs targeting the heat shock protein-90 (HSP-90) chaperone protein and displaying antimyeloma activity, on the expression of NKG2D and DNAM-1 ligands in human myeloma cell lines.	monorden	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-121
19748980-3	2009	In this study, we tested the effect of 17-allylaminogeldanamycin and radicicol, drugs targeting the heat shock protein-90 (HSP-90) chaperone protein and displaying antimyeloma activity, on the expression of NKG2D and DNAM-1 ligands in human myeloma cell lines.	monorden	69-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-129
19805354-7	2009	We hypothesized that sulforaphane treatment would lead to hyperacetylation of HSP90 and that this would destabilize AR and attenuate AR signaling.	sulforaphane	21-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
19805354-8	2009	We confirmed this by demonstrating that sulforaphane enhances HSP90 acetylation, thereby inhibiting its association with AR.	sulforaphane	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
19805354-11	2009	The inactivation by sulforaphane of HDAC6-mediated HSP90 deacetylation and consequent attenuation of AR signaling represents a newly defined mechanism that may help explain this agent"s effects in prostate cancer.	sulforaphane	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19920922-11	2009	For instance, one cluster gathers three types of proteins (HSP90, topoisomerase VI, and BCK) which all bind the drug radicicol.	monorden	117-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
19642705-6	2009	We have used two mechanism-based inactivators, guanabenz and NG-amino-L-arginine, to alter the heme/substrate binding cleft and promote nNOS ubiquitination that can be inhibited by Hsp90.	Guanabenz	47-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
19642705-6	2009	We have used two mechanism-based inactivators, guanabenz and NG-amino-L-arginine, to alter the heme/substrate binding cleft and promote nNOS ubiquitination that can be inhibited by Hsp90.	N(G)-aminoarginine	61-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
19642705-6	2009	We have used two mechanism-based inactivators, guanabenz and NG-amino-L-arginine, to alter the heme/substrate binding cleft and promote nNOS ubiquitination that can be inhibited by Hsp90.	Heme	95-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	181-186
19333787-4	2009	CBX clearly induced not only Hsp70 but also Hsp90 (HSPC1), Hsp40 (DNAJB1), and Hsp27 (HSPB1) at concentrations of 10 to 800 microM for 16 h incubation.	Carbenoxolone	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
19333787-4	2009	CBX clearly induced not only Hsp70 but also Hsp90 (HSPC1), Hsp40 (DNAJB1), and Hsp27 (HSPB1) at concentrations of 10 to 800 microM for 16 h incubation.	Carbenoxolone	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19754360-7	2009	Several direct inhibitors of HSP90 have been developed, and they are classified into four groups: benzoquinon ansamycines and their derivatives, radicicol and its derivates, small synthetic inhibitors and a final group of other inhibitors.	benzoquinon ansamycines	98-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19754360-7	2009	Several direct inhibitors of HSP90 have been developed, and they are classified into four groups: benzoquinon ansamycines and their derivatives, radicicol and its derivates, small synthetic inhibitors and a final group of other inhibitors.	monorden	145-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19826195-5	2009	In this paper we showed that HSP90 inhibitors, geldanamycin and its analogs, can profoundly affect proliferation of rhabdomyosarcoma cells.	geldanamycin	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19654002-5	2009	Co-immunoprecipitation experiments revealed that hypoxia inhibited interaction of hERG with Hsp90 chaperone required for maturation, which was restored in the presence of ROS scavengers.	Reactive Oxygen Species	171-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
19654002-6	2009	These results demonstrate that ROS generated during hypoxia prevents maturation of the hERG protein by inhibiting Hsp90 interaction resulting in decreased protein expression and currents.	Reactive Oxygen Species	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
19482076-8	2009	All these results collectively suggest that 4-HPR-induced apoptosis is associated with a ROS-mediated conformational change in Akt, and this change, as a consequence, mediates dephosphorylation of Akt via regulating Akt-Hsp90 or Akt-PP2A complex formation.	ros	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
19826195-10	2009	Collectively, our findings suggest that blocking HSP90 action through geldanmycins could be in the future a part of new therapeutic strategies in rhabdomyosarcoma treatment.	geldanmycins	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
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.	Digitonin	98-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
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
19628238-3	2009	A highly specific Hsp90 inhibitor, 17-allylamono-demethoxygeldanamycin (17-AAG) was used to delineate the functional role of Hsp90.	17-allylamono-demethoxygeldanamycin	35-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
19628238-3	2009	A highly specific Hsp90 inhibitor, 17-allylamono-demethoxygeldanamycin (17-AAG) was used to delineate the functional role of Hsp90.	17-allylamono-demethoxygeldanamycin	35-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
19628238-3	2009	A highly specific Hsp90 inhibitor, 17-allylamono-demethoxygeldanamycin (17-AAG) was used to delineate the functional role of Hsp90.	tanespimycin	72-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
19628238-3	2009	A highly specific Hsp90 inhibitor, 17-allylamono-demethoxygeldanamycin (17-AAG) was used to delineate the functional role of Hsp90.	tanespimycin	72-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
19560353-1	2009	Structure-based virtual screening identified pyrimidine-2,4,6-trione and 4H-1,2,4-triazole-3-thiol as novel scaffolds of Hsp90 ATPase inhibitors.	pyrimidine-2,4,6-trione	45-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
19440708-1	2009	PURPOSE: 17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat-shock protein 90 (Hsp90) inhibitor, has been intensively investigated for cancer therapy and is undergoing clinical trials.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	9-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-95
19440708-1	2009	PURPOSE: 17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat-shock protein 90 (Hsp90) inhibitor, has been intensively investigated for cancer therapy and is undergoing clinical trials.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	9-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
19440708-1	2009	PURPOSE: 17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat-shock protein 90 (Hsp90) inhibitor, has been intensively investigated for cancer therapy and is undergoing clinical trials.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-95
19440708-1	2009	PURPOSE: 17-Dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat-shock protein 90 (Hsp90) inhibitor, has been intensively investigated for cancer therapy and is undergoing clinical trials.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
19440708-2	2009	Human epidermal growth factor receptor 2 (HER-2) is one of the client proteins of Hsp90 and its expression is decreased upon 17-DMAG treatment.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	125-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
19671844-4	2009	RESULTS: The novel orally administrable HSP90 inhibitor BIIB021 (CNF2024) inhibited Hodgkin"s lymphoma cell viability at low nanomolar concentrations in synergy with doxorubicin and gemcitabine.	Doxorubicin	166-177	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19671844-4	2009	RESULTS: The novel orally administrable HSP90 inhibitor BIIB021 (CNF2024) inhibited Hodgkin"s lymphoma cell viability at low nanomolar concentrations in synergy with doxorubicin and gemcitabine.	gemcitabine	182-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19610616-0	2009	Combining hit identification strategies: fragment-based and in silico approaches to orally active 2-aminothieno[2,3-d]pyrimidine inhibitors of the Hsp90 molecular chaperone.	2-aminothieno[2,3-d]pyrimidine	98-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
19610616-2	2009	Here we describe novel 2-aminothieno[2,3-d]pyrimidine ATP competitive Hsp90 inhibitors, which were designed by combining structural elements of distinct low affinity hits generated from fragment-based and in silico screening exercises in concert with structural information from X-ray protein crystallography.	2-aminothieno[2,3-d]pyrimidine	23-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
19610616-2	2009	Here we describe novel 2-aminothieno[2,3-d]pyrimidine ATP competitive Hsp90 inhibitors, which were designed by combining structural elements of distinct low affinity hits generated from fragment-based and in silico screening exercises in concert with structural information from X-ray protein crystallography.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
19082595-1	2009	PURPOSE: 17-(demethoxy), 17-allylamino geldanamycin (17-AAG) suppresses growth in some cancers by inhibiting Heat shock protein 90 (Hsp90).	17-(demethoxy	9-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-130
19082595-1	2009	PURPOSE: 17-(demethoxy), 17-allylamino geldanamycin (17-AAG) suppresses growth in some cancers by inhibiting Heat shock protein 90 (Hsp90).	17-(demethoxy	9-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
19082595-1	2009	PURPOSE: 17-(demethoxy), 17-allylamino geldanamycin (17-AAG) suppresses growth in some cancers by inhibiting Heat shock protein 90 (Hsp90).	tanespimycin	25-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-130
19082595-1	2009	PURPOSE: 17-(demethoxy), 17-allylamino geldanamycin (17-AAG) suppresses growth in some cancers by inhibiting Heat shock protein 90 (Hsp90).	tanespimycin	25-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
19082595-1	2009	PURPOSE: 17-(demethoxy), 17-allylamino geldanamycin (17-AAG) suppresses growth in some cancers by inhibiting Heat shock protein 90 (Hsp90).	tanespimycin	53-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-130
19082595-1	2009	PURPOSE: 17-(demethoxy), 17-allylamino geldanamycin (17-AAG) suppresses growth in some cancers by inhibiting Heat shock protein 90 (Hsp90).	tanespimycin	53-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
19082595-2	2009	We examined the effects of 17-AAG-mediated Hsp90 inhibition on human hepatocellular carcinoma (HCC) growth in vitro and in vivo.	tanespimycin	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
19082595-9	2009	Hsp90 inhibition by 17-AAG also decreased HCC xenograft growth in association with decreased cdc2 expression.	tanespimycin	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19082595-10	2009	CONCLUSIONS: 17-AAG-mediated inhibition of Hsp90 abrogates human HCC cell growth in vitro and in vivo through cdc2 decrease, which in turn induces G(2)/M cell cycle arrest and apoptosis.	tanespimycin	13-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
19578756-7	2009	Furthermore, cisplatin administration resulted in a Granzyme B-mediated proteolytic cleavage of Hsp90 molecular chaperone, exclusively occurring in RT4 cells.	Cisplatin	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
19671750-0	2009	Antitumor efficacy of IPI-504, a selective heat shock protein 90 inhibitor against human epidermal growth factor receptor 2-positive human xenograft models as a single agent and in combination with trastuzumab or lapatinib.	tanespimycin	22-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-64
19671750-1	2009	IPI-504 is a novel, highly soluble small-molecule inhibitor of heat shock protein 90 (Hsp90), a protein chaperone essential for regulating homeostasis of oncoproteins and cell signaling proteins.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-84
19671750-1	2009	IPI-504 is a novel, highly soluble small-molecule inhibitor of heat shock protein 90 (Hsp90), a protein chaperone essential for regulating homeostasis of oncoproteins and cell signaling proteins.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
19560353-1	2009	Structure-based virtual screening identified pyrimidine-2,4,6-trione and 4H-1,2,4-triazole-3-thiol as novel scaffolds of Hsp90 ATPase inhibitors.	mercaptotriazole	73-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
19560353-2	2009	Their binding modes in the ATP-binding pocket of Hsp90 were analyzed using AutoDoc program combined with molecular dynamics (MD) simulations.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
19552433-0	2009	Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents.	anthranilamide	19-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-71
19552433-2	2009	These indol-4-one and indazol-4-one derived 2-aminobenzamides showed strong binding affinity to Hsp90, and optimized analogues exhibited nanomolar antiproliferative activity across multiple cancer cell lines.	indol-4-one	6-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
19552433-2	2009	These indol-4-one and indazol-4-one derived 2-aminobenzamides showed strong binding affinity to Hsp90, and optimized analogues exhibited nanomolar antiproliferative activity across multiple cancer cell lines.	indazol-4-one	22-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
19552433-2	2009	These indol-4-one and indazol-4-one derived 2-aminobenzamides showed strong binding affinity to Hsp90, and optimized analogues exhibited nanomolar antiproliferative activity across multiple cancer cell lines.	anthranilamide	44-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
19607667-4	2009	Here we analysed the effects of HSP90 inhibition by geldanamycin derivative 17-AAG or RNA interference (RNAi) on aberrant Jak-STAT signaling in cHL cells.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
19607667-4	2009	Here we analysed the effects of HSP90 inhibition by geldanamycin derivative 17-AAG or RNA interference (RNAi) on aberrant Jak-STAT signaling in cHL cells.	tanespimycin	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
19410458-0	2009	Synthesis of pochoxime prodrugs as potent HSP90 inhibitors.	pochoxime	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
19410458-1	2009	Pochoximes are potent inhibitors of heat shock protein 90 (HSP90) based on the radicicol pharmacophores.	monorden	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-57
19410458-1	2009	Pochoximes are potent inhibitors of heat shock protein 90 (HSP90) based on the radicicol pharmacophores.	monorden	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
19492825-1	2009	Previously, we reported the Hsp90 inhibitory activity of radamide, an open chain amide chimera of geldanamycin and radicicol.	radamide	57-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19492825-1	2009	Previously, we reported the Hsp90 inhibitory activity of radamide, an open chain amide chimera of geldanamycin and radicicol.	Amides	60-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19492825-1	2009	Previously, we reported the Hsp90 inhibitory activity of radamide, an open chain amide chimera of geldanamycin and radicicol.	geldanamycin	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19492825-1	2009	Previously, we reported the Hsp90 inhibitory activity of radamide, an open chain amide chimera of geldanamycin and radicicol.	monorden	115-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19492825-2	2009	Attempts to further expand upon structure-activity relationships for this class of Hsp90 inhibitors led to the preparation of a series of radamide analogues focused on differing tether lengths and quinone mimics.	radamide	138-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
19492825-3	2009	In addition, the cup-shaped conformation adopted by the two natural products when bound to the Hsp90 N-terminal ATP binding pocket suggests that conformationally biased compounds may demonstrate improved binding and inhibition.	Adenosine Triphosphate	112-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
18830594-3	2009	METHOD: We investigated the effect of a DNA methyltransferase (DNMT) inhibitor, zebularine (Zeb), on the chemosensitivity of 5-FU and cisplatin (CDDP) by MTT and TUNEL methods, and compared the molecular mechanism of action with those of a GSK3beta inhibitor, LiCl, and an Hsp90 inhibitor, 17-AAG.	pyrimidin-2-one beta-ribofuranoside	80-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	273-278
19457105-5	2009	The role of calpain has been confirmed by immunoprecipitation experiments revealing that also mu-calpain is specifically recruited into the NMDA-R-nNOS-HSP90 complex following calcium loading.	Calcium	176-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
19440035-6	2009	Vorinostat also induced hyperacetylation of hsp90 and disrupted the association of hsp90 with its co-chaperones p23 and cdc37, as well as with its client proteins CDK4 and c-RAF.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
19440035-6	2009	Vorinostat also induced hyperacetylation of hsp90 and disrupted the association of hsp90 with its co-chaperones p23 and cdc37, as well as with its client proteins CDK4 and c-RAF.	Vorinostat	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
19137416-0	2009	Low concentration of GA activates a preconditioning response in HepG2 cells during oxidative stress-roles of Hsp90 and vimentin.	geldanamycin	21-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
19137416-6	2009	GA treatment leads to enhanced expression of Hsp90 and vimentin and to inhibition of vimentin protein aggregation.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
19137416-8	2009	It is confirmed that low concentrations of GA protected HepG2 cells from subsequent oxidative stress by increasing the levels of Hsp90 and by alleviating the extent of cell apoptosis induced by oxidative stress, which is similar to oxidative preconditioning.	geldanamycin	43-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
19137416-9	2009	However, in contrast to preconditioning, GA treatment obviously changed binding activity of Hsp90 to vimentin cleavages.	geldanamycin	41-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
19502802-4	2009	Here, we evaluated the initial inhibitory effects of, and the likelihood of escape from, the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and the c-Met TKI SU11274, using two cell lines harboring MET gene amplification.	tanespimycin	109-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
19441108-8	2009	PU-H71 showed potent and prolonged in vivo Hsp90 inhibitory activity and reduced tumor growth without causing toxicity.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
19441108-10	2009	Non-quinone Hsp90 inhibitors exhibit tumor-specific accumulation and exert potent antineoplastic activity without causing significant hepatotoxicity.	quinone	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
19458189-4	2009	In the present study, we show that heat-shock protein (Hsp) 90 activity is required for efficient targeting of hAgo2 to PBs and SGs.	pbs	120-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-62
19567782-5	2009	We show that geldanamycin, an Hsp90 antagonist, dramatically destabilizes newly synthesized EphA2 protein and diminishes receptor levels in a proteasome-dependent pathway.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
19329208-10	2009	LBH589 led acetylation of histone H3 and HSP90.	Panobinostat	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
19438225-6	2009	Western blotting analysis demonstrated that (-)-EGCG induced downregulation of oncogenic Hsp90 client proteins by approximately 70-95%, including Akt, Cdk4, Raf-1, Her-2, and pERK.	epigallocatechin gallate	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
19438225-7	2009	Co-immunoprecipitation showed that (-)-EGCG decreased the association of cochaperones p23 and Hsc70 with Hsp90 by more than 50%, while it had little effect on the ATP binding to Hsp90.	epigallocatechin gallate	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
19438225-8	2009	Proteolytic fingerprinting assay confirmed direct binding between (-)-EGCG and the Hsp90 C-terminal domain.	epigallocatechin gallate	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
19438225-9	2009	These data suggest that the binding of (-)-EGCG to Hsp90 impairs the association of Hsp90 with its cochaperones, thereby inducing degradation of Hsp90 client proteins, resulting antiproliferating effects in pancreatic cancer cells.	epigallocatechin gallate	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19438225-9	2009	These data suggest that the binding of (-)-EGCG to Hsp90 impairs the association of Hsp90 with its cochaperones, thereby inducing degradation of Hsp90 client proteins, resulting antiproliferating effects in pancreatic cancer cells.	epigallocatechin gallate	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
19438225-9	2009	These data suggest that the binding of (-)-EGCG to Hsp90 impairs the association of Hsp90 with its cochaperones, thereby inducing degradation of Hsp90 client proteins, resulting antiproliferating effects in pancreatic cancer cells.	epigallocatechin gallate	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
19598015-7	2009	PR rate was 50% in cases with up-regulated expression of HSP90, and 53.1% in the others with down-regulated expression of HSP90, whose difference was not significant.	Praseodymium	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
19598015-7	2009	PR rate was 50% in cases with up-regulated expression of HSP90, and 53.1% in the others with down-regulated expression of HSP90, whose difference was not significant.	Praseodymium	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
19536328-6	2009	Hsp90 can attenuate CHIP-mediated degradation and this can be blocked by the Hsp90 inhibitor geldanamycin.	geldanamycin	93-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19764559-6	2009	The inhibition of HSP70 through quercetin induced up-regulation and delayed descent of HSP90.	Quercetin	32-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
19528462-5	2009	Several Hsp90 inhibitors, including the geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17AAG), have displayed convincing antineoplastic efficacy and cancer selectivity in a variety of preclinical models, including gastrointestinal carcinomas.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
19528462-5	2009	Several Hsp90 inhibitors, including the geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17AAG), have displayed convincing antineoplastic efficacy and cancer selectivity in a variety of preclinical models, including gastrointestinal carcinomas.	tanespimycin	64-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
19528462-5	2009	Several Hsp90 inhibitors, including the geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17AAG), have displayed convincing antineoplastic efficacy and cancer selectivity in a variety of preclinical models, including gastrointestinal carcinomas.	tanespimycin	104-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
19438225-0	2009	(-)-Epigallocatechin-3-gallate inhibits Hsp90 function by impairing Hsp90 association with cochaperones in pancreatic cancer cell line Mia Paca-2.	epigallocatechin gallate	0-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19438225-0	2009	(-)-Epigallocatechin-3-gallate inhibits Hsp90 function by impairing Hsp90 association with cochaperones in pancreatic cancer cell line Mia Paca-2.	epigallocatechin gallate	0-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
19438225-2	2009	(-)-EGCG was reported to bind to the C-terminal domain of heat shock protein 90 (Hsp90).	epigallocatechin gallate	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-79
19438225-2	2009	(-)-EGCG was reported to bind to the C-terminal domain of heat shock protein 90 (Hsp90).	epigallocatechin gallate	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19438225-3	2009	The purpose of this study is to investigate (-)-EGCG as a novel Hsp90 inhibitor to impair Hsp90 superchaperone complex for simultaneous downregulation of oncogenic proteins in pancreatic cancer cells.	epigallocatechin gallate	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
19438225-3	2009	The purpose of this study is to investigate (-)-EGCG as a novel Hsp90 inhibitor to impair Hsp90 superchaperone complex for simultaneous downregulation of oncogenic proteins in pancreatic cancer cells.	epigallocatechin gallate	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
19509149-0	2009	CUDC-305, a novel synthetic HSP90 inhibitor with unique pharmacologic properties for cancer therapy.	CUDC 305	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19509149-1	2009	PURPOSE: We designed and synthesized CUDC-305, an HSP90 inhibitor of the novel imidazopyridine class.	CUDC 305	37-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
19509149-1	2009	PURPOSE: We designed and synthesized CUDC-305, an HSP90 inhibitor of the novel imidazopyridine class.	imidazopyridine	79-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
19509149-6	2009	RESULTS: CUDC-305 shows high affinity for HSP90alpha/beta (IC(50), approximately 100 nmol/L) and HSP90 complex derived from cancer cells (IC(50), 48.8 nmol/L).	CUDC 305	9-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-52
19509149-6	2009	RESULTS: CUDC-305 shows high affinity for HSP90alpha/beta (IC(50), approximately 100 nmol/L) and HSP90 complex derived from cancer cells (IC(50), 48.8 nmol/L).	CUDC 305	9-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
19494268-4	2009	Inactivation of HSP90 function using geldanamycin or radicicol inhibited MHC class II presentation of exogenous and endogenous GAD, but did not perturb the presentation of several other intra- and extracellular Ags.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
19494268-4	2009	Inactivation of HSP90 function using geldanamycin or radicicol inhibited MHC class II presentation of exogenous and endogenous GAD, but did not perturb the presentation of several other intra- and extracellular Ags.	monorden	53-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
19582223-0	2009	Measurement of nanomolar dissociation constants by titration calorimetry and thermal shift assay - radicicol binding to Hsp90 and ethoxzolamide binding to CAII.	monorden	99-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
19435295-0	2009	Design, synthesis, and biological evaluation of conformationally constrained cis-amide Hsp90 inhibitors.	cis-amide	77-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
19435295-1	2009	Conformationally constrained cis-amide chimeric inhibitors of Hsp90 have been synthesized and evaluated for their Hsp90 inhibitory activity.	cis-amide	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
19435295-1	2009	Conformationally constrained cis-amide chimeric inhibitors of Hsp90 have been synthesized and evaluated for their Hsp90 inhibitory activity.	cis-amide	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
19458065-0	2009	Targeting focal adhesion kinase with dominant-negative FRNK or Hsp90 inhibitor 17-DMAG suppresses tumor growth and metastasis of SiHa cervical xenografts.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	79-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19458065-7	2009	FAK-related nonkinase as well as the Hsp90 inhibitor 17-dimethylaminoethylamino-17-demethoxygeldanamycin both negatively interfere with FAK signaling and focal adhesion turnover.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19536328-6	2009	Hsp90 can attenuate CHIP-mediated degradation and this can be blocked by the Hsp90 inhibitor geldanamycin.	geldanamycin	93-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
19466875-0	2009	Tanespimycin: the opportunities and challenges of targeting heat shock protein 90.	tanespimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
19466875-3	2009	OBJECTIVE: Data supporting the development of tanespimycin, which targets HSP90, are reviewed.	tanespimycin	46-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
19293389-4	2009	17Beta-estradiol produced a concentration-dependent relaxation of endothelium-denuded porcine coronary arteries in vitro, and this response was attenuated by inhibiting Hsp90 function with 1 microM geldanamycin (GA) or 100 microg/ml radicicol (RAD).	Estradiol	0-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
19467916-5	2009	We discuss how the cross-talk between major downstream signaling pathways, such as PI3K/PTEN/Akt/mTOR, RAS/Raf/MEK/ERK, and Jak/STAT, can be exploited for therapeutic purposes by targeting key signaling molecules with selective inhibitors, such as mTOR inhibitors, HSP90 inhibitors, or farnesyltransferase inhibitors, and identifying those agents with the ability to positively combine with inhibitors of FLT3, such as PKC412 and sunitinib.	Sunitinib	430-439	heat shock protein 90 alpha family class A member 1	Homo sapiens	265-270
19289404-7	2009	On the other hand, Cdc25A was protected by Hsp90 in HEK293 cells because the specific inhibition of Hsp90 with Geldanamycin caused Cdc25A degradation in HEK293 implicating that Cdc25A is an Hsp90 client.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
19289404-7	2009	On the other hand, Cdc25A was protected by Hsp90 in HEK293 cells because the specific inhibition of Hsp90 with Geldanamycin caused Cdc25A degradation in HEK293 implicating that Cdc25A is an Hsp90 client.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
19289404-7	2009	On the other hand, Cdc25A was protected by Hsp90 in HEK293 cells because the specific inhibition of Hsp90 with Geldanamycin caused Cdc25A degradation in HEK293 implicating that Cdc25A is an Hsp90 client.	geldanamycin	111-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
19293389-4	2009	17Beta-estradiol produced a concentration-dependent relaxation of endothelium-denuded porcine coronary arteries in vitro, and this response was attenuated by inhibiting Hsp90 function with 1 microM geldanamycin (GA) or 100 microg/ml radicicol (RAD).	geldanamycin	198-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
19293389-4	2009	17Beta-estradiol produced a concentration-dependent relaxation of endothelium-denuded porcine coronary arteries in vitro, and this response was attenuated by inhibiting Hsp90 function with 1 microM geldanamycin (GA) or 100 microg/ml radicicol (RAD).	geldanamycin	212-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
19293389-4	2009	17Beta-estradiol produced a concentration-dependent relaxation of endothelium-denuded porcine coronary arteries in vitro, and this response was attenuated by inhibiting Hsp90 function with 1 microM geldanamycin (GA) or 100 microg/ml radicicol (RAD).	monorden	233-242	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
19293389-4	2009	17Beta-estradiol produced a concentration-dependent relaxation of endothelium-denuded porcine coronary arteries in vitro, and this response was attenuated by inhibiting Hsp90 function with 1 microM geldanamycin (GA) or 100 microg/ml radicicol (RAD).	monorden	244-247	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
19364129-7	2009	Overexpression of 14-3-3zeta in MM cells attenuated ATO-induced cell death, whereas RNAi-based 14-3-3zeta knock-down or the inhibition of HSP90 enhanced tumor cell sensitivity to the ATO induction.	Arsenic Trioxide	183-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19364129-8	2009	These observations implicate 14-3-3zeta and HSP90 as potential molecular targets for drug intervention of multiple myeloma and thus improve our understanding on the mechanisms of antitumor activity of ATO.	Arsenic Trioxide	201-204	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
19433452-2	2009	In this study, we show that an oxazoline analogue of apratoxin A (oz-apraA), a cyclodepsipeptide isolated from a marine cyanobacterium, promotes the degradation of Hsp90 clients through chaperone-mediated autophagy (CMA).	Oxazoline	31-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
19405528-1	2009	17-Allylamino-17-demethoxygeldanamycin (17-AAG) inhibits the activity of Hsp90, an important target for treatment of cancers.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
19405528-3	2009	In accordance with crystal structures reported for complexes of GDMs with Hsp90, bulky groups attached to C-11 interfered with Hsp90 binding while smaller groups such as 11-O-methyl allowed Hsp90 binding.	11-o-methyl	170-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
19405528-5	2009	Esterification of the 11-OH of 17-AAG eliminated Hsp90 binding in vitro.	11-oh	22-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
19361515-1	2009	Hsp90 chaperones contain an N-terminal ATP binding site that has been effectively targeted by competitive inhibitors.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19361515-5	2009	Here, we present side-by-side comparisons of the structures of yeast Hsp90 and mammalian GRP94, bound to the pan-Hsp90 inhibitors geldanamycin (Gdm) and radamide.	geldanamycin	130-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
19361515-5	2009	Here, we present side-by-side comparisons of the structures of yeast Hsp90 and mammalian GRP94, bound to the pan-Hsp90 inhibitors geldanamycin (Gdm) and radamide.	geldanamycin	144-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
19361515-5	2009	Here, we present side-by-side comparisons of the structures of yeast Hsp90 and mammalian GRP94, bound to the pan-Hsp90 inhibitors geldanamycin (Gdm) and radamide.	radamide	153-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
19416831-0	2009	Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19433452-2	2009	In this study, we show that an oxazoline analogue of apratoxin A (oz-apraA), a cyclodepsipeptide isolated from a marine cyanobacterium, promotes the degradation of Hsp90 clients through chaperone-mediated autophagy (CMA).	apratoxin A	53-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
19433452-2	2009	In this study, we show that an oxazoline analogue of apratoxin A (oz-apraA), a cyclodepsipeptide isolated from a marine cyanobacterium, promotes the degradation of Hsp90 clients through chaperone-mediated autophagy (CMA).	oz-apraa	66-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
19433452-6	2009	We propose that apratoxin A inhibits Hsp90 function by stabilizing the interaction of Hsp90 client proteins with Hsc70/Hsp70 and thus prevents their interactions with Hsp90.	apratoxin A	16-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19433452-6	2009	We propose that apratoxin A inhibits Hsp90 function by stabilizing the interaction of Hsp90 client proteins with Hsc70/Hsp70 and thus prevents their interactions with Hsp90.	apratoxin A	16-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
19433452-6	2009	We propose that apratoxin A inhibits Hsp90 function by stabilizing the interaction of Hsp90 client proteins with Hsc70/Hsp70 and thus prevents their interactions with Hsp90.	apratoxin A	16-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
19308924-7	2009	A 15-hydroxyl-17-demethoxy non-quinone analogue, DHQ3, exhibited stronger inhibition of Hsp90 ATPase activity (4.6-fold) than geldanamycin.	15-hydroxyl-17-demethoxy	2-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
19308924-7	2009	A 15-hydroxyl-17-demethoxy non-quinone analogue, DHQ3, exhibited stronger inhibition of Hsp90 ATPase activity (4.6-fold) than geldanamycin.	quinone	31-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
19308924-7	2009	A 15-hydroxyl-17-demethoxy non-quinone analogue, DHQ3, exhibited stronger inhibition of Hsp90 ATPase activity (4.6-fold) than geldanamycin.	dhq3	49-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
19279403-3	2009	Similar to treatment with the hsp90 inhibitor 17-DMAG, treatment with panobinostat also inhibited the chaperone association of heat shock protein 90 with DNMT1 and EZH2, which promoted the proteasomal degradation of DNMT1 and EZH2.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	46-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
19279403-3	2009	Similar to treatment with the hsp90 inhibitor 17-DMAG, treatment with panobinostat also inhibited the chaperone association of heat shock protein 90 with DNMT1 and EZH2, which promoted the proteasomal degradation of DNMT1 and EZH2.	Panobinostat	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
19383903-1	2009	The heat shock protein (HSP) 90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in clinical trials because of its unique mechanism of action and antitumor activity.	tanespimycin	42-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-31
18800240-6	2009	In addition, spherical cells were significantly more sensitive to Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin compared to flattened cells.	tanespimycin	82-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
19167484-6	2009	Interestingly, geldanamycin, an HSP90 inhibitor and non-specific Raf inhibitor, abrogated the PTP inhibitor-mediated increase in survival following Cr(VI) exposure and abolished the expression/activity of c-Raf and activity of Mek.	geldanamycin	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
19147678-6	2009	Moreover, the Hsp90 inhibitor geldanamycin (GA) disrupted the interaction between Hsp90 and the IP(3)R.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19147678-6	2009	Moreover, the Hsp90 inhibitor geldanamycin (GA) disrupted the interaction between Hsp90 and the IP(3)R.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
19147678-6	2009	Moreover, the Hsp90 inhibitor geldanamycin (GA) disrupted the interaction between Hsp90 and the IP(3)R.	geldanamycin	44-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19147678-6	2009	Moreover, the Hsp90 inhibitor geldanamycin (GA) disrupted the interaction between Hsp90 and the IP(3)R.	geldanamycin	44-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
19359180-1	2009	Hsp90 chaperone function requires traversal of a nucleotide-dependent conformational cycle, but the slow and variable rate of Hsp90-mediated ATP hydrolysis is difficult to envision as a determinant of conformational change.	Adenosine Triphosphate	141-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
19416831-4	2009	Here, we demonstrate that these tumors are sensitive to the heat shock protein 90 (Hsp90) inhibitor PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	100-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
19416831-4	2009	Here, we demonstrate that these tumors are sensitive to the heat shock protein 90 (Hsp90) inhibitor PU-H71.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	100-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
19416831-10	2009	The results identify Hsp90 as a critical and multimodal target in this most difficult to treat breast cancer subtype and support the use of the Hsp90 inhibitor PU-H71 for clinical trials involving patients with TNBC.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	160-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
19416831-10	2009	The results identify Hsp90 as a critical and multimodal target in this most difficult to treat breast cancer subtype and support the use of the Hsp90 inhibitor PU-H71 for clinical trials involving patients with TNBC.	9H-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-N-(1-methylethyl)-	160-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
19251694-11	2009	SEPT9_v1 also protected HIF-1alpha from degradation induced by HSP90 inhibition by preventing the interaction of HIF-1alpha with the RACK1 protein, which promotes its oxygen-independent proteasomal degradation.	Oxygen	167-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19143589-10	2009	In comparison, OGC (oxoglutarate carrier) lacks a presequence and was more soluble, though it is still dependent on both Hsc70 and Hsp90.	Ketoglutaric Acids	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
19301319-2	2009	Herein we report the identification of an Hsp90 inhibitor identified by fragment screening using a high-concentration biochemical assay, as well as its optimisation by in silico searching coupled with a structure-based drug design (SBDD) approach.	sbdd	232-236	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
19331414-1	2009	We describe the discovery of a novel indazole-based scaffold that represents the "first-in-class" dual Hsp90/tubulin binding compound.	Indazoles	37-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
19371599-5	2009	siRNA-mediated attenuation of the expression of the inducible isoform of HSP70 (HSP70i) or HSP90alpha/beta also enhanced ATO-induced apoptosis.	Arsenic Trioxide	121-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-101
19372565-2	2009	BIIB021 is a novel, fully synthetic inhibitor of Hsp90 that binds competitively with geldanamycin in the ATP-binding pocket of Hsp90.	geldanamycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
19159681-0	2009	Hsp90 and a tyrosine embedded in the Hsp90 recognition loop are required for the Fer tyrosine kinase activity.	Tyrosine	12-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
19159681-5	2009	Mutation analysis unveiled a tyrosine (Tyr(616)) embedded in the Hsp90 recognition loop, which is required for the kinase activity of Fer.	Tyrosine	29-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
19159681-5	2009	Mutation analysis unveiled a tyrosine (Tyr(616)) embedded in the Hsp90 recognition loop, which is required for the kinase activity of Fer.	Tyrosine	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
19162015-3	2009	The ansamycins, such as geldanamycin and 17-allylamino-17-demethoxygeldanamycin (17-AAG) act as specific HSP90 inhibitors, are potent anti-tumor agents and are currently undergoing clinical trials.	Lactams, Macrocyclic	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
19162015-3	2009	The ansamycins, such as geldanamycin and 17-allylamino-17-demethoxygeldanamycin (17-AAG) act as specific HSP90 inhibitors, are potent anti-tumor agents and are currently undergoing clinical trials.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
19162015-3	2009	The ansamycins, such as geldanamycin and 17-allylamino-17-demethoxygeldanamycin (17-AAG) act as specific HSP90 inhibitors, are potent anti-tumor agents and are currently undergoing clinical trials.	tanespimycin	41-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
19162015-5	2009	Geldanamycin, 17-AAG and another chemically unrelated HSP90 inhibitor, radicicol, were extremely cytotoxic for OPCs.	monorden	71-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
19158250-5	2009	Here, Hsp90 overexpression restored IKK1 levels in MC160-expressing cells, suggesting that MC160 competitively interacted with Hsp90.	mc160	51-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
19414399-7	2009	EGCG decreased the protein levels of Bcl-2, Bcl-xl, xIAP, cIAP, Hsp70 and Hsp90, but increased the protein expression of Bad, Bax, Fas/CD95, cytochrome c, Apaf-1, AIF, GADD153, GRP78, and caspase-3, -7,-8 and -9 as observed by Western blotting examination.	epigallocatechin gallate	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
19372565-2	2009	BIIB021 is a novel, fully synthetic inhibitor of Hsp90 that binds competitively with geldanamycin in the ATP-binding pocket of Hsp90.	geldanamycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
19372565-2	2009	BIIB021 is a novel, fully synthetic inhibitor of Hsp90 that binds competitively with geldanamycin in the ATP-binding pocket of Hsp90.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
19372565-2	2009	BIIB021 is a novel, fully synthetic inhibitor of Hsp90 that binds competitively with geldanamycin in the ATP-binding pocket of Hsp90.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
18682579-4	2009	17-allylamino-17-demethoxygeldanamycin (17-AAG) is a well-characterized HSP90 inhibitor that should be able to target many of the aberrant signal transduction pathways in GBM.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
19244114-1	2009	Heat shock protein 90 (HSP90) inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin), which is currently in phase II/phase III clinical trials, are promising new anticancer agents.	tanespimycin	50-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	monorden	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	monorden	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	monorden	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	monorden	75-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	108-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	108-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	108-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	108-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19150985-2	2009	Here, we report a new and effective strategy for inhibiting HCV replication using 17-allylaminogeldanamycin (17-AAG), an inhibitor of heat-shock protein 90 (Hsp90).	tanespimycin	82-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
19150985-2	2009	Here, we report a new and effective strategy for inhibiting HCV replication using 17-allylaminogeldanamycin (17-AAG), an inhibitor of heat-shock protein 90 (Hsp90).	tanespimycin	109-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
19150985-7	2009	These results suggest that the suppression of HCV RNA replication is due to the destabilization of NS3 in disruption of the Hsp90 chaperone complex by 17-AAG.	tanespimycin	151-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
19136580-7	2009	Hsp90 antagonism with radicicol induced greatest constriction in PRA from 12-day-old piglets.	monorden	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19136580-9	2009	Hsp90 inhibition abolished ACh-mediated dilation in PRA from the older piglets.	Acetylcholine	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19136580-10	2009	ACh failed to stimulate Hsp90-eNOS binding in 2-day-old but induced a significant increase in Hsp90-eNOS coimmunoprecipitation in PRA from the older age groups, which was blocked by Hsp90 antagonism.	Acetylcholine	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
19136580-10	2009	ACh failed to stimulate Hsp90-eNOS binding in 2-day-old but induced a significant increase in Hsp90-eNOS coimmunoprecipitation in PRA from the older age groups, which was blocked by Hsp90 antagonism.	Acetylcholine	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
19320098-8	2009	Upon exposure of the set of Hsp90 test strains to the two Hsp90 inhibitors radicicol (Rd) and geldanamycin (GA), we found that the strain with Pf Hsp90 is relatively more sensitive to GA than to Rd compared to the strains with human Hsp90"s.	geldanamycin	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19017562-2	2009	While compounds with different modes of action are known, the focus of this review is on those classes of compounds which inhibit Hsp90 by binding to the N-terminal ATP pocket.	Adenosine Triphosphate	165-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
18726712-5	2009	Geldanamycin (GA), an HSP90 inhibitor, decreased the expression of HIF-1alpha in NPCs during hypoxia-driven proliferation and reduced the expression level of HIF-1alpha protein under hypoxia in a time-dependent manner.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
18726712-5	2009	Geldanamycin (GA), an HSP90 inhibitor, decreased the expression of HIF-1alpha in NPCs during hypoxia-driven proliferation and reduced the expression level of HIF-1alpha protein under hypoxia in a time-dependent manner.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
18726712-6	2009	The proliferation of NPCs induced by hypoxia was inhibited after GA treatment for 24 h. Another HSP90 inhibitor, radicicol, had the same effect on NPCs as GA.	monorden	113-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
19220840-0	2009	5,7-dihydroxy-3,4,6-trimethoxyflavone inhibits the inflammatory effects induced by Bacteroides fragilis enterotoxin via dissociating the complex of heat shock protein 90 and I kappaB alpha and I kappaB kinase-gamma in intestinal epithelial cell culture.	eupatilin	0-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-169
19220840-7	2009	In addition, herbimycin A, a specific inhibitor of heat shock protein 90 (Hsp90), decreased the BFT-induced activation of IKK and NF-kappaB, suggesting that Hsp90 is associated with a pathway of IKK-NF-kappaB-IL-8/cyclo-oxygenase-2 gene signalling.	herbimycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
19220840-7	2009	In addition, herbimycin A, a specific inhibitor of heat shock protein 90 (Hsp90), decreased the BFT-induced activation of IKK and NF-kappaB, suggesting that Hsp90 is associated with a pathway of IKK-NF-kappaB-IL-8/cyclo-oxygenase-2 gene signalling.	herbimycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
19220840-7	2009	In addition, herbimycin A, a specific inhibitor of heat shock protein 90 (Hsp90), decreased the BFT-induced activation of IKK and NF-kappaB, suggesting that Hsp90 is associated with a pathway of IKK-NF-kappaB-IL-8/cyclo-oxygenase-2 gene signalling.	herbimycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
19220840-8	2009	Furthermore, eupatilin dissociated the complex between Hsp90 and IKK-gamma in BFT-stimulated HT-29 cells.	eupatilin	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
19244114-1	2009	Heat shock protein 90 (HSP90) inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin), which is currently in phase II/phase III clinical trials, are promising new anticancer agents.	tanespimycin	50-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
19244114-1	2009	Heat shock protein 90 (HSP90) inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin), which is currently in phase II/phase III clinical trials, are promising new anticancer agents.	tanespimycin	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
19244114-1	2009	Heat shock protein 90 (HSP90) inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin), which is currently in phase II/phase III clinical trials, are promising new anticancer agents.	tanespimycin	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
19234166-9	2009	Our studies also show that the ability of RIG-I to respond to stimulation with polyinosinic:polycytidylic acid is abolished when its interaction with HSP90 is inhibited.	Poly C	92-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
19300478-2	2009	ATP binding and hydrolysis facilitate Hsp90 conformational changes required for client activation.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
19229106-5	2009	Here, we report the synthesis and properties of Gamitrinibs, a class of small molecules designed to selectively target Hsp90 in human tumor mitochondria.	gamitrinibs	48-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
19229106-6	2009	Gamitrinibs were shown to accumulate in the mitochondria of human tumor cell lines and to inhibit Hsp90 activity by acting as ATPase antagonists.	gamitrinibs	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
19187436-3	2009	Treatment of SH-SY5Y neuroblastoma cells and human embryonic kidney cells with the HSP90 inhibitors novobiocin and geldanamycin caused substantial decreases in the level of Akt in the mitochondria without affecting the level of Akt in the cytosol.	Novobiocin	100-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
19187436-3	2009	Treatment of SH-SY5Y neuroblastoma cells and human embryonic kidney cells with the HSP90 inhibitors novobiocin and geldanamycin caused substantial decreases in the level of Akt in the mitochondria without affecting the level of Akt in the cytosol.	geldanamycin	115-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
19234467-0	2009	Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.	Adenosine Triphosphate	18-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
19234467-1	2009	The molecular chaperone heat-shock protein 90 (Hsp90) couples ATP hydrolysis to conformational changes driving a reaction cycle that is required for substrate activation.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-45
19234467-1	2009	The molecular chaperone heat-shock protein 90 (Hsp90) couples ATP hydrolysis to conformational changes driving a reaction cycle that is required for substrate activation.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19091746-13	2009	These Hsp90-binding regions, however, are tethered to the C-terminal tail via a "molecular clamp" formed between the PXXP motif and a conserved Tyr (Tyr-446) in the alphaE-helix.	Tyrosine	144-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
19091746-13	2009	These Hsp90-binding regions, however, are tethered to the C-terminal tail via a "molecular clamp" formed between the PXXP motif and a conserved Tyr (Tyr-446) in the alphaE-helix.	Tyrosine	149-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
19306500-5	2009	report the synthesis of Gamitrinibs, which target mitochondrially localized HSP90, specifically killing human cancer cell lines, and provide a fresh approach for cancer treatment.	gamitrinibs	24-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
18984579-12	2009	Consistent with these results, a significant reduction in HepG2.2.15 HBV secretion was observed when the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin was used to treat HepG2.2.15 cells.	tanespimycin	121-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
19196973-4	2009	For the most prevalent fungal pathogen of humans, Candida albicans, Hsp90 mediates resistance to azoles, which inhibit ergosterol biosynthesis and are the most widely deployed antifungals in the clinic.	Azoles	97-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
19196973-4	2009	For the most prevalent fungal pathogen of humans, Candida albicans, Hsp90 mediates resistance to azoles, which inhibit ergosterol biosynthesis and are the most widely deployed antifungals in the clinic.	Ergosterol	119-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
19196973-5	2009	For the emerging opportunistic pathogen Aspergillus terreus, Hsp90 is required for basal resistance to echinocandins, which inhibit beta(1, 3)-glucan synthesis and are the only new class of antifungals to reach the clinic in decades.	Echinocandins	103-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
19196973-5	2009	For the emerging opportunistic pathogen Aspergillus terreus, Hsp90 is required for basal resistance to echinocandins, which inhibit beta(1, 3)-glucan synthesis and are the only new class of antifungals to reach the clinic in decades.	beta-1,3-glucan	132-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
19196973-7	2009	Combination therapy with Hsp90 inhibitors that are well tolerated in humans and an azole rescued larvae from lethal C. albicans infections.	Azoles	83-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
19196973-9	2009	In a murine model of disseminated candidiasis, genetic compromise of C. albicans HSP90 expression enhanced the therapeutic efficacy of an azole.	Azoles	138-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19168355-0	2009	5-Aryl-4-(5-substituted-2,4-dihydroxyphenyl)-1,2,3-thiadiazoles as inhibitors of Hsp90 chaperone.	5-aryl-4-(5-substituted-2,4-dihydroxyphenyl)-1,2,3-thiadiazoles	0-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
19168355-1	2009	A series of 5-aryl-4-(5-substituted-2,4-dihydroxyphenyl)-1,2,3-thiadiazoles were synthesized and their binding to several constructs of human Hsp90 chaperone measured by isothermal titration calorimetry (ITC).	5-aryl-4-(5-substituted-2,4-dihydroxyphenyl)-1,2,3-thiadiazoles	12-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
19176399-7	2009	Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells.	tanespimycin	32-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19176399-7	2009	Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells.	tanespimycin	32-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
19176399-7	2009	Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells.	tanespimycin	32-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
19176399-7	2009	Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells.	deguelin	74-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19176399-7	2009	Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells.	deguelin	74-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
19176399-7	2009	Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells.	deguelin	74-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
18842335-0	2009	Antiproliferative and apoptotic activities of tosylcyclonovobiocic acids as potent heat shock protein 90 inhibitors in human cancer cells.	tosylcyclonovobiocic acids	46-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
18842335-1	2009	We evaluated whether inhibition of heat shock protein 90 (hsp90) function by novobiocin derivatives could induce the degradation of signal transducers that drive cancer cell growth and thereby promote apoptosis.	Novobiocin	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-56
18842335-1	2009	We evaluated whether inhibition of heat shock protein 90 (hsp90) function by novobiocin derivatives could induce the degradation of signal transducers that drive cancer cell growth and thereby promote apoptosis.	Novobiocin	77-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19113837-6	2009	Hsp90 chaperone function, as assessed by its ability to mediate refolding of denatured luciferase, was inhibited by EGCG treatment.	epigallocatechin gallate	116-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19118525-0	2009	Tosylcyclonovobiocic acids promote cleavage of the hsp90-associated cochaperone p23.	tosylcyclonovobiocic acids	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19118525-2	2009	Tosylcyclonovobiocic acids (4TCNA and 7TCNA) are potent analogs of novobiocin and induce cell cycle arrest, apoptosis and degradation of hsp90 client proteins in a panel of cancer cells.	tosylcyclonovobiocic acids	0-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
19118525-2	2009	Tosylcyclonovobiocic acids (4TCNA and 7TCNA) are potent analogs of novobiocin and induce cell cycle arrest, apoptosis and degradation of hsp90 client proteins in a panel of cancer cells.	4tcna	28-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
19118525-2	2009	Tosylcyclonovobiocic acids (4TCNA and 7TCNA) are potent analogs of novobiocin and induce cell cycle arrest, apoptosis and degradation of hsp90 client proteins in a panel of cancer cells.	7tcna	38-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
19014912-3	2009	In this paper, we investigated whether an oxidative stress generated during ascorbate-driven menadione redox cycling (ascorbate/menadione), affects Hsp90 leading to the degradation of some critical proteins and cell death.	Ascorbic Acid	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
19014912-3	2009	In this paper, we investigated whether an oxidative stress generated during ascorbate-driven menadione redox cycling (ascorbate/menadione), affects Hsp90 leading to the degradation of some critical proteins and cell death.	Vitamin K 3	93-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
19014912-3	2009	In this paper, we investigated whether an oxidative stress generated during ascorbate-driven menadione redox cycling (ascorbate/menadione), affects Hsp90 leading to the degradation of some critical proteins and cell death.	Ascorbic Acid	118-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
19014912-3	2009	In this paper, we investigated whether an oxidative stress generated during ascorbate-driven menadione redox cycling (ascorbate/menadione), affects Hsp90 leading to the degradation of some critical proteins and cell death.	Vitamin K 3	128-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
19014912-4	2009	Unlike 17-AAG, which inhibits Hsp90 but enhances Hsp70 levels, ascorbate/menadione-treated cells present an additional Hsp90 protein band of about 70kDa as shown by Western blot analysis, suggesting Hsp90 cleavage.	Ascorbic Acid	63-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
19036086-0	2009	The heat shock protein 90 inhibitor IPI-504 induces apoptosis of AKT-dependent diffuse large B-cell lymphomas.	tanespimycin	36-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-25
19036086-4	2009	Thereafter, we assessed the activity of the HSP90 inhibitor, IPI-504, in an extensive panel of DLBCL cell lines.	tanespimycin	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
19036086-5	2009	IPI-504, which interacts with the conserved ATP-binding site in both HSP90 isoforms, inhibited proliferation and induced apoptosis in the majority of DLBCL cell lines at low micromolar concentrations.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
19036086-5	2009	IPI-504, which interacts with the conserved ATP-binding site in both HSP90 isoforms, inhibited proliferation and induced apoptosis in the majority of DLBCL cell lines at low micromolar concentrations.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
19036086-6	2009	IPI-504-sensitive cell lines expressed high levels of the HSP90 client protein, pAKT, and exhibited dose-dependent decreases in pAKT levels following IPI-504 treatment and significantly reduced proliferation following AKT RNAi.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19036086-6	2009	IPI-504-sensitive cell lines expressed high levels of the HSP90 client protein, pAKT, and exhibited dose-dependent decreases in pAKT levels following IPI-504 treatment and significantly reduced proliferation following AKT RNAi.	tanespimycin	150-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
19036086-9	2009	The HSP90 inhibitor IPI-504 warrants further investigation in DLBCL alone and in combination with identified client protein inhibitors and active chemotherapeutic agents.	tanespimycin	20-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
19179103-3	2009	Current Hsp90 inhibitors are categorized into several classes based on distinct modes of inhibition, including (i) blockade of ATP binding, (ii) disruption of co-chaperone/Hsp90 interactions, (iii) antagonism of client/Hsp90 associations and (iv) interference with post-translational modifications of Hsp90.	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
19236263-6	2009	METHODS: The latest evidence regarding the use of geldanamycin analogues or newer water-soluble and synthetics molecules that inhibit the binding of HSP90 to client proteins was reviewed.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
19236263-6	2009	METHODS: The latest evidence regarding the use of geldanamycin analogues or newer water-soluble and synthetics molecules that inhibit the binding of HSP90 to client proteins was reviewed.	Water	82-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
19148492-3	2009	We used 17-AAG to inhibit Hsp90 and rapamycin to inhibit mTOR, in the osteosarcoma cell lines, HOS and KHOS/NP.	tanespimycin	8-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
19084447-4	2009	The natural antibiotic Geldanamycin is the first Hsp90 inhibitor that has been identified.	geldanamycin	23-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
19084447-5	2009	Nevertheless, more potent and water-soluble small molecules are currently in development, and many X-ray crystallographic structures of Hsp90-inhibitor complexes are available for drug discovery purposes.	Water	30-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
18950863-4	2009	The results showed that the specific inhibitor geldanamycin (GA) of Hsp90 dramatically inhibited IL-1beta stimulated TAK1-MAPKs and TAK1-nuclear factor-kappaB (NF-kappaB) activation, resulting in the decrease of cyclooxygenase-2 (COX-2) protein expression.	geldanamycin	47-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
18950863-4	2009	The results showed that the specific inhibitor geldanamycin (GA) of Hsp90 dramatically inhibited IL-1beta stimulated TAK1-MAPKs and TAK1-nuclear factor-kappaB (NF-kappaB) activation, resulting in the decrease of cyclooxygenase-2 (COX-2) protein expression.	geldanamycin	61-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
18948577-0	2009	SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis in multiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK.	SNX 2112	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
18948577-2	2009	Here we investigate the biologic significance of Hsp90 inhibition in multiple myeloma (MM) and other hematologic tumors using an orally available novel small molecule inhibitor SNX-2112, which exhibits unique activities relative to 17-allyamino-17-demethoxy-geldanamycin (17-AAG).	SNX 2112	177-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
18948577-8	2009	Our results indicate that blockade of Hsp90 by SNX-2112 not only inhibits MM cell growth but also acts in the bone marrow microenvironment to block angiogenesis and osteoclastogenesis.	SNX 2112	47-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
19193894-6	2009	Furthermore, geldanamycin, an HSP90 inhibitor, not only prevented resecretion of eSNCA but also attenuated neurotoxicity induced by eSNCA.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
19194158-9	2009	Isoflurane increased nitric oxide production in human coronary artery endothelial cells concomitantly with an increase in Hsp90-eNOS interaction (immunoprecipitation, immunoblotting, and immunohistochemistry).	Isoflurane	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
19194158-10	2009	Pretreatment with Hsp90 inhibitors abolished isoflurane-dependent nitric oxide production and decreased Hsp90-eNOS interactions.	Isoflurane	45-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
19194158-10	2009	Pretreatment with Hsp90 inhibitors abolished isoflurane-dependent nitric oxide production and decreased Hsp90-eNOS interactions.	Nitric Oxide	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
19014912-4	2009	Unlike 17-AAG, which inhibits Hsp90 but enhances Hsp70 levels, ascorbate/menadione-treated cells present an additional Hsp90 protein band of about 70kDa as shown by Western blot analysis, suggesting Hsp90 cleavage.	Ascorbic Acid	63-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
19014912-4	2009	Unlike 17-AAG, which inhibits Hsp90 but enhances Hsp70 levels, ascorbate/menadione-treated cells present an additional Hsp90 protein band of about 70kDa as shown by Western blot analysis, suggesting Hsp90 cleavage.	Ascorbic Acid	63-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
19014912-4	2009	Unlike 17-AAG, which inhibits Hsp90 but enhances Hsp70 levels, ascorbate/menadione-treated cells present an additional Hsp90 protein band of about 70kDa as shown by Western blot analysis, suggesting Hsp90 cleavage.	Vitamin K 3	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
19014912-4	2009	Unlike 17-AAG, which inhibits Hsp90 but enhances Hsp70 levels, ascorbate/menadione-treated cells present an additional Hsp90 protein band of about 70kDa as shown by Western blot analysis, suggesting Hsp90 cleavage.	Vitamin K 3	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
19014912-9	2009	Both Hsp90 cleavage and Bcr-Abl degradation were observed by incubating K562 cells with another H(2)O(2)-generating system (glucose/glucose oxidase) and by incubating KU812 cells (another leukemia cell line) with ascorbate/menadione.	Ascorbic Acid	213-222	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
19014912-9	2009	Both Hsp90 cleavage and Bcr-Abl degradation were observed by incubating K562 cells with another H(2)O(2)-generating system (glucose/glucose oxidase) and by incubating KU812 cells (another leukemia cell line) with ascorbate/menadione.	Vitamin K 3	223-232	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
19148492-11	2009	Rapamycin also down-regulated the activity of p70S6, pAkt and p-mTOR, but had no effect on pGSK-3beta, p44Erk, pCdc2, TSC1/2 or Hsp70 or Hsp90.	Sirolimus	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
19142186-0	2009	Hsp90 is expressed and represents a therapeutic target in human oesophageal cancer using the inhibitor 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	103-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19113837-7	2009	Hsp90 dimerization, which occurs at the C-terminal end, was also inhibited by EGCG treatment.	epigallocatechin gallate	78-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19113837-8	2009	Coimmunoprecipitation studies showed that EGCG stabilizes an AhR complex that includes hsp90 and XAP2 (hepatitis B virus X-associated protein 2), and decreases the association of aryl hydrocarbon nuclear translocator (Arnt) with ligand-activated AhR.	epigallocatechin gallate	42-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
19113837-9	2009	Thus, EGCG, through its ability to bind to hsp90, blocks AhR response element (AhRE) recognition.	epigallocatechin gallate	6-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
19113837-11	2009	In EGCG-treated human ovarian carcinoma SKOV3 cells, decreased levels of several cancer-related hsp90 client proteins, such as ErbB2, Raf-1 and phospho-AKT, were observed.	epigallocatechin gallate	3-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
19113837-12	2009	EGCG also modified the association of hsp90 with several cochaperones.	epigallocatechin gallate	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
19113837-13	2009	Overall, these data indicate that EGCG is a novel hsp90 inhibitor.	epigallocatechin gallate	34-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
18977205-4	2009	We show that in the colon cancer cells HT-29 the inhibition of the chaperone function of Hsp90 by geldanamycin (GA) enhances the ubiquitinylation of cyclin E and triggers active degradation via the proteasome pathway.	geldanamycin	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
19028451-5	2009	IL-8 up-regulation in response to HSP90 was also attenuated by IkappaB, rasveratrol, curcumin, diphenyleneiodium, N-acetylcystein, U0126, and SB202190.	rasveratrol	72-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19028451-5	2009	IL-8 up-regulation in response to HSP90 was also attenuated by IkappaB, rasveratrol, curcumin, diphenyleneiodium, N-acetylcystein, U0126, and SB202190.	Curcumin	85-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19028451-5	2009	IL-8 up-regulation in response to HSP90 was also attenuated by IkappaB, rasveratrol, curcumin, diphenyleneiodium, N-acetylcystein, U0126, and SB202190.	diphenyleneiodium	95-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19028451-5	2009	IL-8 up-regulation in response to HSP90 was also attenuated by IkappaB, rasveratrol, curcumin, diphenyleneiodium, N-acetylcystein, U0126, and SB202190.	N-Acetyl-L-cysteine	114-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19028451-5	2009	IL-8 up-regulation in response to HSP90 was also attenuated by IkappaB, rasveratrol, curcumin, diphenyleneiodium, N-acetylcystein, U0126, and SB202190.	U 0126	131-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19028451-5	2009	IL-8 up-regulation in response to HSP90 was also attenuated by IkappaB, rasveratrol, curcumin, diphenyleneiodium, N-acetylcystein, U0126, and SB202190.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	142-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
19101151-0	2009	Synthesis and evaluation of Hsp90 inhibitors that contain the 1,4-naphthoquinone scaffold.	1,4-naphthoquinone	62-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19101151-1	2009	High-throughput screening of a library of diverse molecules has identified the 1,4-naphthoquinone scaffold as a new class of Hsp90 inhibitors.	1,4-naphthoquinone	79-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
19101151-5	2009	The identification of these naphthoquinones as Hsp90 inhibitors provides a new scaffold upon which improved Hsp90 inhibitors can be developed.	Naphthoquinones	28-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
19101151-5	2009	The identification of these naphthoquinones as Hsp90 inhibitors provides a new scaffold upon which improved Hsp90 inhibitors can be developed.	Naphthoquinones	28-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
18931700-7	2009	Furthermore, combining CDC37 silencing with the HSP90 inhibitor 17-AAG induced more extensive and sustained depletion of kinase clients and potentiated cell cycle arrest and apoptosis.	tanespimycin	64-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
18992762-5	2009	CDDP significantly increased renal abundances of HO-1, HSP60, HSP72 and HSP90 at days 1, 3, and 5.	Cisplatin	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
18793708-1	2009	17-Allylamino-17-demethoxy geldanamycin (17-AAG), an inhibitor of heat shock protein 90 (Hsp90) function, is being developed as antitumor drug in patients with breast cancer.	tanespimycin	0-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-87
18793708-1	2009	17-Allylamino-17-demethoxy geldanamycin (17-AAG), an inhibitor of heat shock protein 90 (Hsp90) function, is being developed as antitumor drug in patients with breast cancer.	tanespimycin	0-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
19113837-0	2009	(-)-Epigallocatechin-3-gallate is a novel Hsp90 inhibitor.	epigallocatechin gallate	0-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
19113837-3	2009	Unlike other AhR antagonists that directly bind to the AhR, EGCG inhibits AhR-mediated transcription by binding to hsp90.	epigallocatechin gallate	60-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
19113837-4	2009	We hypothesize that EGCG exerts anti-AhR and anticancer effects by acting as an hsp90 inhibitor.	epigallocatechin gallate	20-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
19113837-5	2009	Using proteolytic footprinting, immunoprecipitation, and an ATP-agarose pull-down assay, EGCG was found to directly modulate the conformation of hsp90 and bind at or near to a C-terminal ATP binding site.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
19113837-5	2009	Using proteolytic footprinting, immunoprecipitation, and an ATP-agarose pull-down assay, EGCG was found to directly modulate the conformation of hsp90 and bind at or near to a C-terminal ATP binding site.	epigallocatechin gallate	89-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
18977205-4	2009	We show that in the colon cancer cells HT-29 the inhibition of the chaperone function of Hsp90 by geldanamycin (GA) enhances the ubiquitinylation of cyclin E and triggers active degradation via the proteasome pathway.	geldanamycin	112-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
19585625-0	2009	Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol.	Triterpenes	111-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19585625-0	2009	Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol.	celastrol	122-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
19560753-2	2009	Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90.	Adenosine Triphosphate	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18945937-0	2009	High glucose-induced IKK-Hsp-90 interaction contributes to endothelial dysfunction.	Glucose	5-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-31
18945937-4	2009	In this study, we have investigated the interaction of Hsp-90-IKKbeta in endothelial cells under conditions of high glucose (HG) as a possible mechanism that diminishes Hsp-90-eNOS interaction, which could contribute to reduced bioavailability of NO.	Glucose	116-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-61
18945937-4	2009	In this study, we have investigated the interaction of Hsp-90-IKKbeta in endothelial cells under conditions of high glucose (HG) as a possible mechanism that diminishes Hsp-90-eNOS interaction, which could contribute to reduced bioavailability of NO.	Glucose	116-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-175
18945937-8	2009	Inhibition of Hsp-90 with geldanamycin (2 microM) or Radicicol (20 microM) mitigated (0.45 +/- 0.04-fold and 0.93 +/- 0.16-fold, respectively) HG induced-IKKbeta activity (2.5 +/- 0.42-fold).	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-20
18945937-9	2009	Blocking of IKKbeta expression by IKK inhibitor II (15 microM wedelolactone) or small interferring RNA (siRNA) improved Hsp-90-eNOS interaction and NO production under conditions of HG.	wedelolactone	62-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-126
19689285-5	2009	Development of HSP90 inhibitors, derived from the natural compound geldanamycin that mimics the ATP binding site of HSP90, was designed to target HSP90 and allow degradation of these client proteins.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
19689285-5	2009	Development of HSP90 inhibitors, derived from the natural compound geldanamycin that mimics the ATP binding site of HSP90, was designed to target HSP90 and allow degradation of these client proteins.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
19689285-5	2009	Development of HSP90 inhibitors, derived from the natural compound geldanamycin that mimics the ATP binding site of HSP90, was designed to target HSP90 and allow degradation of these client proteins.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
19689285-5	2009	Development of HSP90 inhibitors, derived from the natural compound geldanamycin that mimics the ATP binding site of HSP90, was designed to target HSP90 and allow degradation of these client proteins.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
19689285-5	2009	Development of HSP90 inhibitors, derived from the natural compound geldanamycin that mimics the ATP binding site of HSP90, was designed to target HSP90 and allow degradation of these client proteins.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
19689285-5	2009	Development of HSP90 inhibitors, derived from the natural compound geldanamycin that mimics the ATP binding site of HSP90, was designed to target HSP90 and allow degradation of these client proteins.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
19560753-2	2009	Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90.	Adenosine Triphosphate	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
19560753-2	2009	Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90.	Adenosine Triphosphate	129-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
19560753-2	2009	Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90.	Adenosine Diphosphate	133-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19560753-2	2009	Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90.	Adenosine Diphosphate	133-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
19560753-2	2009	Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90.	Adenosine Diphosphate	133-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
19560753-6	2009	A selective inhibitor of Hsp90, geldanamycin (GA), shortened MEKK3 half-life, and induced ubiquitination and proteasomal degradation of MEKK3.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
19560753-6	2009	A selective inhibitor of Hsp90, geldanamycin (GA), shortened MEKK3 half-life, and induced ubiquitination and proteasomal degradation of MEKK3.	geldanamycin	46-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
19082486-4	2009	Doxorubicin induced dose-dependent G2/M and/or G1/S cell cycle arrest, followed by grade- and dose-dependent reduction in the amount of the cytosolic trimeric form of FasL, activation of Caspase-8, Caspase-9, Caspase-3, cleavage of PARP, Lamin A/C, Bcl-XL/S and interestingly Hsp90, and finally cell death.	Doxorubicin	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	276-281
19860729-5	2009	It further summarizes various high throughput assays (and secondary confirmatory assays) developed to identify new Hsp90 inhibitors from chemical libraries based on the inhibitors ability to: inhibit Hsp90"s ATPase activity; compete for ligand binding to Hsp90 and its N-terminal ATP-binding domain; inhibit Hsp90-dependent refolding of denatured luciferase; and deplete culture cells of Hsp90-dependnet client protein or induce Hsp70 expression.	Adenosine Triphosphate	208-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
19860729-5	2009	It further summarizes various high throughput assays (and secondary confirmatory assays) developed to identify new Hsp90 inhibitors from chemical libraries based on the inhibitors ability to: inhibit Hsp90"s ATPase activity; compete for ligand binding to Hsp90 and its N-terminal ATP-binding domain; inhibit Hsp90-dependent refolding of denatured luciferase; and deplete culture cells of Hsp90-dependnet client protein or induce Hsp70 expression.	Adenosine Triphosphate	208-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
19860729-5	2009	It further summarizes various high throughput assays (and secondary confirmatory assays) developed to identify new Hsp90 inhibitors from chemical libraries based on the inhibitors ability to: inhibit Hsp90"s ATPase activity; compete for ligand binding to Hsp90 and its N-terminal ATP-binding domain; inhibit Hsp90-dependent refolding of denatured luciferase; and deplete culture cells of Hsp90-dependnet client protein or induce Hsp70 expression.	Adenosine Triphosphate	208-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
19860729-5	2009	It further summarizes various high throughput assays (and secondary confirmatory assays) developed to identify new Hsp90 inhibitors from chemical libraries based on the inhibitors ability to: inhibit Hsp90"s ATPase activity; compete for ligand binding to Hsp90 and its N-terminal ATP-binding domain; inhibit Hsp90-dependent refolding of denatured luciferase; and deplete culture cells of Hsp90-dependnet client protein or induce Hsp70 expression.	Adenosine Triphosphate	208-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
19860729-5	2009	It further summarizes various high throughput assays (and secondary confirmatory assays) developed to identify new Hsp90 inhibitors from chemical libraries based on the inhibitors ability to: inhibit Hsp90"s ATPase activity; compete for ligand binding to Hsp90 and its N-terminal ATP-binding domain; inhibit Hsp90-dependent refolding of denatured luciferase; and deplete culture cells of Hsp90-dependnet client protein or induce Hsp70 expression.	Adenosine Triphosphate	208-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
19860731-3	2009	All of these agents inhibit Hsp90"s protein folding activity by binding to the N-terminal ATP binding site of the Hsp90 molecular chaperone.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
19860731-3	2009	All of these agents inhibit Hsp90"s protein folding activity by binding to the N-terminal ATP binding site of the Hsp90 molecular chaperone.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
19860732-0	2009	Purine-scaffold Hsp90 inhibitors.	purine	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
19860732-5	2009	This review focuses on the purine class of Hsp90 inhibitors, their discovery through rational design, and on efforts aimed towards their optimization and development into clinically viable drugs for the treatment of cancer.	purine	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
19860733-0	2009	Hsp90 inhibition with resorcyclic acid lactones (RALs).	resorcyclic acid lactones	22-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19860733-1	2009	Heat shock protein 90 (Hsp90) is an ATP-dependent chaperone which is involved in the post-translational maturation and stabilization of over one hundred proteins ("its clients").	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
19860733-1	2009	Heat shock protein 90 (Hsp90) is an ATP-dependent chaperone which is involved in the post-translational maturation and stabilization of over one hundred proteins ("its clients").	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
19860734-0	2009	Ansamycin inhibitors of Hsp90: nature"s prototype for anti-chaperone therapy.	Rifabutin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
19032597-2	2009	In contrast, ATP utilization by human Hsp90s is less well studied, and appears to operate differently.	Adenosine Triphosphate	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
19032597-7	2009	Mutation of residues implicated in N-terminal dimerization of yeast Hsp90 (L15R and L18R in yeast, L24R and L27R in humans) significantly reduced the ATPase activity of yeast and human Hsp90s, showing that ATP-dependent association of the N-terminal domains in the Hsp90 dimer is also essential in both systems.	Adenosine Triphosphate	150-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
19032597-7	2009	Mutation of residues implicated in N-terminal dimerization of yeast Hsp90 (L15R and L18R in yeast, L24R and L27R in humans) significantly reduced the ATPase activity of yeast and human Hsp90s, showing that ATP-dependent association of the N-terminal domains in the Hsp90 dimer is also essential in both systems.	Adenosine Triphosphate	150-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
19058963-2	2009	Among small molecule Hsp90 inhibitors with clinical applicability are derivatives of 8-arylmethyl-9H-purin-6-amine class.	8-arylmethyl-9h-purin-6-amine	85-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
18820127-2	2009	Herein, we report that treatment with the 90-kDa heat shock protein (Hsp90) molecular chaperone inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) selectively abrogates the G(2)/M checkpoint induced by 7-ethyl-10-hydroxycamptothecin (SN-38), an active metabolite of irinotecan, in p53-null compared with p53-intact HCT116 colon cancer cells.	tanespimycin	106-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
18820127-2	2009	Herein, we report that treatment with the 90-kDa heat shock protein (Hsp90) molecular chaperone inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) selectively abrogates the G(2)/M checkpoint induced by 7-ethyl-10-hydroxycamptothecin (SN-38), an active metabolite of irinotecan, in p53-null compared with p53-intact HCT116 colon cancer cells.	Irinotecan	208-238	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
18820127-2	2009	Herein, we report that treatment with the 90-kDa heat shock protein (Hsp90) molecular chaperone inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) selectively abrogates the G(2)/M checkpoint induced by 7-ethyl-10-hydroxycamptothecin (SN-38), an active metabolite of irinotecan, in p53-null compared with p53-intact HCT116 colon cancer cells.	Irinotecan	240-245	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
18820127-2	2009	Herein, we report that treatment with the 90-kDa heat shock protein (Hsp90) molecular chaperone inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) selectively abrogates the G(2)/M checkpoint induced by 7-ethyl-10-hydroxycamptothecin (SN-38), an active metabolite of irinotecan, in p53-null compared with p53-intact HCT116 colon cancer cells.	Irinotecan	272-282	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
18820127-7	2009	Coimmunoprecipitation experiments showed that Hsp90 and Wee1 interacted in whole cells, and 17AAG treatment decreased the degradative half-life of Wee1, indicating that Wee1 is another Hsp90 client in mammalian cells.	tanespimycin	92-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	185-190
19242542-6	2009	In this report we demonstrate that in response to heat shock or treatment with the Hsp90 inhibitor geldanamycin, the J protein Hsp40 becomes a major component of the CSPalpha complex.	geldanamycin	99-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
20225761-0	2009	Targeting of multiple signaling pathways by the Hsp90 inhibitor SNX-2112 in EGFR resistance models as a single agent or in combination with erlotinib.	SNX 2112	64-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
18929486-0	2008	Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone.	dihydroxylphenyl amides	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
19353939-1	2009	5 mg of Geldanamycin, an inhibitor of stress protein HSP86 which express on mammalian germ cells, were administered to E8 pregnant mice.	geldanamycin	8-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
19088048-3	2008	We conducted a phase II trial using the hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) in melanoma patients.	tanespimycin	56-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19088048-3	2008	We conducted a phase II trial using the hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) in melanoma patients.	tanespimycin	96-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
19088048-6	2008	The hsp90 inhibitor 17-AAG was administered i.v.	tanespimycin	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
19026643-3	2008	However, Hsp90 is not required for the activation of TAK1 as short exposure to the Hsp90 inhibitor, 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) did not affect its activation by LPS or IL-1.	tanespimycin	100-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
18826913-3	2008	This is followed by a virtual screening docking study of the PU3 family of compounds and Hsp90 incorporating several conserved water molecules.	Water	127-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
18768392-0	2008	Geldanamycin-induced Lyn dissociation from aberrant Hsp90-stabilized cytosolic complex is an early event in apoptotic mechanisms in B-chronic lymphocytic leukemia.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
18768392-6	2008	We also demonstrate that treatment of B-CLL cells with geldanamycin, an Hsp90 inhibitor already reported to induce cell death, is capable of dissociating the CL complex in the early phases of apoptosis and thus inactivating CL itself.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
18820283-7	2008	To determine the physiological significance of this interaction, SCC4 cells were exposed to geldanamycin (GA), a competitive inhibitor of hsp90.	geldanamycin	92-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
18820283-7	2008	To determine the physiological significance of this interaction, SCC4 cells were exposed to geldanamycin (GA), a competitive inhibitor of hsp90.	geldanamycin	106-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
19047110-11	2008	CONCLUSIONS: Hsp90 overexpression represents a poor prognosticator that correlates with several adverse parameters, highlighting its role in disease progression and alternative therapy for high-risk, imatinib-resistant gastrointestinal stromal tumors.	Imatinib Mesylate	200-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18833289-5	2008	RAR1 partly shares the same binding site with HSP90 as the CS domain, whereas AHA1 does not.	Cesium	59-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
19035474-1	2008	OBJECTIVE: To evaluate the ability of SNX-7081, a novel small molecule inhibitor of Hsp90, to block components of inflammation, including cytokine production, protein kinase activity, and angiogenic signaling.	SNX-7081	38-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
19035474-3	2008	METHODS: SNX-7081 binding to Hsp90 was characterized in Jurkat cells and RA synovial fibroblasts (RASFs).	SNX-7081	9-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
19035474-9	2008	RESULTS: SNX-7081 showed strong binding affinity to Hsp90 and expected induction of Hsp70.	SNX-7081	9-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
19035474-16	2008	The strong in vivo efficacy observed with SNX-4414 provides preclinical validation for consideration of Hsp90 inhibitors in the treatment of RA.	snx-4414	42-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
18682551-6	2008	DHA also enhanced expression of 2 proteins instrumental in activation of eNOS: phospho-Akt (5 and 50 nM) and HSP90 (50 nM and 1 microM).	Dihydroalprenolol	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
18682551-8	2008	Findings suggest that DHA enhances eNOS and Akt activity, augments HSP90 expression, and increases NO bioavailability in response to Akt kinase activation.	Dihydroalprenolol	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
18393300-0	2008	Stability of the Hsp90 inhibitor 17AAG hydroquinone and prevention of metal-catalyzed oxidation.	tanespimycin	33-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
18393300-0	2008	Stability of the Hsp90 inhibitor 17AAG hydroquinone and prevention of metal-catalyzed oxidation.	Metals	70-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
18393300-1	2008	17-(allylamino)-17-demethoxygeldanamycin (17AAG) is a benzoquinone ansamycin Hsp90 inhibitor which has promising anticancer activity in vitro, in animal models and in clinical trials.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
18393300-1	2008	17-(allylamino)-17-demethoxygeldanamycin (17AAG) is a benzoquinone ansamycin Hsp90 inhibitor which has promising anticancer activity in vitro, in animal models and in clinical trials.	tanespimycin	42-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
18393300-1	2008	17-(allylamino)-17-demethoxygeldanamycin (17AAG) is a benzoquinone ansamycin Hsp90 inhibitor which has promising anticancer activity in vitro, in animal models and in clinical trials.	benzoquinone ansamycin	54-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
18393300-3	2008	The hydroquinone derivative of 17AAG, 17AAG hydroquinone (17AAGH(2)), is considerably more water soluble and since we previously demonstrated that 17AAGH(2) was a more potent Hsp90 inhibitor than its parent quinone, it is a good candidate for clinical use and is currently in clinical trials.	hydroquinone	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
18393300-3	2008	The hydroquinone derivative of 17AAG, 17AAG hydroquinone (17AAGH(2)), is considerably more water soluble and since we previously demonstrated that 17AAGH(2) was a more potent Hsp90 inhibitor than its parent quinone, it is a good candidate for clinical use and is currently in clinical trials.	tanespimycin	31-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
18393300-3	2008	The hydroquinone derivative of 17AAG, 17AAG hydroquinone (17AAGH(2)), is considerably more water soluble and since we previously demonstrated that 17AAGH(2) was a more potent Hsp90 inhibitor than its parent quinone, it is a good candidate for clinical use and is currently in clinical trials.	tanespimycin	38-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
18393300-3	2008	The hydroquinone derivative of 17AAG, 17AAG hydroquinone (17AAGH(2)), is considerably more water soluble and since we previously demonstrated that 17AAGH(2) was a more potent Hsp90 inhibitor than its parent quinone, it is a good candidate for clinical use and is currently in clinical trials.	quinone	9-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	175-180
18726985-5	2008	Furthermore, we demonstrate that quercetin promotes cancer cell apoptosis by down-regulating the levels of heat shock protein (Hsp) 90.	Quercetin	33-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-134
18726985-6	2008	Depletion of Hsp90 by quercetin results in decreased cell viability, levels of surrogate markers of Hsp90 inhibition (intracellular and secreted), induced apoptosis and activation of caspases in cancer cells but not in normal prostate epithelial cells.	Quercetin	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18726985-6	2008	Depletion of Hsp90 by quercetin results in decreased cell viability, levels of surrogate markers of Hsp90 inhibition (intracellular and secreted), induced apoptosis and activation of caspases in cancer cells but not in normal prostate epithelial cells.	Quercetin	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
18955054-0	2008	Cisplatin differently affects amino terminal and carboxyl terminal domains of HSP90.	Cisplatin	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
18726985-8	2008	CONCLUSION: Our results demonstrate that quercetin down-regulates the expression of Hsp90 which, in turn, induces inhibition of growth and cell death in prostate cancer cells while exerting no quantifiable effect on normal prostate epithelial cells.	Quercetin	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
18939877-1	2008	Novobiocin, a known DNA gyrase inhibitor, binds to a nucleotide-binding site located on the Hsp90 C-terminus and induces degradation of Hsp90-dependent client proteins at approximately 700 microM in breast cancer cells (SKBr3).	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
18939877-1	2008	Novobiocin, a known DNA gyrase inhibitor, binds to a nucleotide-binding site located on the Hsp90 C-terminus and induces degradation of Hsp90-dependent client proteins at approximately 700 microM in breast cancer cells (SKBr3).	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
18954528-2	2008	We evaluated the mechanism and effect of 17-(allylamino)-17-demethoxygeldanamycin (17AAG), a novel inhibitor of heat shock protein 90 (Hsp90), on the IL-6 gene expression in human prostatic carcinoma (PC-3) cells.	tanespimycin	41-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
18954528-2	2008	We evaluated the mechanism and effect of 17-(allylamino)-17-demethoxygeldanamycin (17AAG), a novel inhibitor of heat shock protein 90 (Hsp90), on the IL-6 gene expression in human prostatic carcinoma (PC-3) cells.	tanespimycin	41-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
18954528-2	2008	We evaluated the mechanism and effect of 17-(allylamino)-17-demethoxygeldanamycin (17AAG), a novel inhibitor of heat shock protein 90 (Hsp90), on the IL-6 gene expression in human prostatic carcinoma (PC-3) cells.	tanespimycin	83-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
18954528-2	2008	We evaluated the mechanism and effect of 17-(allylamino)-17-demethoxygeldanamycin (17AAG), a novel inhibitor of heat shock protein 90 (Hsp90), on the IL-6 gene expression in human prostatic carcinoma (PC-3) cells.	tanespimycin	83-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
18591204-9	2008	CONCLUSION: Activation of NHE via calcium-dependent calpain contributes to hyperglycaemia-induced endothelial dysfunction through dissociation of hsp90 from eNOS.	Calcium	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
18955054-2	2008	We previously demonstrated that the antineoplastic reagent, cisplatin, inhibits the aggregation prevention activity of mammalian HSP90.	Cisplatin	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
18955054-3	2008	We now show that cisplatin binds both the amino terminal and carboxyl terminal domains of the human HSP90 and differently affects these two domains.	Cisplatin	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
18955054-5	2008	In contrast, cisplatin induces a conformational change in HSP90N, but not HSP90C.	Cisplatin	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-64
18955054-6	2008	These results indicate that cisplatin modulates the HSP90 activities through two different mechanisms using the two distinct binding sites of the HSP90 molecule.	Cisplatin	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
18955054-6	2008	These results indicate that cisplatin modulates the HSP90 activities through two different mechanisms using the two distinct binding sites of the HSP90 molecule.	Cisplatin	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
19138996-1	2008	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (HSP90), plays a significant role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	116-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
19138996-1	2008	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (HSP90), plays a significant role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	116-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
19000834-5	2008	We demonstrate the ATP-sensitive interaction of the cofilin phosphatase chronophin (CIN) with the chaperone hsp90 to form a biosensor that mediates cofilin/actin rod formation.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
19000834-6	2008	Our results suggest a model whereby attenuated interactions between CIN and hsp90 during ATP depletion enhance CIN-dependent cofilin dephosphorylation and consequent rod assembly, thereby providing a mechanism for the formation of pathological actin/cofilin aggregates during neurodegenerative energy flux.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
19138996-1	2008	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (HSP90), plays a significant role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	149-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
19138996-1	2008	The aryl hydrocarbon receptor (AhR), a client protein of heat shock protein 90 (HSP90), plays a significant role in polycyclic aromatic hydrocarbon (PAH)-induced carcinogenesis.	Polycyclic Aromatic Hydrocarbons	149-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
19138996-3	2008	The main objectives of this study were to determine whether HSP90 inhibitors suppress PAH-mediated induction of CYP1A1 and CYP1B1 or block benzo(a)pyrene [B(a)P]-induced formation of DNA adducts.	Polycyclic Aromatic Hydrocarbons	86-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
19138996-5	2008	Inhibitors of HSP90 [17-allylamino-17-demethoxygeldanamycin (17-AAG); celastrol] suppressed these inductive effects of PAHs.	tanespimycin	21-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19138996-5	2008	Inhibitors of HSP90 [17-allylamino-17-demethoxygeldanamycin (17-AAG); celastrol] suppressed these inductive effects of PAHs.	tanespimycin	61-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19138996-5	2008	Inhibitors of HSP90 [17-allylamino-17-demethoxygeldanamycin (17-AAG); celastrol] suppressed these inductive effects of PAHs.	celastrol	70-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19138996-5	2008	Inhibitors of HSP90 [17-allylamino-17-demethoxygeldanamycin (17-AAG); celastrol] suppressed these inductive effects of PAHs.	Polycyclic Aromatic Hydrocarbons	119-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
19138996-6	2008	Treatment with 17-AAG and celastrol also caused a rapid and marked decrease in amounts of AhR protein without modulating levels of HSP90.	celastrol	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
19138996-8	2008	The reduction in B(a)P-induced DNA adducts was due, at least in part, to reduced metabolic activation of B(a)P. Collectively, these results suggest that 17-AAG and celastrol, inhibitors of HSP90, suppress the activation of AhR-dependent gene expression, leading, in turn, to reduced formation of B(a)P-induced DNA adducts.	tanespimycin	153-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-194
19138996-8	2008	The reduction in B(a)P-induced DNA adducts was due, at least in part, to reduced metabolic activation of B(a)P. Collectively, these results suggest that 17-AAG and celastrol, inhibitors of HSP90, suppress the activation of AhR-dependent gene expression, leading, in turn, to reduced formation of B(a)P-induced DNA adducts.	celastrol	164-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-194
19138996-8	2008	The reduction in B(a)P-induced DNA adducts was due, at least in part, to reduced metabolic activation of B(a)P. Collectively, these results suggest that 17-AAG and celastrol, inhibitors of HSP90, suppress the activation of AhR-dependent gene expression, leading, in turn, to reduced formation of B(a)P-induced DNA adducts.	Benzo(a)pyrene	17-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-194
18689673-9	2008	Hsp90, another HSF-1 target gene, was decreased during short-term alcohol but increased after prolonged alcohol exposure.	Alcohols	66-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18689673-9	2008	Hsp90, another HSF-1 target gene, was decreased during short-term alcohol but increased after prolonged alcohol exposure.	Alcohols	104-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18689673-10	2008	Decreased hsp90-HSF-1 complexes after short-term alcohol indicated dissociation of HSF-1 from hsp90.	Alcohols	49-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
18689673-11	2008	On the other hand, hsp90 interacted with client protein IkappaB kinase beta, a signaling intermediate of the LPS pathway, followed by IkappaBalpha degradation and increased NF-kappaB activity after chronic alcohol exposure, indicating that hsp90 plays an important role in supporting inflammatory cytokine production.	Alcohols	206-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
18689673-11	2008	On the other hand, hsp90 interacted with client protein IkappaB kinase beta, a signaling intermediate of the LPS pathway, followed by IkappaBalpha degradation and increased NF-kappaB activity after chronic alcohol exposure, indicating that hsp90 plays an important role in supporting inflammatory cytokine production.	Alcohols	206-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	240-245
18689673-12	2008	Inhibition of hsp90 using geldanamycin prevented prolonged alcohol-induced elevation in LPS-induced NF-kappaB and TNF-alpha production.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18689673-12	2008	Inhibition of hsp90 using geldanamycin prevented prolonged alcohol-induced elevation in LPS-induced NF-kappaB and TNF-alpha production.	Alcohols	59-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18689673-13	2008	These results suggest that alcohol exposure differentially regulates hsp70 and hsp90 via HSF-1 activation.	Alcohols	27-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
18689673-14	2008	Further, hsp90 regulates TNF-alpha production in macrophages contributing to alcohol-induced inflammation.	Alcohols	77-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
18339423-9	2008	The inhibition of HSP90 with geldanamycin attenuated phosphorylated STAT3 and made B5/Bu250(6) and KBM3/Bu250(6) more Bu-sensitive.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
18339423-9	2008	The inhibition of HSP90 with geldanamycin attenuated phosphorylated STAT3 and made B5/Bu250(6) and KBM3/Bu250(6) more Bu-sensitive.	bu250	86-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
18339423-9	2008	The inhibition of HSP90 with geldanamycin attenuated phosphorylated STAT3 and made B5/Bu250(6) and KBM3/Bu250(6) more Bu-sensitive.	bu250	104-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
18339423-9	2008	The inhibition of HSP90 with geldanamycin attenuated phosphorylated STAT3 and made B5/Bu250(6) and KBM3/Bu250(6) more Bu-sensitive.	Busulfan	86-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
18974397-4	2008	Here, we report that the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) blocks MMP-9 secretion and that HA-induced nuclear factor-kappaB (NF-kappaB) activation is mediated by IkappaB kinase, which phosphorylates the NF-kappaB inhibitor IkappaBalpha and promotes its degradation.	tanespimycin	41-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
18682401-0	2008	Functional role of HSP90 complexes with endothelial nitric-oxide synthase (eNOS) and calpain on nitric oxide generation in endothelial cells.	Nitric Oxide	96-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
18682401-4	2008	Furthermore, in the presence of the HSP90 inhibitor geldanamycin, a significant decrease in NO production and an extensive degradation of eNOS protein occurs, indicating that dissociation from membranes and association with the chaperone is correlated to the protection of the synthase.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
18703510-4	2008	Addition of recombinant hsp90alpha to cell lysate enhanced chymotrypsin-like activity of the 26 S proteasome in an ATP-dependent manner as determined by an in-gel hydrolysis assay.	Adenosine Triphosphate	115-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-34
18785742-4	2008	Hsp90 functions in multichaperone complexes driven by the binding and hydrolysis of ATP.	Adenosine Triphosphate	84-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18785742-5	2008	Encouraging results have been obtained by inhibiting Hsp90 with 17-AAG, an active-site binding ATP analog.	tanespimycin	64-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
18785742-5	2008	Encouraging results have been obtained by inhibiting Hsp90 with 17-AAG, an active-site binding ATP analog.	Adenosine Triphosphate	95-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
18703510-5	2008	We successfully pulled down histidine-tagged hsp90alpha- and PA28alpha-induced, newly assembled 26 S proteasomes from the cell extracts for in vitro epitope production assay, and we found these structures to be sensitive to geldanamycin, an hsp90 inhibitor.	Histidine	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
18703510-5	2008	We successfully pulled down histidine-tagged hsp90alpha- and PA28alpha-induced, newly assembled 26 S proteasomes from the cell extracts for in vitro epitope production assay, and we found these structures to be sensitive to geldanamycin, an hsp90 inhibitor.	Histidine	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
18703510-5	2008	We successfully pulled down histidine-tagged hsp90alpha- and PA28alpha-induced, newly assembled 26 S proteasomes from the cell extracts for in vitro epitope production assay, and we found these structures to be sensitive to geldanamycin, an hsp90 inhibitor.	geldanamycin	224-236	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-55
18703510-5	2008	We successfully pulled down histidine-tagged hsp90alpha- and PA28alpha-induced, newly assembled 26 S proteasomes from the cell extracts for in vitro epitope production assay, and we found these structures to be sensitive to geldanamycin, an hsp90 inhibitor.	geldanamycin	224-236	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
18703510-8	2008	Inhibition of hsp90 in vivo by geldanamycin partly disrupted the 26 S proteasome structure, consistent with down-regulated MHC class I expression.	geldanamycin	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18655187-7	2008	Interestingly, data from immunocomplex studies revealed that quercetin promoted interaction between Her-2/neu and Hsp90 which is a molecular chaperone involved in stabilization of Her-2/neu.	Quercetin	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
18927309-0	2008	Phase I pharmacokinetic and pharmacodynamic study of LAQ824, a hydroxamate histone deacetylase inhibitor with a heat shock protein-90 inhibitory profile, in patients with advanced solid tumors.	LAQ824	53-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-133
18927314-2	2008	We conducted a phase I study of irinotecan and the Hsp90 inhibitor 17AAG, which can also down-regulate Chk1, in patients with solid tumors.	tanespimycin	67-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
18927314-13	2008	Evidence for Hsp90 inhibition by 17AAG, resulting in phospho-Chk1 loss, abrogation of the G(2)-M cell cycle checkpoint, and cell death could be shown in tumor biopsy samples obtained at the MTD.	tanespimycin	33-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18840695-5	2008	In the current study, we show that, in contrast to its activity against prostate cancer cells in vitro and its inhibition of s.c. prostate cancer xenografts, the Hsp90 inhibitor 17-AAG stimulates the intraosseous growth of PC-3M prostate carcinoma cells.	tanespimycin	178-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
18855578-5	2008	Small molecule Hsp90 inhibitors bind to the ATP binding pocket, inhibit chaperone function and could potentially result in cytostasis or cell death.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
18660379-5	2008	Although cross-resistant to antileukemia agents (eg, cytarabine, etoposide, and TRAIL), HL-60/LR cells are collaterally sensitive to the hsp90 inhibitor 17-AAG.	tanespimycin	153-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
18193424-1	2008	PURPOSE: To study the interactions of the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and carboplatin in vitro and in vivo.	tanespimycin	82-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
18193424-1	2008	PURPOSE: To study the interactions of the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and carboplatin in vitro and in vivo.	tanespimycin	82-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
18193424-1	2008	PURPOSE: To study the interactions of the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and carboplatin in vitro and in vivo.	tanespimycin	122-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
18193424-1	2008	PURPOSE: To study the interactions of the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and carboplatin in vitro and in vivo.	tanespimycin	122-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
18193424-1	2008	PURPOSE: To study the interactions of the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and carboplatin in vitro and in vivo.	Carboplatin	134-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
18193424-1	2008	PURPOSE: To study the interactions of the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) and carboplatin in vitro and in vivo.	Carboplatin	134-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
18193424-4	2008	The ability of 17-AAG to deplete HSP90 client proteins either alone or in combination with carboplatin was evaluated by western blotting.	tanespimycin	15-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
18769124-3	2008	HSP90 inhibitors such as 17-allylaminodemethoxygeldanamycin (17-AAG), potently downregulate the cell surface ErbB2.	17-allylaminodemethoxygeldanamycin	25-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	benzoquinone ansamycin	26-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-81
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	benzoquinone ansamycin	26-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	Barium	50-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-81
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	Barium	50-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	hydroquinone ansamycins	139-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-81
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	hydroquinone ansamycins	139-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	188-193
18635747-1	2008	Two-electron reduction of benzoquinone ansamycin (BA) heat shock protein (Hsp) 90 inhibitors by NAD(P)H:quinone oxidoreductase 1 (NQO1) to hydroquinone ansamycins (BAH2s) leads to greater Hsp90 inhibitory activity.	bah2s	164-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-81
18635747-11	2008	Minimizing the propensity of BA derivatives to undergo one-electron reduction and glutathione conjugation while maximizing their two-electron reduction to stable Hsp90 inhibitory hydroquinones may be a useful strategy for optimizing the therapeutic index of BAs.	Barium	29-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
18635747-11	2008	Minimizing the propensity of BA derivatives to undergo one-electron reduction and glutathione conjugation while maximizing their two-electron reduction to stable Hsp90 inhibitory hydroquinones may be a useful strategy for optimizing the therapeutic index of BAs.	Hydroquinones	179-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
18657349-3	2008	Inhibitors of heat shock protein 90 (HSP90), a chaperone for which Kit is a client protein, have demonstrated activity against human cancers and evidence suggests they downregulate several mutated and imatinib-resistant forms of Kit.	Imatinib Mesylate	201-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
18657349-3	2008	Inhibitors of heat shock protein 90 (HSP90), a chaperone for which Kit is a client protein, have demonstrated activity against human cancers and evidence suggests they downregulate several mutated and imatinib-resistant forms of Kit.	Imatinib Mesylate	201-209	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
18655187-8	2008	In this condition, inhibition of Hsp90 activity by a specific inhibitor, geldanamycin (GA), or intracellular ATP depletion caused dissociation of Hsp90 from Her-2/neu and promoted ubiquitination and down-regulation of Her-2/neu protein.	geldanamycin	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
18655187-8	2008	In this condition, inhibition of Hsp90 activity by a specific inhibitor, geldanamycin (GA), or intracellular ATP depletion caused dissociation of Hsp90 from Her-2/neu and promoted ubiquitination and down-regulation of Her-2/neu protein.	geldanamycin	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
18655187-8	2008	In this condition, inhibition of Hsp90 activity by a specific inhibitor, geldanamycin (GA), or intracellular ATP depletion caused dissociation of Hsp90 from Her-2/neu and promoted ubiquitination and down-regulation of Her-2/neu protein.	geldanamycin	87-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
18655187-8	2008	In this condition, inhibition of Hsp90 activity by a specific inhibitor, geldanamycin (GA), or intracellular ATP depletion caused dissociation of Hsp90 from Her-2/neu and promoted ubiquitination and down-regulation of Her-2/neu protein.	geldanamycin	87-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
18655187-8	2008	In this condition, inhibition of Hsp90 activity by a specific inhibitor, geldanamycin (GA), or intracellular ATP depletion caused dissociation of Hsp90 from Her-2/neu and promoted ubiquitination and down-regulation of Her-2/neu protein.	Adenosine Triphosphate	109-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
18827603-4	2008	METHODS: We investigated how 17-allylamino-17-demethoxygeldanamycin (17-AAG), a small molecule inhibitor of Hsp90, is implicated in human malignant pleural mesothelioma (MM).	tanespimycin	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
18852123-0	2008	Genistein down-regulates androgen receptor by modulating HDAC6-Hsp90 chaperone function.	Genistein	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18852123-7	2008	The increased ubiquitination of AR after genistein treatment is attributed to decreased Hsp90 chaperone activity as assessed by its increased functionally inactive acetylated form.	Genistein	41-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
18852123-8	2008	Consistent with this result, we find that HDAC6, which is a Hsp90 deacetylase, is inhibited by the antiestrogenic activity of genistein.	Genistein	126-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
18852123-9	2008	Hence, in this study, we elucidate a novel mechanism of AR down-regulation by genistein through inhibition of HDAC6-Hsp90 cochaperone function required to stabilize AR protein.	Genistein	78-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
18852129-1	2008	Benzoquinone ansamycin antibiotics such as geldanamycin (GA) bind to the NH(2)-terminal ATP-binding domain of heat shock protein (Hsp) 90 and inhibit its chaperone functions.	benzoquinone ansamycin	0-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-137
18852129-1	2008	Benzoquinone ansamycin antibiotics such as geldanamycin (GA) bind to the NH(2)-terminal ATP-binding domain of heat shock protein (Hsp) 90 and inhibit its chaperone functions.	geldanamycin	43-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-137
18852129-1	2008	Benzoquinone ansamycin antibiotics such as geldanamycin (GA) bind to the NH(2)-terminal ATP-binding domain of heat shock protein (Hsp) 90 and inhibit its chaperone functions.	geldanamycin	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-137
18852129-1	2008	Benzoquinone ansamycin antibiotics such as geldanamycin (GA) bind to the NH(2)-terminal ATP-binding domain of heat shock protein (Hsp) 90 and inhibit its chaperone functions.	Adenosine Triphosphate	88-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-137
18852131-3	2008	This study aimed to assess the antitumor activity of the Hsp90 inhibitor, IPI-504, in pancreatic cancer and to determine the biological effects of the agent.	tanespimycin	74-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18852131-4	2008	In vitro, we show that pharmacologic inhibition of Hsp90 by IPI-504 exerts antiproliferative effects in a panel of pancreatic cancer cells in a dose- and time-dependent manner.	tanespimycin	60-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
18852131-6	2008	Although known Hsp90 client proteins were significantly modulated in IPI-504-treated cell line, no consistent alteration of these proteins was observed in vivo other than induction of Hsp70 expression in the treated xenografted tumors.	tanespimycin	69-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
18800759-1	2008	A biosynthetic medicinal chemistry approach was applied to the optimization of the natural product Hsp90 inhibitor macbecin.	Macbecin	115-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
18800759-2	2008	By genetic engineering, mutants have been created to produce novel macbecin analogues including a nonquinone compound (5) that has significantly improved binding affinity to Hsp90 (Kd 3 nM vs 240 nM for macbecin) and reduced toxicity (MTD &gt; or = 250 mg/kg).	Macbecin	67-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
18800759-2	2008	By genetic engineering, mutants have been created to produce novel macbecin analogues including a nonquinone compound (5) that has significantly improved binding affinity to Hsp90 (Kd 3 nM vs 240 nM for macbecin) and reduced toxicity (MTD &gt; or = 250 mg/kg).	Macbecin	203-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
18504430-2	2008	In this study we examined the effect of heat-shock protein 90 (HSP90) inhibitor, geldanamycin (GA), on IR-induced G(2) arrest in human colon adenocarcinoma cells with different p53 status.	geldanamycin	81-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
18504430-2	2008	In this study we examined the effect of heat-shock protein 90 (HSP90) inhibitor, geldanamycin (GA), on IR-induced G(2) arrest in human colon adenocarcinoma cells with different p53 status.	geldanamycin	81-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18504430-2	2008	In this study we examined the effect of heat-shock protein 90 (HSP90) inhibitor, geldanamycin (GA), on IR-induced G(2) arrest in human colon adenocarcinoma cells with different p53 status.	geldanamycin	95-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
18504430-2	2008	In this study we examined the effect of heat-shock protein 90 (HSP90) inhibitor, geldanamycin (GA), on IR-induced G(2) arrest in human colon adenocarcinoma cells with different p53 status.	geldanamycin	95-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18762423-0	2008	Synthesis and SAR study of N-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)-arylsulfonamides: heat shock protein 90 (Hsp90) inhibitors with submicromolar activity in an in vitro assay.	n-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)-arylsulfonamides	27-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-116
18769157-6	2008	Finally, the Hsp90 inhibitor 17-AAG, by simultaneously and durably inhibiting multiple signaling activators including ErbB and Src kinases, does not permit oncogene switching and results in a more prolonged and robust inhibition of downstream signaling pathways in breast cancer cells than do individual TKIs.	tanespimycin	29-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18794130-1	2008	Despite studies that show the antitumor activity of Hsp90 inhibitors, such as geldanamycin (GA) and its derivative 17-allylamino-demethoxygeldanamycin (17-AAG), recent reports indicate that these inhibitors lack significant single-agent clinical activity.	geldanamycin	78-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
18794130-1	2008	Despite studies that show the antitumor activity of Hsp90 inhibitors, such as geldanamycin (GA) and its derivative 17-allylamino-demethoxygeldanamycin (17-AAG), recent reports indicate that these inhibitors lack significant single-agent clinical activity.	geldanamycin	92-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
18794130-1	2008	Despite studies that show the antitumor activity of Hsp90 inhibitors, such as geldanamycin (GA) and its derivative 17-allylamino-demethoxygeldanamycin (17-AAG), recent reports indicate that these inhibitors lack significant single-agent clinical activity.	17-allylamino-demethoxygeldanamycin	115-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
18794130-1	2008	Despite studies that show the antitumor activity of Hsp90 inhibitors, such as geldanamycin (GA) and its derivative 17-allylamino-demethoxygeldanamycin (17-AAG), recent reports indicate that these inhibitors lack significant single-agent clinical activity.	tanespimycin	152-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
18794130-9	2008	Transfection with siRNA directed against Hsp27, Hsp70, or Hsp27 and Hsp70 also increased sensitivity to EC78, a purine scaffold-based Hsp90 inhibitor that is not a P-gp substrate.	ec78	104-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
18794130-9	2008	Transfection with siRNA directed against Hsp27, Hsp70, or Hsp27 and Hsp70 also increased sensitivity to EC78, a purine scaffold-based Hsp90 inhibitor that is not a P-gp substrate.	purine	112-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
18762423-0	2008	Synthesis and SAR study of N-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)-arylsulfonamides: heat shock protein 90 (Hsp90) inhibitors with submicromolar activity in an in vitro assay.	n-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)-arylsulfonamides	27-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
18762423-2	2008	In a program directed toward identifying novel chemical probes for Hsp90, we found N-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)benzene sulfonamide as an Hsp90 inhibitor with very weak activity.	n-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)benzene sulfonamide	83-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
18762423-2	2008	In a program directed toward identifying novel chemical probes for Hsp90, we found N-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)benzene sulfonamide as an Hsp90 inhibitor with very weak activity.	n-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)benzene sulfonamide	83-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
18591380-2	2008	Treatment with pan-HDAC inhibitors or depletion of HDAC6 by siRNA induces hyperacetylation and inhibits ATP binding and chaperone function of hsp90.	Adenosine Triphosphate	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
18591380-3	2008	Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins.	17-allylamino-demothoxy geldanamycin	15-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
18591380-3	2008	Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins.	17-allylamino-demothoxy geldanamycin	15-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
18591380-3	2008	Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins.	Adenosine Triphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
18591380-3	2008	Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins.	Adenosine Triphosphate	75-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
18591380-5	2008	Hyperacetylation of hsp90 increased its binding to 17-AAG, as well as enhanced 17-AAG-mediated attenuation of ATP and the cochaperone p23 binding to hsp90.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
18394702-0	2008	MS-275, a novel histone deacetylase inhibitor with selectivity against HDAC1, induces degradation of FLT3 via inhibition of chaperone function of heat shock protein 90 in AML cells.	entinostat	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-167
18307035-10	2008	Inhibition of the function of Hsp90 chaperone with geldanamycin strongly inhibited the E2-induced ERE-transactivation.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
21442009-0	2008	Efficient Synthesis of a Novel Resorcyclide as Anticancer Agent Based on Hsp90 Inhibition.	resorcyclide	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
21442009-1	2008	The highly efficient synthesis of a novel heat shock protein 90 (Hsp90)-based anticancer agent, triazole-cycloproparadicicol (5), is described.	triazole-cycloproparadicicol	96-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
21442009-1	2008	The highly efficient synthesis of a novel heat shock protein 90 (Hsp90)-based anticancer agent, triazole-cycloproparadicicol (5), is described.	triazole-cycloproparadicicol	96-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
18594209-3	2008	We now report that Akt activation in response to rapamycin is abrogated by 17-allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor.	Sirolimus	49-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
18594209-3	2008	We now report that Akt activation in response to rapamycin is abrogated by 17-allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor.	Sirolimus	49-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
18594209-3	2008	We now report that Akt activation in response to rapamycin is abrogated by 17-allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor.	tanespimycin	75-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
18594209-3	2008	We now report that Akt activation in response to rapamycin is abrogated by 17-allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor.	tanespimycin	75-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
18594209-3	2008	We now report that Akt activation in response to rapamycin is abrogated by 17-allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor.	tanespimycin	115-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-147
18594209-3	2008	We now report that Akt activation in response to rapamycin is abrogated by 17-allylamino-17-demethoxygeldanamycin (17-AAG), a heat shock protein 90 (HSP90) inhibitor.	tanespimycin	115-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
18594209-8	2008	Rapamycin/17-AAG combination alleviates the induction of HSP90 protein, a heat shock response frequently associated with 17-AAG monotherapy.	Sirolimus	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18594209-8	2008	Rapamycin/17-AAG combination alleviates the induction of HSP90 protein, a heat shock response frequently associated with 17-AAG monotherapy.	tanespimycin	10-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18594209-8	2008	Rapamycin/17-AAG combination alleviates the induction of HSP90 protein, a heat shock response frequently associated with 17-AAG monotherapy.	tanespimycin	121-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18676850-5	2008	We therefore inhibited HSP90 with 17-allylamino-17-demethoxygeldanamycin (17-AAG) and siRNA, and observed that ES cell line growth and survival were reduced, especially in the resistant cell lines.	tanespimycin	34-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18676850-5	2008	We therefore inhibited HSP90 with 17-allylamino-17-demethoxygeldanamycin (17-AAG) and siRNA, and observed that ES cell line growth and survival were reduced, especially in the resistant cell lines.	tanespimycin	74-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18676850-7	2008	17-AAG treatment induced HSP90 client protein degradation, including AKT, KIT, or IGF1R, by inhibiting their physical interaction with HSP90.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
18676850-7	2008	17-AAG treatment induced HSP90 client protein degradation, including AKT, KIT, or IGF1R, by inhibiting their physical interaction with HSP90.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
18676857-1	2008	The geldanamycin derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) are promising chemotherapeutic drugs that inhibit heat shock protein 90 (HSP90) function.	tanespimycin	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-214
18676857-1	2008	The geldanamycin derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) are promising chemotherapeutic drugs that inhibit heat shock protein 90 (HSP90) function.	tanespimycin	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	216-221
18676857-1	2008	The geldanamycin derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) are promising chemotherapeutic drugs that inhibit heat shock protein 90 (HSP90) function.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	81-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-214
18676857-1	2008	The geldanamycin derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) are promising chemotherapeutic drugs that inhibit heat shock protein 90 (HSP90) function.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	81-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	216-221
18676857-8	2008	These results suggest that in addition to direct inhibition of HSP90, the antitumor effect of geldanamycin and its derivatives is also mediated though the production of ROS, which may directly inactivate tumorigenic mutant BRAF(V600E).	geldanamycin	94-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18677112-4	2008	While we detected abundant expression of the R661W protein, we noted marked instability of both endogenous and recombinant R661W following treatment in vivo with the Hsp90 inhibitor, geldanamycin and stabilization of R661W following heat shock.	geldanamycin	183-195	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
18666033-8	2008	Finally, the discovery that inhibitors of calcineurin or Hsp90 result in dramatic synergism with either azoles or glucan synthase inhibitors (candins) provides another therapeutic vantage point.	Azoles	104-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18644253-4	2008	It will refer to the two 17-AAG formulations, tanespimycin and IPI-504, and to synthetic small molecules, among which are the purine-scaffold Hsp90 inhibitor CNF2024/BIIB021, the isoxazole derivative VER-52296/NVP-AUY922, and the carbazol-4-one benzamide derivative SNX-5422, and will present our current knowledge on their clinical performance.	purine	126-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
18480838-0	2008	Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVP-AUY922 in multiple myeloma.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
18480838-5	2008	We analysed the biochemical effects of a novel diarylisoxazole-based Hsp90 inhibitor (NVP-AUY922) on signalling pathways and cell death in a large set of primary MM tumour samples and in MM cell lines.	diarylisoxazole	47-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
18394702-4	2008	Further studies found that MS-275 induced acetylation of heat shock protein 90 (HSP90) in conjunction with ubiquitination of FLT3, leading to degradation of FLT3 proteins in these cells.	entinostat	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-78
18394702-4	2008	Further studies found that MS-275 induced acetylation of heat shock protein 90 (HSP90) in conjunction with ubiquitination of FLT3, leading to degradation of FLT3 proteins in these cells.	entinostat	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
18492664-0	2008	Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.	Adenosine Triphosphate	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
18571929-0	2008	Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): Synthesis, biology, and molecular modeling.	Aminoquinolines	13-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
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
18485433-11	2008	HSP90 inhibitor 17-DMAG sensitized cells to arsenite treatment and increased arsenite-induced centrosome abnormalities.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	16-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18485433-11	2008	HSP90 inhibitor 17-DMAG sensitized cells to arsenite treatment and increased arsenite-induced centrosome abnormalities.	arsenite	44-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18485433-11	2008	HSP90 inhibitor 17-DMAG sensitized cells to arsenite treatment and increased arsenite-induced centrosome abnormalities.	arsenite	77-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18485433-13	2008	Thus, arsenite-induced abnormal centrosome amplification and subsequent mitotic arrest is independent of effects on tubulin polymerization and may be due to specific stresses that are protected against by HSP90 and HSP70.	arsenite	6-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-210
18571929-0	2008	Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): Synthesis, biology, and molecular modeling.	Aminoquinolines	13-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
18571929-4	2008	In a high-throughput screening exercise, we identified quinoline 7 as a moderate inhibitor of Hsp90.	quinoline 7	55-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
19693369-2	2008	The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells.	Adenosine Triphosphate	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19693369-2	2008	The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells.	Adenosine Triphosphate	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
19693369-2	2008	The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19693369-2	2008	The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
19693369-2	2008	The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells.	Adenosine Triphosphate	186-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
19693369-2	2008	The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells.	Adenosine Triphosphate	186-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
18591668-5	2008	Inhibition of Hsp90 function by using small-molecule inhibitors such as 17-allylamino-17-demethoxygeldanamycin (17AAG), and also at the genetic level, blocks TGFbeta-induced signaling and transcriptional responses.	tanespimycin	72-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18456663-4	2008	Inactivation of Hsp90 by geldanamycin led to decreased SGK-1 phosphorylation independently of increased proteasomal protein degradation, and inhibition of PI3K activity by LY294002 appeared to eliminate SGK-1 phosphorylation at the same residues as those affected by geldanamycin treatment.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
18456663-4	2008	Inactivation of Hsp90 by geldanamycin led to decreased SGK-1 phosphorylation independently of increased proteasomal protein degradation, and inhibition of PI3K activity by LY294002 appeared to eliminate SGK-1 phosphorylation at the same residues as those affected by geldanamycin treatment.	geldanamycin	267-279	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
18591668-5	2008	Inhibition of Hsp90 function by using small-molecule inhibitors such as 17-allylamino-17-demethoxygeldanamycin (17AAG), and also at the genetic level, blocks TGFbeta-induced signaling and transcriptional responses.	tanespimycin	112-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18591668-7	2008	Our data reveal an essential level of TGFbeta signaling regulation mediated by Hsp90 by its ability to chaperone TbetaRs and also implicate the use of Hsp90 inhibitors in blocking undesired activation of TGFbeta signaling in diseases.	tbetars	113-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
18356818-3	2008	HSP90 inhibitors such as geldanamycin (GA) or 17-allylaminogeldanamycin result in pharmacologic upregulation of HSP70 and they are currently in clinical testing as cancer therapeutics.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18356818-3	2008	HSP90 inhibitors such as geldanamycin (GA) or 17-allylaminogeldanamycin result in pharmacologic upregulation of HSP70 and they are currently in clinical testing as cancer therapeutics.	geldanamycin	39-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18356818-3	2008	HSP90 inhibitors such as geldanamycin (GA) or 17-allylaminogeldanamycin result in pharmacologic upregulation of HSP70 and they are currently in clinical testing as cancer therapeutics.	tanespimycin	46-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18410996-0	2008	Radiosensitization of human vascular endothelial cells through Hsp90 inhibition with 17-N-allilamino-17-demethoxygeldanamycin.	17-n-allilamino-17-demethoxygeldanamycin	85-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18410996-2	2008	The purpose of the present work is to investigate how 17-N-allilamino-17-demethoxygeldanamycin (17AAG), known as an anticancer drug inhibiting heat shock protein 90 (Hsp90), modifies radiation responses of human vascular ECs.	17-n-allilamino-17-demethoxygeldanamycin	54-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-164
18410996-2	2008	The purpose of the present work is to investigate how 17-N-allilamino-17-demethoxygeldanamycin (17AAG), known as an anticancer drug inhibiting heat shock protein 90 (Hsp90), modifies radiation responses of human vascular ECs.	17-n-allilamino-17-demethoxygeldanamycin	54-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
18279962-5	2008	Interestingly, only in IGROV-1/Pt1 cells, in which cisplatin up-regulated HSP70 and HSP90, targeting of HSP90 resulted in sensitization of resistant cells, suggesting a protective role of stress response.	Cisplatin	51-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
18418407-0	2008	Disruption of the Bcr-Abl/Hsp90 protein complex: a possible mechanism to inhibit Bcr-Abl-positive human leukemic blasts by novobiocin.	Novobiocin	123-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
18449204-9	2008	Furthermore, GRN163L-induced myeloma cell death could be significantly enhanced by Hsp90 inhibitor 17AAG.	tanespimycin	99-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
18260120-0	2008	Stage 1 testing and pharmacodynamic evaluation of the HSP90 inhibitor alvespimycin (17-DMAG, KOS-1022) by the pediatric preclinical testing program.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
18260120-1	2008	BACKGROUND: Alvespimycin (17-DMAG, KOS-1022), a potent small-molecule inhibitor of the protein chaperone Hsp90, is being developed as an anticancer agent because of the multiple Hsp90 client proteins involved in cancer cell growth and survival.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	12-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
18260120-1	2008	BACKGROUND: Alvespimycin (17-DMAG, KOS-1022), a potent small-molecule inhibitor of the protein chaperone Hsp90, is being developed as an anticancer agent because of the multiple Hsp90 client proteins involved in cancer cell growth and survival.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	12-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
18260120-1	2008	BACKGROUND: Alvespimycin (17-DMAG, KOS-1022), a potent small-molecule inhibitor of the protein chaperone Hsp90, is being developed as an anticancer agent because of the multiple Hsp90 client proteins involved in cancer cell growth and survival.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	26-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
18260120-1	2008	BACKGROUND: Alvespimycin (17-DMAG, KOS-1022), a potent small-molecule inhibitor of the protein chaperone Hsp90, is being developed as an anticancer agent because of the multiple Hsp90 client proteins involved in cancer cell growth and survival.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	26-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
18260120-1	2008	BACKGROUND: Alvespimycin (17-DMAG, KOS-1022), a potent small-molecule inhibitor of the protein chaperone Hsp90, is being developed as an anticancer agent because of the multiple Hsp90 client proteins involved in cancer cell growth and survival.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
18260120-1	2008	BACKGROUND: Alvespimycin (17-DMAG, KOS-1022), a potent small-molecule inhibitor of the protein chaperone Hsp90, is being developed as an anticancer agent because of the multiple Hsp90 client proteins involved in cancer cell growth and survival.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	35-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
18400751-2	2008	The activation process depends on the hydrolysis of ATP by Hsp90.	Adenosine Triphosphate	52-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
18400751-3	2008	Hsp90 consists of a C-terminal dimerization domain, a middle domain, which may interact with substrate protein, and an N-terminal ATP-binding domain.	Adenosine Triphosphate	130-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18400751-6	2008	ATP hydrolysis by human Hsp90alpha and Hsp90beta is 10-fold slower than that of yeast Hsp90.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-34
18400751-9	2008	Furthermore, similar to yeast Hsp90, the slow ATP hydrolysis by human Hsp90s can be stimulated up to over 100-fold by the addition of the co-chaperone Aha1 from either human or yeast origin.	Adenosine Triphosphate	46-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
18442981-7	2008	N-Acetylcysteine, a thiol antioxidant, prevented all of the TA-induced effects, including oxidation of heat shock proteins, degradation of Hsp90 client proteins, and apoptosis.	Acetylcysteine	0-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
18410996-2	2008	The purpose of the present work is to investigate how 17-N-allilamino-17-demethoxygeldanamycin (17AAG), known as an anticancer drug inhibiting heat shock protein 90 (Hsp90), modifies radiation responses of human vascular ECs.	tanespimycin	96-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-164
18410996-2	2008	The purpose of the present work is to investigate how 17-N-allilamino-17-demethoxygeldanamycin (17AAG), known as an anticancer drug inhibiting heat shock protein 90 (Hsp90), modifies radiation responses of human vascular ECs.	tanespimycin	96-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
18410996-8	2008	The drug-induced radiosensitization of ECs seems to be caused by prevention of Hsp90-dependent phosphorylation (activation) of Akt that results in blocking the radioprotective phosphatidylinositol 3-kinase/Akt pathway.	Phosphatidylinositols	176-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
18489177-0	2008	Total synthesis of the Hsp90 inhibitor geldanamycin.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18489177-1	2008	An enantioselective synthesis of the Hsp90 inhibitor geldanamycin was achieved in 20 linear steps and 2.0% overall yield from 2-methoxyhydroquinone.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
18489177-1	2008	An enantioselective synthesis of the Hsp90 inhibitor geldanamycin was achieved in 20 linear steps and 2.0% overall yield from 2-methoxyhydroquinone.	2-Methoxyhydroquinone	126-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
18511277-0	2008	Discovery of benzamide tetrahydro-4H-carbazol-4-ones as novel small molecule inhibitors of Hsp90.	benzamide tetrahydro-4h-carbazol-4-ones	13-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
18511277-3	2008	X-ray data show that the scaffold binds competitively at the ATP site on Hsp90.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
18559531-1	2008	Heat shock protein (hsp) 90 is an ATP-dependent molecular chaperone that maintains the active conformation of client oncoproteins in cancer cells.	Adenosine Triphosphate	34-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-27
18559531-3	2008	Knockdown of histone deacetylase (HDAC) 6, which deacetylates lysine residues in hsp90, induces reversible hyperacetylation and attenuates ATP binding and chaperone function of hsp90.	Lysine	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
18559531-3	2008	Knockdown of histone deacetylase (HDAC) 6, which deacetylates lysine residues in hsp90, induces reversible hyperacetylation and attenuates ATP binding and chaperone function of hsp90.	Lysine	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
18559531-3	2008	Knockdown of histone deacetylase (HDAC) 6, which deacetylates lysine residues in hsp90, induces reversible hyperacetylation and attenuates ATP binding and chaperone function of hsp90.	Adenosine Triphosphate	139-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
18559531-3	2008	Knockdown of histone deacetylase (HDAC) 6, which deacetylates lysine residues in hsp90, induces reversible hyperacetylation and attenuates ATP binding and chaperone function of hsp90.	Adenosine Triphosphate	139-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
18559531-4	2008	Here, using mass spectrometry, we identified seven lysine residues in hsp90alpha that are hyperacetylated after treatment of eukaryotic cells with a pan-HDAC inhibitor that also inhibits HDAC6.	Lysine	51-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-80
18559531-5	2008	Depending on the specific lysine residue in the middle domain involved, although acetylation affects ATP, cochaperone, and client protein binding to hsp90alpha, acetylation of all seven lysines increased the binding of hsp90alpha to 17-allyl-amino-demethoxy geldanamycin.	Lysine	26-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-229
18559531-5	2008	Depending on the specific lysine residue in the middle domain involved, although acetylation affects ATP, cochaperone, and client protein binding to hsp90alpha, acetylation of all seven lysines increased the binding of hsp90alpha to 17-allyl-amino-demethoxy geldanamycin.	Lysine	186-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-229
18559531-5	2008	Depending on the specific lysine residue in the middle domain involved, although acetylation affects ATP, cochaperone, and client protein binding to hsp90alpha, acetylation of all seven lysines increased the binding of hsp90alpha to 17-allyl-amino-demethoxy geldanamycin.	17-allyl-amino-demethoxy geldanamycin	233-270	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-229
18559531-6	2008	Notably, after treatment with the pan-HDAC inhibitor panobinostat (LBH589), the extracellular hsp90alpha was hyperacetylated and it bound to MMP-2, which was associated with increased in vitro tumor cell invasiveness.	Panobinostat	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-104
18559531-6	2008	Notably, after treatment with the pan-HDAC inhibitor panobinostat (LBH589), the extracellular hsp90alpha was hyperacetylated and it bound to MMP-2, which was associated with increased in vitro tumor cell invasiveness.	Panobinostat	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-104
18559533-7	2008	Interestingly, AZ628-resistant cells demonstrating either primary drug insensitivity or acquired drug resistance exhibit exquisite sensitivity to the HSP90 inhibitor geldanamycin.	AZ-628	15-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
18559533-7	2008	Interestingly, AZ628-resistant cells demonstrating either primary drug insensitivity or acquired drug resistance exhibit exquisite sensitivity to the HSP90 inhibitor geldanamycin.	geldanamycin	166-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
18485364-12	2008	However, the Hsp90-Hop complex is weakened by the conformational changes that occur in Hsp90 upon ATP binding.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18485364-12	2008	However, the Hsp90-Hop complex is weakened by the conformational changes that occur in Hsp90 upon ATP binding.	Adenosine Triphosphate	98-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
18485364-14	2008	It is likely that Hop binds to both monomers of Hsp90 in the form of a clamp, interacting with residues in the middle domain of Hsp90, thus preventing ATP hydrolysis, possibly by the prevention of association of N-terminal and middle domains in individual Hsp90 monomers.	Adenosine Triphosphate	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
18485364-14	2008	It is likely that Hop binds to both monomers of Hsp90 in the form of a clamp, interacting with residues in the middle domain of Hsp90, thus preventing ATP hydrolysis, possibly by the prevention of association of N-terminal and middle domains in individual Hsp90 monomers.	Adenosine Triphosphate	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
18485364-14	2008	It is likely that Hop binds to both monomers of Hsp90 in the form of a clamp, interacting with residues in the middle domain of Hsp90, thus preventing ATP hydrolysis, possibly by the prevention of association of N-terminal and middle domains in individual Hsp90 monomers.	Adenosine Triphosphate	151-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-133
18511558-4	2008	This study suggests that structural plasticity of the Hsp90 NTD can be exploited by the molecular chaperone machinery to modulate enhanced structural rigidity during ATP binding and increased protein flexibility as a consequence of the inhibitor binding.	Adenosine Triphosphate	166-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
18442981-7	2008	N-Acetylcysteine, a thiol antioxidant, prevented all of the TA-induced effects, including oxidation of heat shock proteins, degradation of Hsp90 client proteins, and apoptosis.	Tantalum	60-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
18442981-9	2008	Taken together, our results demonstrate that the TA inhibits the activity of Hsp90-Hsp70 chaperone complex, at least in part, by a direct thiol oxidation, which in turn leads to the destabilization and depletion of Hsp90 client proteins and thus causes cell cycle arrest and apoptosis in MDA-MB-231 cells.	Sulfhydryl Compounds	138-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
18442981-9	2008	Taken together, our results demonstrate that the TA inhibits the activity of Hsp90-Hsp70 chaperone complex, at least in part, by a direct thiol oxidation, which in turn leads to the destabilization and depletion of Hsp90 client proteins and thus causes cell cycle arrest and apoptosis in MDA-MB-231 cells.	Sulfhydryl Compounds	138-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	215-220
18442981-10	2008	Therefore, TA can be considered as a new type of inhibitor of Hsp90-Hsp70 chaperone complex, which has the potential to be developed as a novel strategy for cancer treatment.	Tantalum	11-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
18218611-9	2008	Gamendazole elicited degradation of the HSP90-dependent client proteins AKT1 and ERBB2 and had an antiproliferative effect in MCF-7 cells without inducing HSP90.	gamendazole	0-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
18385287-0	2008	Asymmetric dimethylarginine inhibits HSP90 activity in pulmonary arterial endothelial cells: role of mitochondrial dysfunction.	dimethylarginine	11-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
18429957-12	2008	We show here that resveratrol could considerably enhance the apoptosis induction in K562 cells by 17-allylamino-17-demethoxygeldanamycin, an anticancer agent that inhibits Hsp90 but augments Hsp70 levels.	Resveratrol	18-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
18385287-7	2008	Finally, we found that the decrease in ATP resulted in a reduction in the chaperone activity of HSP90 resulting in a decrease in its interaction with eNOS.	Adenosine Triphosphate	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
18455150-2	2008	The requirement of Hsp90 activity in the NF-kappaB pathway has been recently reported by several authors using the Hsp90 ATPase inhibitor geldanamycin (GA), an anti-tumor drug.	geldanamycin	138-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
18455150-2	2008	The requirement of Hsp90 activity in the NF-kappaB pathway has been recently reported by several authors using the Hsp90 ATPase inhibitor geldanamycin (GA), an anti-tumor drug.	geldanamycin	138-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
18455150-2	2008	The requirement of Hsp90 activity in the NF-kappaB pathway has been recently reported by several authors using the Hsp90 ATPase inhibitor geldanamycin (GA), an anti-tumor drug.	geldanamycin	152-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
18455150-2	2008	The requirement of Hsp90 activity in the NF-kappaB pathway has been recently reported by several authors using the Hsp90 ATPase inhibitor geldanamycin (GA), an anti-tumor drug.	geldanamycin	152-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
18455150-3	2008	Hsp90 inhibition blocks the synthesis and activation of the IKK complex, the major kinases complex responsible for IkappaBalpha phosphorylation on serine 32 and 36, a key step for its degradation and the nuclear translocation of NF-kappaB.	Serine	147-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18455150-10	2008	We conclude that c-Src requires Hsp90 for its tyrosine kinase activity, and its inhibition by GA blocks c-Src-dependent signalling pathways, such as NF-kappaB activation induced by sodium pervanadate.	geldanamycin	94-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
18455150-10	2008	We conclude that c-Src requires Hsp90 for its tyrosine kinase activity, and its inhibition by GA blocks c-Src-dependent signalling pathways, such as NF-kappaB activation induced by sodium pervanadate.	Sodium orthovanadate	181-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
18620539-6	2008	Geldanamycin, a specific inhibitor of heat shock protein Hsp90, completely abolished the antiapoptotic effect of 0.1 nM APC on glutamate-induced cytotoxicity in the hippocampal neurons.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18620539-6	2008	Geldanamycin, a specific inhibitor of heat shock protein Hsp90, completely abolished the antiapoptotic effect of 0.1 nM APC on glutamate-induced cytotoxicity in the hippocampal neurons.	Glutamic Acid	127-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18281615-1	2008	PURPOSE: The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) has been shown to have promising results in antitumor activity through the degradation of the activated V600E mutant of B-Raf (V600E B-Raf) in cutaneous melanoma cell lines.	tanespimycin	29-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18281615-1	2008	PURPOSE: The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) has been shown to have promising results in antitumor activity through the degradation of the activated V600E mutant of B-Raf (V600E B-Raf) in cutaneous melanoma cell lines.	tanespimycin	69-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18281615-5	2008	METHODS: Human uveal melanoma cell lines were treated with the HSP90 inhibitors 17-AAG and 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17-DMAG).	tanespimycin	80-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18281615-5	2008	METHODS: Human uveal melanoma cell lines were treated with the HSP90 inhibitors 17-AAG and 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17-DMAG).	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	145-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18520302-8	2008	Several new classes of Hsp90 inhibitors are emerging, including purines and pyrazoles that have entered phase 1 trials.	Purines	64-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18520302-8	2008	Several new classes of Hsp90 inhibitors are emerging, including purines and pyrazoles that have entered phase 1 trials.	Pyrazoles	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18429957-12	2008	We show here that resveratrol could considerably enhance the apoptosis induction in K562 cells by 17-allylamino-17-demethoxygeldanamycin, an anticancer agent that inhibits Hsp90 but augments Hsp70 levels.	tanespimycin	98-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
18343820-11	2008	Interestingly, we observed that ethanol treatment resulted in an increase in TH association with the chaperone heat shock protein (HSP90) that was mediated by the cAMP/PKA pathway and inhibited by GDNF.	Ethanol	32-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
18440021-0	2008	The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ.	monorden	20-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
18440021-0	2008	The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
18440021-0	2008	The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ.	phoq	95-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
18440021-1	2008	Sensor kinases in the bacterial two-component system share a unique ATP-binding Bergerat fold with the GHL (gyrase, Hsp90, and MutL) family of proteins.	Adenosine Triphosphate	68-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
18440021-3	2008	Using crystallographic approaches, we show that radicicol (an Hsp90 inhibitor) binds and interacts specifically with residues in the ATP-binding pocket of PhoQ.	monorden	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
18440021-3	2008	Using crystallographic approaches, we show that radicicol (an Hsp90 inhibitor) binds and interacts specifically with residues in the ATP-binding pocket of PhoQ.	Adenosine Triphosphate	133-136	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
18440021-3	2008	Using crystallographic approaches, we show that radicicol (an Hsp90 inhibitor) binds and interacts specifically with residues in the ATP-binding pocket of PhoQ.	phoq	155-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
18440021-4	2008	The interaction between radicicol and PhoQcat demonstrates significant similarities as well as differences compared to AMPPNP (a non-hydrolyzable ATP analog) bound to PhoQcat and radicicol bound to Hsp90.	monorden	24-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
18440021-4	2008	The interaction between radicicol and PhoQcat demonstrates significant similarities as well as differences compared to AMPPNP (a non-hydrolyzable ATP analog) bound to PhoQcat and radicicol bound to Hsp90.	monorden	179-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
18343820-11	2008	Interestingly, we observed that ethanol treatment resulted in an increase in TH association with the chaperone heat shock protein (HSP90) that was mediated by the cAMP/PKA pathway and inhibited by GDNF.	Cyclic AMP	163-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-136
18343820-12	2008	Taken together, these data suggest that prolonged ethanol exposure leads to increased association of TH and HSP90 via the cAMP/PKA pathway, resulting in the stabilization and subsequent accumulation of TH.	Ethanol	50-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
18343820-12	2008	Taken together, these data suggest that prolonged ethanol exposure leads to increased association of TH and HSP90 via the cAMP/PKA pathway, resulting in the stabilization and subsequent accumulation of TH.	Cyclic AMP	122-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
18343820-13	2008	GDNF reverses this ethanol-mediated adaptation by inhibiting the interaction of TH with HSP90.	Ethanol	19-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
18342836-7	2008	In addition, we showed that inactivation of the heat shock protein-90 (Hsp90) is involved in SAHA-induced ERalpha degradation, and ubiquitin ligase CHIP (C-terminal Hsc70 interacting protein) enhances SAHA-induced ERalpha degradation.	Vorinostat	93-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-69
18342836-7	2008	In addition, we showed that inactivation of the heat shock protein-90 (Hsp90) is involved in SAHA-induced ERalpha degradation, and ubiquitin ligase CHIP (C-terminal Hsc70 interacting protein) enhances SAHA-induced ERalpha degradation.	Vorinostat	93-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
18342836-7	2008	In addition, we showed that inactivation of the heat shock protein-90 (Hsp90) is involved in SAHA-induced ERalpha degradation, and ubiquitin ligase CHIP (C-terminal Hsc70 interacting protein) enhances SAHA-induced ERalpha degradation.	Vorinostat	201-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
18683558-1	2008	Geldanamycin (GA), an ansamycin antibiotic specifically binding heat shock protein 90 (Hsp90), exhibits a broad-spectrum antiviral effect.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
18373709-4	2008	The present study showed that inhibition of Hsp90 by 17-allylamino-17-demethoxygeldanamycin (17-AAG) was cytotoxic to primary AML cells expressing mutant FLT3.	tanespimycin	53-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
18373709-4	2008	The present study showed that inhibition of Hsp90 by 17-allylamino-17-demethoxygeldanamycin (17-AAG) was cytotoxic to primary AML cells expressing mutant FLT3.	tanespimycin	93-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
18373709-5	2008	Inhibition of Hsp90 results in altered downstream signalling effects in primary AML cells with disruption of Janus kinase-signal transducer and activator of transcription (JAK-STAT), mitogen-activated protein kinase and phosphatidylinositol 3/AKT signalling pathways.	Phosphatidylinositols	220-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18683558-1	2008	Geldanamycin (GA), an ansamycin antibiotic specifically binding heat shock protein 90 (Hsp90), exhibits a broad-spectrum antiviral effect.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
18683558-1	2008	Geldanamycin (GA), an ansamycin antibiotic specifically binding heat shock protein 90 (Hsp90), exhibits a broad-spectrum antiviral effect.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
18683558-1	2008	Geldanamycin (GA), an ansamycin antibiotic specifically binding heat shock protein 90 (Hsp90), exhibits a broad-spectrum antiviral effect.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
18683558-1	2008	Geldanamycin (GA), an ansamycin antibiotic specifically binding heat shock protein 90 (Hsp90), exhibits a broad-spectrum antiviral effect.	Rifabutin	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-85
18683558-1	2008	Geldanamycin (GA), an ansamycin antibiotic specifically binding heat shock protein 90 (Hsp90), exhibits a broad-spectrum antiviral effect.	Rifabutin	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
18347582-0	2008	Conjugated linoleic acids produced by Lactobacillus dissociates IKK-gamma and Hsp90 complex in Helicobacter pylori-infected gastric epithelial cells.	Linoleic Acids	11-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
17624530-0	2008	IPI-504, a novel and soluble HSP-90 inhibitor, blocks the unfolded protein response in multiple myeloma cells.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-35
17624530-2	2008	Here, we investigate the effect of IPI-504, a novel and highly soluble inhibitor of the Hsp90 ATPase activity, on the unfolded protein response (UPR) in MM cells.	tanespimycin	35-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
18194434-0	2008	Dopamine-induced toxicity is synergistically potentiated by simultaneous HSP-90 and Akt inhibition in oligodendrocyte progenitors.	Dopamine	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-79
18347582-2	2008	This study investigates the role of conjugated linoleic acids (CLA) produced by probiotics in interactions of IkappaB kinase (IKK) and heat shock protein 90 (Hsp90) to activate the nuclear factor-kappaB (NF-kappaB) signaling pathway in human gastric epithelial cells infected with H. pylori.	Linoleic Acids	47-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-156
18347582-2	2008	This study investigates the role of conjugated linoleic acids (CLA) produced by probiotics in interactions of IkappaB kinase (IKK) and heat shock protein 90 (Hsp90) to activate the nuclear factor-kappaB (NF-kappaB) signaling pathway in human gastric epithelial cells infected with H. pylori.	Linoleic Acids	47-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
18347582-2	2008	This study investigates the role of conjugated linoleic acids (CLA) produced by probiotics in interactions of IkappaB kinase (IKK) and heat shock protein 90 (Hsp90) to activate the nuclear factor-kappaB (NF-kappaB) signaling pathway in human gastric epithelial cells infected with H. pylori.	Linoleic Acids, Conjugated	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-156
18347582-2	2008	This study investigates the role of conjugated linoleic acids (CLA) produced by probiotics in interactions of IkappaB kinase (IKK) and heat shock protein 90 (Hsp90) to activate the nuclear factor-kappaB (NF-kappaB) signaling pathway in human gastric epithelial cells infected with H. pylori.	Linoleic Acids, Conjugated	63-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
18347582-6	2008	Furthermore, Hsp90 was associated with IKK-alpha and IKK-gamma in H. pylori-infected cells, and CM with CLA dissociated the complex between Hsp90 and IKK-gamma.	Linoleic Acids, Conjugated	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
18505931-7	2008	Treatment with LBH589 induces hyperacetylation of Hsp90, thereby inhibiting the association of DNMT1 with Hsp90 and promoting ubiquitination of DNMT1.	Panobinostat	15-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
18445155-6	2008	The heat shock protein Hsp90 was identified by peptide sequencing as a major fluorescent band on SDS-PAGE of lysine-labelled Walker cell extracts.	Sodium Dodecyl Sulfate	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18445155-6	2008	The heat shock protein Hsp90 was identified by peptide sequencing as a major fluorescent band on SDS-PAGE of lysine-labelled Walker cell extracts.	Lysine	109-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18359116-4	2008	When cells were treated with an Hsp90 inhibitor (geldanamycin or novobiocin), levels of PINK1 were greatly diminished, reflecting its rapid degradation via ubiquitin-proteasome pathway.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
18359116-4	2008	When cells were treated with an Hsp90 inhibitor (geldanamycin or novobiocin), levels of PINK1 were greatly diminished, reflecting its rapid degradation via ubiquitin-proteasome pathway.	Novobiocin	65-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
18505931-7	2008	Treatment with LBH589 induces hyperacetylation of Hsp90, thereby inhibiting the association of DNMT1 with Hsp90 and promoting ubiquitination of DNMT1.	Panobinostat	15-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
18313664-4	2008	Various pre- and clinical studies have revealed that heat shock protein 90 (HSP90) inhibitors, such as geldanamycin and radicicol, are promising drugs in the treatment of different malignant processes.	geldanamycin	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-74
18313664-4	2008	Various pre- and clinical studies have revealed that heat shock protein 90 (HSP90) inhibitors, such as geldanamycin and radicicol, are promising drugs in the treatment of different malignant processes.	geldanamycin	103-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
18313664-4	2008	Various pre- and clinical studies have revealed that heat shock protein 90 (HSP90) inhibitors, such as geldanamycin and radicicol, are promising drugs in the treatment of different malignant processes.	monorden	120-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-74
18313664-4	2008	Various pre- and clinical studies have revealed that heat shock protein 90 (HSP90) inhibitors, such as geldanamycin and radicicol, are promising drugs in the treatment of different malignant processes.	monorden	120-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
18363347-1	2008	A series of substituted quinoline-5,8-diones were synthesized and evaluated as inhibitors of the chaperone protein Hsp90 using two assays: competition for binding to C-terminal ATP-binding site and competition for binding to N-terminal ATP-binding site.	quinoline-5,8-diones	24-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
18413753-1	2008	We describe the biological properties of NVP-AUY922, a novel resorcinylic isoxazole amide heat shock protein 90 (HSP90) inhibitor.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-111
18413753-1	2008	We describe the biological properties of NVP-AUY922, a novel resorcinylic isoxazole amide heat shock protein 90 (HSP90) inhibitor.	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide	45-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
18413753-1	2008	We describe the biological properties of NVP-AUY922, a novel resorcinylic isoxazole amide heat shock protein 90 (HSP90) inhibitor.	isoxazole amide	74-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-111
18413753-1	2008	We describe the biological properties of NVP-AUY922, a novel resorcinylic isoxazole amide heat shock protein 90 (HSP90) inhibitor.	isoxazole amide	74-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	113-118
17982489-4	2008	Primary CLL cells of defined ataxia telangiectasia mutated (ATM)/p53 status were incubated with the Hsp90 inhibitor geldanamycin (GA) and analysed by western blotting for the expression of p53, p21, MDM2 and Akt.	geldanamycin	116-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
18216498-7	2008	In parallel, OSU causes PERK-dependent increases in HSP70 expression and decreases in HSP90 and Grp78/BiP expression.	osu	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
18304811-0	2008	Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90).	denoviose	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-135
18304811-0	2008	Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90).	denoviose	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
18304811-0	2008	Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90).	Coumarins	58-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-135
18304811-0	2008	Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90).	Coumarins	58-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
18304811-0	2008	Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90).	Novobiocin	79-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-135
18304811-0	2008	Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90).	Novobiocin	79-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
18304811-1	2008	A new series of coumarin inhibitors of hsp90 lacking the noviose moiety as well as substituents on C-7 and C-8 positions of the aromatic ring was synthesised and their hsp90 inhibitory activity has been delineated: for example, their capacity to induce the degradation of client proteins and to inhibit estradiol-induced transcription in human breast cancer cells.	coumarin	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
18304811-1	2008	A new series of coumarin inhibitors of hsp90 lacking the noviose moiety as well as substituents on C-7 and C-8 positions of the aromatic ring was synthesised and their hsp90 inhibitory activity has been delineated: for example, their capacity to induce the degradation of client proteins and to inhibit estradiol-induced transcription in human breast cancer cells.	coumarin	16-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
18304811-1	2008	A new series of coumarin inhibitors of hsp90 lacking the noviose moiety as well as substituents on C-7 and C-8 positions of the aromatic ring was synthesised and their hsp90 inhibitory activity has been delineated: for example, their capacity to induce the degradation of client proteins and to inhibit estradiol-induced transcription in human breast cancer cells.	noviose	57-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
17579866-3	2008	Hsp90 inhibitors which are derivates of the natural compound geldanamycin, such as the orally bioavailable 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), are currently being tested in clinical trials and small molecule inhibitors are in development.	geldanamycin	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17579866-3	2008	Hsp90 inhibitors which are derivates of the natural compound geldanamycin, such as the orally bioavailable 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), are currently being tested in clinical trials and small molecule inhibitors are in development.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	107-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17579866-3	2008	Hsp90 inhibitors which are derivates of the natural compound geldanamycin, such as the orally bioavailable 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), are currently being tested in clinical trials and small molecule inhibitors are in development.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	162-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17579866-19	2008	Additional factors might be (1) an altered abundance and/or activity of primary (Hsp90) and secondary (e.g., Akt) target(s), (2) a narrow therapeutic range of 17-DMAG by oral application and (3) response-modifying factors within the tumor environment.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	159-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
18375819-2	2008	BRAF that is activated by the common V600E and other mutations, as well as by upstream NRAS mutations, has been shown to require the molecular chaperone heat shock protein 90 (HSP90) for stabilization and is depleted by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG)].	tanespimycin	240-278	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-174
18375819-2	2008	BRAF that is activated by the common V600E and other mutations, as well as by upstream NRAS mutations, has been shown to require the molecular chaperone heat shock protein 90 (HSP90) for stabilization and is depleted by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG)].	tanespimycin	240-278	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
18375819-2	2008	BRAF that is activated by the common V600E and other mutations, as well as by upstream NRAS mutations, has been shown to require the molecular chaperone heat shock protein 90 (HSP90) for stabilization and is depleted by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG)].	tanespimycin	240-278	heat shock protein 90 alpha family class A member 1	Homo sapiens	224-229
18182481-4	2008	In parallel, OSU caused PERK-dependent increases in 70-kDa heat shock protein (HSP70) expression and decreases in 90-kDa heat shock protein (HSP90) and Grp78/BiP expression.	osu	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
18193284-3	2008	Inhibition of Hsp90 activity by geldanamycin (GA) reduced cell growth and increased the level of Hsp90.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18193284-3	2008	Inhibition of Hsp90 activity by geldanamycin (GA) reduced cell growth and increased the level of Hsp90.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
18193284-4	2008	Both the bloodstream and procyclic forms of T. brucei showed a several-fold greater sensitivity than the mammalian cells to GA and also to 17-AAG, a less toxic derivative of GA, suggesting that Hsp90 could be a potential chemotherapeuric target for African trypanosomiasis.	tanespimycin	139-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199
18193284-10	2008	Together, these results suggest that TbPP5 positively regulates the function of Hsp90 to maintain cellular homeostasis during proteotoxic stresses in T. brucei.	tbpp5	37-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
18293999-1	2008	Recent studies have shown that the DNA gyrase inhibitor, novobiocin, binds to a previously unrecognized ATP-binding site located at the C-terminus of Hsp90 and induces degradation of Hsp90-dependent client proteins at approximately 700 microM.	Novobiocin	57-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
18293999-1	2008	Recent studies have shown that the DNA gyrase inhibitor, novobiocin, binds to a previously unrecognized ATP-binding site located at the C-terminus of Hsp90 and induces degradation of Hsp90-dependent client proteins at approximately 700 microM.	Novobiocin	57-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
18293999-1	2008	Recent studies have shown that the DNA gyrase inhibitor, novobiocin, binds to a previously unrecognized ATP-binding site located at the C-terminus of Hsp90 and induces degradation of Hsp90-dependent client proteins at approximately 700 microM.	Adenosine Triphosphate	104-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
18293999-2	2008	As a result of these studies, several analogues of the coumarin family of antibiotics have been reported and shown to exhibit increased Hsp90 inhibitory activity; however, the monomeric species lacked the ability to manifest anti-proliferative activity against cancer cell lines at concentrations tested.	coumarin	55-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
18242595-4	2008	Treatment of endothelial cells with geldanamycin, a commonly used HSP90 inhibitor, augmented HGF-stimulated eNOS phosphorylation at Ser-1179, while it did not alter eNOS phosphorylation at Thr-497.	geldanamycin	36-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
18347186-2	2008	EXPERIMENTAL DESIGN: The anticancer effects of an HSP90 inhibitor (geldanamycin) in pancreatic cells were investigated in hypoxia and normoxia.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
18347186-3	2008	A hexokinase II inhibitor, 3-broma-pyruvate (3BrPA), was evaluated for selective glycolysis inhibition in hypoxia as a sensitizer of HSP90 inhibitor against pancreatic cancer.	3brpa	45-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
18347186-7	2008	3BrPA selectively inhibited glycolysis and sensitized geldanamycin against pancreatic cancer cells by 17- to 400-fold through HSP90 client protein degradation.	3brpa	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
18182164-1	2008	We investigated the role of Heat shock protein 90 (Hsp90) in vitamin D action in Caco-2 cells using geldanamycin (GA) to block Hsp90 function and RNA interference to reduce Hsp90beta expression.	Vitamin D	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-49
18182164-1	2008	We investigated the role of Heat shock protein 90 (Hsp90) in vitamin D action in Caco-2 cells using geldanamycin (GA) to block Hsp90 function and RNA interference to reduce Hsp90beta expression.	Vitamin D	61-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
17891170-0	2008	Proapoptotic role of Hsp90 by its interaction with c-Jun N-terminal kinase in lipid rafts in edelfosine-mediated antileukemic therapy.	edelfosine	93-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
17891170-2	2008	However, we have found that inhibitors of Hsp90 diminished the apoptotic response induced in leukemic cells by the antitumor alkyl-lysophospholipid analog edelfosine, which acts through lipid raft reorganization.	2-O-Methyl-PAF (C)	125-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
17891170-2	2008	However, we have found that inhibitors of Hsp90 diminished the apoptotic response induced in leukemic cells by the antitumor alkyl-lysophospholipid analog edelfosine, which acts through lipid raft reorganization.	edelfosine	155-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
17891170-3	2008	Edelfosine treatment recruited Hsp90, c-Jun N-terminal kinase (JNK) and apoptotic molecules in lipid rafts, but not the JNK regulators apoptosis signal-regulating kinase 1 (ASK1) and Daxx, or the survival signaling molecules extracellular signal-regulated kinase (ERK) and Akt.	edelfosine	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
17891170-4	2008	Following edelfosine treatment, Hsp90 bound to JNK in lipid rafts and Hsp90-JNK clusters were identified at the plasma membrane by immunoelectron microscopy.	edelfosine	10-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
17891170-4	2008	Following edelfosine treatment, Hsp90 bound to JNK in lipid rafts and Hsp90-JNK clusters were identified at the plasma membrane by immunoelectron microscopy.	edelfosine	10-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
17891170-5	2008	Hsp90 inhibition reduced JNK protein level in lipid rafts and turned proapoptotic persistent JNK activation into a transient response in edelfosine-treated cells.	edelfosine	137-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17891170-6	2008	Decrease in edelfosine-induced JNK activation and apoptosis by Hsp90 inhibition was prevented through proteasome inhibition, suggesting that Hsp90 inhibition diminishes apoptosis by promoting JNK protein degradation.	edelfosine	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
17891170-6	2008	Decrease in edelfosine-induced JNK activation and apoptosis by Hsp90 inhibition was prevented through proteasome inhibition, suggesting that Hsp90 inhibition diminishes apoptosis by promoting JNK protein degradation.	edelfosine	12-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
18211007-6	2008	The N-terminal site involves noncontiguous amino acids within or near the ATP binding pocket of Hsp90.	Adenosine Triphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
18065756-6	2008	We demonstrated that the interaction of SMYD2 with HSP90alpha enhances SMYD2 histone methyltransferase activity and specificity for histone H3 at lysine 4 (H3K4) in vitro.	lysine 4	146-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-61
18347135-0	2008	Dicoumarol down-regulates human PTTG1/Securin mRNA expression through inhibition of Hsp90.	Dicumarol	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
18347135-3	2008	Dicoumarol, a long-established oral anticoagulant, is a new Hsp90 inhibitor that represses PTTG1/Securin gene expression and provokes apoptosis through a complex trait involving both intrinsic and extrinsic pathways.	Dicumarol	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
18347135-4	2008	Dicoumarol activity as an Hsp90 inhibitor is confirmed by smaller levels of Hsp90 clients in treated cells and inhibition of in vivo heat shock luciferase activity recovery assays.	Dicumarol	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
18347135-4	2008	Dicoumarol activity as an Hsp90 inhibitor is confirmed by smaller levels of Hsp90 clients in treated cells and inhibition of in vivo heat shock luciferase activity recovery assays.	Dicumarol	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
18347135-5	2008	Likewise, established Hsp90 inhibitors (17-allylamino-geldanamycin and novobiocin) repress PTTG1/Securin gene expression.	tanespimycin	40-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
18347135-5	2008	Likewise, established Hsp90 inhibitors (17-allylamino-geldanamycin and novobiocin) repress PTTG1/Securin gene expression.	Novobiocin	71-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
18347135-6	2008	Also, overexpression of human Hsp90 in yeast makes them hypersensitive to dicoumarol.	Dicumarol	74-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
18347135-9	2008	Overall, we show that expression of PTTG1/Securin gene is Hsp90 dependent and that dicoumarol is a bona fide Hsp90 inhibitor.	Dicumarol	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
18347151-9	2008	Importantly, the Hsp90 inhibitor geldanamycin effectively down-regulates AR expression while having no effect on neuroendocrine differentiation.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
18630678-1	2008	OBJECTIVE: To investigate the effect of heat shock protein 90 (Hsp90) function inhibited on the telomerase activity and P53 expression in human breast cancer cells, in which a specific inhibitor geldanamycin (GA) was used to inhibit Hsp90 function.	geldanamycin	195-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
18290764-4	2008	Hsp90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18630678-1	2008	OBJECTIVE: To investigate the effect of heat shock protein 90 (Hsp90) function inhibited on the telomerase activity and P53 expression in human breast cancer cells, in which a specific inhibitor geldanamycin (GA) was used to inhibit Hsp90 function.	geldanamycin	195-207	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18630678-1	2008	OBJECTIVE: To investigate the effect of heat shock protein 90 (Hsp90) function inhibited on the telomerase activity and P53 expression in human breast cancer cells, in which a specific inhibitor geldanamycin (GA) was used to inhibit Hsp90 function.	geldanamycin	209-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
18630678-1	2008	OBJECTIVE: To investigate the effect of heat shock protein 90 (Hsp90) function inhibited on the telomerase activity and P53 expression in human breast cancer cells, in which a specific inhibitor geldanamycin (GA) was used to inhibit Hsp90 function.	geldanamycin	209-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18630678-10	2008	CONCLUSION: The telomerase activation and mutant P53 expression in MDA-MB-435s cells are related to HSP90 function, of which the inhibition with GA can decrease the telomerase activity and the protein expression of mutant P53, and further repress the proliferation of MDA-MB-435s cells.	geldanamycin	145-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
18281495-3	2008	Treatment of cells with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) results in the degradation of client proteins via the ubiquitin-proteasome pathway.	tanespimycin	84-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
18047824-1	2008	Heat shock protein 90 alpha (Hsp90alpha) was immobilized on aminopropyl silica via the N terminus to create the Hsp90alpha(NT) column or via the C terminus to create the Hsp90alpha(CT) column.	aminopropyl silica	60-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-39
18047824-2	2008	Binding to the exposed C terminus on the Hsp90alpha(NT) column was characterized using frontal chromatography and the C-terminus ligands coumermycin A(1) (CA1) and novobiocin (NOVO).	coumermycin a	137-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-51
18047824-2	2008	Binding to the exposed C terminus on the Hsp90alpha(NT) column was characterized using frontal chromatography and the C-terminus ligands coumermycin A(1) (CA1) and novobiocin (NOVO).	coumermycin	155-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-51
18047824-2	2008	Binding to the exposed C terminus on the Hsp90alpha(NT) column was characterized using frontal chromatography and the C-terminus ligands coumermycin A(1) (CA1) and novobiocin (NOVO).	Novobiocin	164-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-51
18281495-0	2008	Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	141-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
18281495-0	2008	Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	141-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
18281495-1	2008	AHA1 (activator of HSP90 ATPase) is a cochaperone of the ATP-dependent molecular chaperone, HSP90, which is involved in the maturation, stabilization/degradation, and function of oncogenic proteins.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
18281495-1	2008	AHA1 (activator of HSP90 ATPase) is a cochaperone of the ATP-dependent molecular chaperone, HSP90, which is involved in the maturation, stabilization/degradation, and function of oncogenic proteins.	Adenosine Triphosphate	25-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
18281495-2	2008	HSP90 operates in a multimeric complex driven by the binding and hydrolysis of ATP.	Adenosine Triphosphate	79-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18281495-3	2008	Treatment of cells with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) results in the degradation of client proteins via the ubiquitin-proteasome pathway.	tanespimycin	44-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
18281495-4	2008	As AHA1 increases the ATPase activity of HSP90, we hypothesized that modulation of AHA1 expression could influence the activity of client proteins and/or the cellular response to 17-AAG.	tanespimycin	179-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
18197612-0	2008	Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90.	benzisoxazoles	13-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
17724475-3	2008	Indeed, we found that NF-kappaB factors bound to one of the two putative consensus sequences present in the hsp90alpha-flanking region; mutation of such motif hampered the phorbol-myristate-13-acetate-stimulated expression of a luciferase reporter gene under the control of the hsp90alpha promoter.	phorbol-myristate-13-acetate	172-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-118
17724475-3	2008	Indeed, we found that NF-kappaB factors bound to one of the two putative consensus sequences present in the hsp90alpha-flanking region; mutation of such motif hampered the phorbol-myristate-13-acetate-stimulated expression of a luciferase reporter gene under the control of the hsp90alpha promoter.	phorbol-myristate-13-acetate	172-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	278-288
18197612-2	2008	We have identified small-molecule benzisoxazole derivatives as Hsp90 inhibitors.	1,2-Benzisoxazole	34-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18081892-6	2008	Because ATO is known to induce a HS-like response in a variety of cells, we investigated its ability to induce gene expression of Hsp in neutrophils and found that ATO increases HSP90AA1, HSPA1 and HSPB1 mRNA in these cells.	Arsenic Trioxide	164-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-186
18245548-2	2008	EXPERIMENTAL DESIGN: Hsp90 expression was determined by immunohistochemistry in 44 paraffin-embedded sections of primary human uveal melanoma and in five uveal melanoma cell lines (92.1, OCM-1, MKT-BR, SP6.5, and UW-1).	Paraffin	83-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
18245548-6	2008	RESULTS: Immunohistochemical expression of Hsp90 was identified in 68% of the paraffin-embedded sections and significantly associated with largest tumor dimension (P = 0.03).	Paraffin	78-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
18245550-3	2008	RESULTS: The combination of Akt inhibitor perifosine and HSP90 inhibitor 17-DMAG was synergistic in inducing MM cell cytotoxicity, evidenced by inhibition of DNA synthesis and induction of apoptosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	73-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
18303190-1	2008	When human neuroblastoma cells (SH-SY5Y) were exposed to 0.5 - 5 mM acrylamide for 18 hr, the levels of heat shock proteins (HSPs) of 90, 70 and 27 kDa (Hsp90, Hsp70, and Hsp27, respectively) were elevated in the incubation media depending on the dose of acrylamide whereas only the Hsp70 level increased within cells.	Acrylamide	68-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
18045990-4	2008	Hsp90 binding to PMR1 is inhibited by geldanamycin, and geldanamycin stabilizes substrate mRNA to PMR1-mediated decay.	geldanamycin	38-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18045990-6	2008	We present a model where Hsp90 interacts transiently to stabilize PMR1 in a manner similar to its interaction with c-Src, thus facilitating the tyrosine phosphorylation and targeting of PMR1 to polysomes.	Tyrosine	144-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
18056992-5	2008	Here we present evidence, using glutathione S-transferase pull-down and transfection assays, for a novel interaction between surface HSP90 and the extracellular domain of HER-2.	Glutathione	32-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
18020435-0	2008	4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer.	4,5-diarylisoxazole	0-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
18020435-2	2008	Here, we describe the structure-based design, synthesis, structure-activity relationships and pharmacokinetics of potent small-molecule inhibitors of Hsp90 based on the 4,5-diarylisoxazole scaffold.	4,5-diarylisoxazole	169-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
18155168-3	2008	Here we show that prolonged hsp90 inhibition in different cell types reduces protein levels of both sGC subunits by about half, an effect that was prevented by the proteasome inhibitor MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	185-190	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
18024423-5	2008	Destabilization of PDK1 induced by geldanamycin (a Hsp90 inhibitor) was partially blocked in HEK 293 cells expressing PDK1-Y9F.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
18024423-9	2008	Furthermore, Tyr(9) phosphorylation is critical for the stabilization of both PDK1 and the PDK1/Src complex via Hsp90-mediated protection of PDK1 degradation.	Tyrosine	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
18199556-0	2008	Inhibition of Hsp90 down-regulates mutant epidermal growth factor receptor (EGFR) expression and sensitizes EGFR mutant tumors to paclitaxel.	Paclitaxel	130-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
18199556-3	2008	Hsp90 inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG), induce the degradation of EGFR and other Hsp90 interacting proteins and may thus have utility in tumors dependent upon sensitive Hsp90 clients.	tanespimycin	26-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
18199556-3	2008	Hsp90 inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG), induce the degradation of EGFR and other Hsp90 interacting proteins and may thus have utility in tumors dependent upon sensitive Hsp90 clients.	tanespimycin	26-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
18199556-3	2008	Hsp90 inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG), induce the degradation of EGFR and other Hsp90 interacting proteins and may thus have utility in tumors dependent upon sensitive Hsp90 clients.	tanespimycin	26-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
19850986-2	2008	As resistance against Imatinib a Bcr-abl inhibitor used in CML, was described, Heat shock protein (Hsp90) became an alternative target as inhibition of Bcr-Abl-Hsp90 complex leads to proliferation arrest.	Imatinib Mesylate	22-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
18364744-0	2008	A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates.	cochaperones	59-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-26
18364744-3	2008	This question was addressed by examining potential differences between the Hsp90 isoforms with respect to both cochaperone and substrate interactions.	cochaperone	111-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
18060774-2	2008	While inhibitors of Hsp90, such as geldanamycin and its derivative 17-AAG, are well known and important anti-cancer leads, Hsp70 has received less attention.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
18060774-2	2008	While inhibitors of Hsp90, such as geldanamycin and its derivative 17-AAG, are well known and important anti-cancer leads, Hsp70 has received less attention.	tanespimycin	67-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
19014541-9	2008	Both prolactin and its downstream protein effector, HSP90alpha, promote survival, as shown by apoptosis assays and by the addition of the HSP90 inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), in both untransformed HC11 mammary epithelial cells and SKBR3 breast cancer cells.	tanespimycin	155-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-62
17909811-1	2008	PURPOSE: The Hsp90-directed anticancer agent 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) is currently undergoing phase I and phase II clinical investigation.	tanespimycin	45-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
19850986-2	2008	As resistance against Imatinib a Bcr-abl inhibitor used in CML, was described, Heat shock protein (Hsp90) became an alternative target as inhibition of Bcr-Abl-Hsp90 complex leads to proliferation arrest.	Imatinib Mesylate	22-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
19850986-3	2008	Here, we used natural product Radicicol (Rad), a macrocyclic antifungal, as an Hsp90 inhibitor to investigate the effect of Bcr-Abl inactivation on erythroid gene expression and subsequently on the transcription factors involved in their regulation.	monorden	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
18347418-1	2008	Heat shock protein 90 (Hsp90) is an ATP-dependent chaperone and a noteworthy component of cellular folding machinery in eukaryotes and bacteria.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
18347418-1	2008	Heat shock protein 90 (Hsp90) is an ATP-dependent chaperone and a noteworthy component of cellular folding machinery in eukaryotes and bacteria.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
18673171-1	2008	Heat shock protein (Hsp90) inhibitors are an increasingly interesting and important class of compounds where the first in class, natural product derived inhibitors such as 17-allylaminogeldanamycin (17-AAG), are entering late stage clinical development.	tanespimycin	172-197	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
18172314-2	2008	Small molecule Hsp90 inhibitors block Hsp90 alpha/p23 and Hsp90 beta/p23 interactions in part by preventing ATP binding to Hsp90.	Adenosine Triphosphate	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
18172314-2	2008	Small molecule Hsp90 inhibitors block Hsp90 alpha/p23 and Hsp90 beta/p23 interactions in part by preventing ATP binding to Hsp90.	Adenosine Triphosphate	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-49
18172314-2	2008	Small molecule Hsp90 inhibitors block Hsp90 alpha/p23 and Hsp90 beta/p23 interactions in part by preventing ATP binding to Hsp90.	Adenosine Triphosphate	108-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
18172314-5	2008	The three geldanamycin-based and seven purine-scaffold Hsp90 inhibitors led to different levels of inhibition of complemented RL activities (10-70%).	purine	39-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
18991631-0	2008	Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
18991631-8	2008	Initial studies by Csermely and co-workers suggested a second ATP-binding site in the C-terminus of Hsp90.	Adenosine Triphosphate	62-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
18991631-13	2008	Novobiocin was reported to bind weakly to the newly discovered Hsp90 C-terminal ATP binding site ( approximately 700 M in SkBr3 cells) and induce degradation of Hsp90 client proteins.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18991631-13	2008	Novobiocin was reported to bind weakly to the newly discovered Hsp90 C-terminal ATP binding site ( approximately 700 M in SkBr3 cells) and induce degradation of Hsp90 client proteins.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
18991631-13	2008	Novobiocin was reported to bind weakly to the newly discovered Hsp90 C-terminal ATP binding site ( approximately 700 M in SkBr3 cells) and induce degradation of Hsp90 client proteins.	Adenosine Triphosphate	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
18756022-9	2008	Interstingly, our data identified four tyrosine residues that can be modified by nitration that are located in the region of eNOS responsible for the binding to heat shock protein 90 (Hsp90), which is responsible for ensuring efficient coupling of eNOS.	Tyrosine	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-182
18756022-9	2008	Interstingly, our data identified four tyrosine residues that can be modified by nitration that are located in the region of eNOS responsible for the binding to heat shock protein 90 (Hsp90), which is responsible for ensuring efficient coupling of eNOS.	Tyrosine	39-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
23480142-0	2008	Discovery and development of purine-scaffold Hsp90 inhibitors.	purine	29-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
23480142-2	2008	The initially identified natural-product inhibitors of Hsp90, such as geldanamycin, played a major role in elucidating its biological function and in determining its clinical relevance.	geldanamycin	70-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
23480142-3	2008	Upcoming synthetic inhibitors, such as the purine-scaffold class, furthered our understanding on Hsp90 in cancer and neurodegenerative diseases and delivered what are promised to be clinical candidates with favorable pharmacologic profiles.	purine	43-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
23480142-4	2008	This review intends to inform the reader on efforts ranging from the discovery of purine-scaffold Hsp90 inhibitors to their clinical translation as well as on their use as chemical tools to dissect the roles of Hsp90 in pathogenic systems.	purine	82-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
19066127-3	2008	17-N-Allylamino-17-demethoxygeldanamycin (17-AAG) is one such agent that has been shown to bind to Hsp90 and thus reduce the stability and activity of many key growth regulatory molecules and pathways.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
17617451-0	2008	HSP90 inhibitor 17AAG causes apoptosis in ATRA-resistant acute promyelocytic leukemia cells.	tanespimycin	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
19568319-2	2008	Utilizing our chimera approach, which encompasses the quinone moiety of geldanamycin and the resorcinol moiety of radicicol, molecules have been produced that are highly effective inhibitors of the Hsp90 protein folding machinery.	quinone	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
19568319-2	2008	Utilizing our chimera approach, which encompasses the quinone moiety of geldanamycin and the resorcinol moiety of radicicol, molecules have been produced that are highly effective inhibitors of the Hsp90 protein folding machinery.	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
19568319-2	2008	Utilizing our chimera approach, which encompasses the quinone moiety of geldanamycin and the resorcinol moiety of radicicol, molecules have been produced that are highly effective inhibitors of the Hsp90 protein folding machinery.	resorcinol	93-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
19568319-2	2008	Utilizing our chimera approach, which encompasses the quinone moiety of geldanamycin and the resorcinol moiety of radicicol, molecules have been produced that are highly effective inhibitors of the Hsp90 protein folding machinery.	monorden	114-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
19568319-4	2008	To circumvent this problem, a highly diversifiable alpha-bromo-alpha,beta-unsaturated ester has been prepared, which allows for the introduction of various functionalities that enable elucidation of structure-activity relationships between chimeric compounds and Hsp90.	alpha-bromo-alpha,beta-unsaturated ester	51-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	263-268
18673171-1	2008	Heat shock protein (Hsp90) inhibitors are an increasingly interesting and important class of compounds where the first in class, natural product derived inhibitors such as 17-allylaminogeldanamycin (17-AAG), are entering late stage clinical development.	tanespimycin	199-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17935235-6	2007	Geldanamycin, an Hsp90 inhibitor, reduces the steady-state abundance of all polyalanine-expanded proteins in transfected cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
18302885-14	2008	CONCLUSION: Levels of HSP90 in peripheral blood lymphocytes and the degree of DNA damage increase with the rise of exposure polycyclic aromatic hydrocarbons (PAHs) dose.	Polycyclic Aromatic Hydrocarbons	124-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
18302885-14	2008	CONCLUSION: Levels of HSP90 in peripheral blood lymphocytes and the degree of DNA damage increase with the rise of exposure polycyclic aromatic hydrocarbons (PAHs) dose.	Polycyclic Aromatic Hydrocarbons	158-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
17935235-6	2007	Geldanamycin, an Hsp90 inhibitor, reduces the steady-state abundance of all polyalanine-expanded proteins in transfected cells.	polyalanine	76-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
18089825-7	2007	We have also discovered synergistic interactions between Cdc37 inactivation and the HSP90-inhibitory anticancer drug 17-(allylamino)-17-demethoxygeldanamycin (17AAG).	tanespimycin	117-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
18089825-7	2007	We have also discovered synergistic interactions between Cdc37 inactivation and the HSP90-inhibitory anticancer drug 17-(allylamino)-17-demethoxygeldanamycin (17AAG).	tanespimycin	159-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
17827253-0	2007	Nitric oxide and superoxide generation from endothelial NOS: modulation by HSP90.	Nitric Oxide	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
18001136-4	2007	Importantly, the Hsp90 inhibitor geldanamycin impaired the retrograde transport of MR, suggesting that the Hsp90.IMM.dynein molecular machinery is required for MR movement.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
18001136-4	2007	Importantly, the Hsp90 inhibitor geldanamycin impaired the retrograde transport of MR, suggesting that the Hsp90.IMM.dynein molecular machinery is required for MR movement.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
17827253-0	2007	Nitric oxide and superoxide generation from endothelial NOS: modulation by HSP90.	Superoxides	17-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
17827253-6	2007	We found that overexpression of HSP90 significantly increased the shear-stimulated association of HSP90 with eNOS and led to significant increases in NO production and reduced NOS-dependent superoxide generation.	Superoxides	190-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
17827253-6	2007	We found that overexpression of HSP90 significantly increased the shear-stimulated association of HSP90 with eNOS and led to significant increases in NO production and reduced NOS-dependent superoxide generation.	Superoxides	190-200	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
17827253-7	2007	Conversely, the exposure of PAECs isolated from fetal lambs to the HSP90 inhibitor radicicol led to significant decreases in eNOS-HSP90 interactions, decreased shear-stimulated NO generation, and increased NOS-dependent superoxide production indicative of eNOS uncoupling.	monorden	83-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
17827253-7	2007	Conversely, the exposure of PAECs isolated from fetal lambs to the HSP90 inhibitor radicicol led to significant decreases in eNOS-HSP90 interactions, decreased shear-stimulated NO generation, and increased NOS-dependent superoxide production indicative of eNOS uncoupling.	monorden	83-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
17827253-7	2007	Conversely, the exposure of PAECs isolated from fetal lambs to the HSP90 inhibitor radicicol led to significant decreases in eNOS-HSP90 interactions, decreased shear-stimulated NO generation, and increased NOS-dependent superoxide production indicative of eNOS uncoupling.	Superoxides	220-230	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
17827253-9	2007	Our data indicate that HSP90-eNOS interactions were decreased in shunt lambs and that this was associated with decreased NO generation and an increase in eNOS-dependent generation of superoxide.	Superoxides	183-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
17827253-10	2007	Together, our data support a significant role for HSP90 in promoting NO generation and inhibiting superoxide generation by eNOS and indicate that the disruption of this interaction may be involved in the endothelial dysfunction associated with pulmonary hypertension.	Superoxides	98-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
18156216-9	2007	Studies with Os RAR1-RNAi and treatment with geldanamycin, an HSP90-specific inhibitor, showed that RAR1 and HSP90 are essential for the Rac1-mediated enhancement of pathogen-associated molecular pattern-triggered immune responses in rice cell cultures.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
17949452-3	2007	The semisynthetic geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17-AAG) inhibits heat shock protein 90 (Hsp90) binding to client proteins, thereby leading to their degradation.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-120
17949452-3	2007	The semisynthetic geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17-AAG) inhibits heat shock protein 90 (Hsp90) binding to client proteins, thereby leading to their degradation.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
17949452-3	2007	The semisynthetic geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17-AAG) inhibits heat shock protein 90 (Hsp90) binding to client proteins, thereby leading to their degradation.	tanespimycin	42-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-120
17949452-3	2007	The semisynthetic geldanamycin derivative 17-allylamino-17-demethoxygeldanamycin (17-AAG) inhibits heat shock protein 90 (Hsp90) binding to client proteins, thereby leading to their degradation.	tanespimycin	42-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
18048823-1	2007	PURPOSE: This phase I study examined whether a heat shock protein (Hsp) 90 inhibitor tanespimycin (17-AAG; KOS-953) could be administered safely in combination with trastuzumab at a dose that inhibits Hsp90 function in vivo in lymphocytes.	tanespimycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-74
18048823-1	2007	PURPOSE: This phase I study examined whether a heat shock protein (Hsp) 90 inhibitor tanespimycin (17-AAG; KOS-953) could be administered safely in combination with trastuzumab at a dose that inhibits Hsp90 function in vivo in lymphocytes.	tanespimycin	85-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	201-206
18156216-9	2007	Studies with Os RAR1-RNAi and treatment with geldanamycin, an HSP90-specific inhibitor, showed that RAR1 and HSP90 are essential for the Rac1-mediated enhancement of pathogen-associated molecular pattern-triggered immune responses in rice cell cultures.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	geldanamycin	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17979263-2	2007	Investigation of novobiocin analogues lacking the noviose moiety as novel inhibitors of hsp90 was carried out.	Novobiocin	17-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
17979263-3	2007	A novel series of 3-aminocoumarin analogues has been produced and screened in cell proliferation, and the molecular signature of hsp90 inhibition was assessed by depletion of estrogen receptor, HER2, Raf-1, and cdk4 in human breast cancer cells.	3-Aminocoumarin	18-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
17979263-4	2007	This structure-activity relationship study highlights the crucial role of the C-4 and/or C-7 positions of coumarin which appeared to be essential for degradation of hsp90 client proteins.	coumarin	106-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
17525741-0	2007	Inhibition of Hsp90 function by ansamycins causes downregulation of cdc2 and cdc25c and G(2)/M arrest in glioblastoma cell lines.	Lactams, Macrocyclic	32-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17525741-1	2007	Ansamycins exert their effects by binding heat shock protein 90 (Hsp90) and targeting important signalling molecules for degradation via the proteasome pathway.	Lactams, Macrocyclic	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
17525741-1	2007	Ansamycins exert their effects by binding heat shock protein 90 (Hsp90) and targeting important signalling molecules for degradation via the proteasome pathway.	Lactams, Macrocyclic	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
17893518-0	2007	HSP90 antagonist, geldanamycin, inhibits proliferation, induces apoptosis and blocks migration of rhabdomyosarcoma cells in vitro and seeding into bone marrow in vivo.	geldanamycin	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17893518-11	2007	Our data show that the HSP90 inhibitor GA has the potential to become a new drug in RMS treatment.	geldanamycin	39-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Fluoxetine	238-248	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Fluoxetine	238-248	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	geldanamycin	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Arsenic Trioxide	129-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Arsenic Trioxide	129-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Pentamidine	173-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Pentamidine	173-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Probucol	191-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Probucol	191-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Cholesterol	203-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17956279-6	2007	Important examples are antineoplastic Hsp90 (heat-shock protein 90) inhibitors such as (i) geldanamycin, (ii) the leukaemia drug arsenic trioxide, (iii) the antiprotozoical pentamidine, (iv) probucol, a cholesterol-lowering drug, and (v) fluoxetine, a widely used antidepressant.	Cholesterol	203-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
17643429-3	2007	We analyzed an immortalized cell line Ba/F3 for sensitivity to the Hsp90 inhibitor geldanamycin in the absence and presence of the oncogenic tyrosine fusion kinase NPM-ALK expressed from a retroviral vector.	geldanamycin	83-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
17979943-4	2007	A comparison with published gene expression studies identified FK binding protein 5 (FKBP5) (also known as FKBP51), a key regulatory component of the Hsp90-steroid-receptor complex to be increased at the mRNA and protein level postdexamethasone exposure.	postdexamethasone	227-244	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
17907782-6	2007	The formation of cross-linked Hsp90 coincided with a rapid loss of carbonyl adducts within cells that had been subjected to a brief "pulse" exposure to a subtoxic concentration of acrolein, suggesting Michael adducts are short-lived within cells due in part to consumption during reactions with protein nucleophiles.	Acrolein	180-188	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
17907782-9	2007	As previously shown for hydralazine, mass spectrometry studies using a model peptide indicated that bisulfite traps carbonyl groups possessed by Michael addition adducts, and such adduct-trapping reactivity appeared to contribute to the blockade of Hsp90 cross-linking in acrolein-preloaded cells.	hydrogen sulfite	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	249-254
17907782-9	2007	As previously shown for hydralazine, mass spectrometry studies using a model peptide indicated that bisulfite traps carbonyl groups possessed by Michael addition adducts, and such adduct-trapping reactivity appeared to contribute to the blockade of Hsp90 cross-linking in acrolein-preloaded cells.	Acrolein	272-280	heat shock protein 90 alpha family class A member 1	Homo sapiens	249-254
17698952-3	2007	The CB2/Hsp90 interaction was confirmed in human embryonic kidney 293 cells expressing transfected CB2 and in differentiated HL-60 cells expressing endogenous CB2, by coimmunoprecipitation and Western blot experiments, as well as by treatment with geldanamycin (GA), a specific Hsp90 inhibitor.	geldanamycin	248-260	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
17870069-0	2007	Geldanamycin, a HSP90 inhibitor, attenuates the hypoxia-induced vascular endothelial growth factor expression in retinal pigment epithelium cells in vitro.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
17870069-2	2007	The purpose of this study is to investigate the role of retinal pigment epithelial (RPE) cells in the regulation of subretinal neovascularization under hypoxia and the possible function of a heat shock protein 90 (HSP90) inhibitor, geldanamycin (GA), in the regulation of VEGF expression.	geldanamycin	232-244	heat shock protein 90 alpha family class A member 1	Homo sapiens	214-219
17870069-2	2007	The purpose of this study is to investigate the role of retinal pigment epithelial (RPE) cells in the regulation of subretinal neovascularization under hypoxia and the possible function of a heat shock protein 90 (HSP90) inhibitor, geldanamycin (GA), in the regulation of VEGF expression.	geldanamycin	246-248	heat shock protein 90 alpha family class A member 1	Homo sapiens	214-219
18025273-3	2007	Moreover, in vitro studies suggested that blocking Hsp90 could overcome p53-mediated resistance of cancer cells to oxaliplatin.	Oxaliplatin	115-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
18025273-4	2007	We therefore hypothesized that blocking oncogenic signaling with a Hsp90 inhibitor would impair metastatic behavior of colon cancer cells and also improve the efficacy of oxaliplatin in vivo.	Oxaliplatin	171-182	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
18025273-5	2007	Human colon cancer cells (HCT116, HT29, and SW620) and the Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) were used for experiments.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	75-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
18025273-13	2007	Hence, targeting Hsp90 could prove valuable for treatment of advanced colorectal cancer by effectively inhibiting colon cancer growth and hepatic metastasis and improving the efficacy of oxaliplatin.	Oxaliplatin	187-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
17698952-3	2007	The CB2/Hsp90 interaction was confirmed in human embryonic kidney 293 cells expressing transfected CB2 and in differentiated HL-60 cells expressing endogenous CB2, by coimmunoprecipitation and Western blot experiments, as well as by treatment with geldanamycin (GA), a specific Hsp90 inhibitor.	geldanamycin	262-264	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
17698952-4	2007	Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration.	glyceryl 2-arachidonate	142-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
17698952-4	2007	Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration.	glyceryl 2-arachidonate	142-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
17698952-4	2007	Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration.	glyceryl 2-arachidonate	142-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
17698952-4	2007	Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration.	glyceryl 2-arachidonate	211-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
17698952-4	2007	Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration.	glyceryl 2-arachidonate	211-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
17698952-4	2007	Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration.	glyceryl 2-arachidonate	211-215	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
17698952-7	2007	These data demonstrate that 2-AG-induced activation of Rac1 is essential for 2-AG-induced cell migration, and the CB2/Hsp90 interaction is needed for 2-AG-induced activation of Rac1.	glyceryl 2-arachidonate	28-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	geldanamycin	34-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	geldanamycin	34-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	geldanamycin	34-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	Adenosine Triphosphate	51-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	Adenosine Diphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	Adenosine Diphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-2	2007	The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes.	Adenosine Diphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17978573-3	2007	Here we show that GA reduces the level of endogenous c-Jun in human embryonic kidney 293 (HEK293) cells in a time and dose dependent manner, and that this decrease can be reversed by transfection of HSP90 plasmids.	geldanamycin	18-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	199-204
17978573-5	2007	We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxy-carbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	155-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17978573-5	2007	We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxy-carbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	155-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
17978573-5	2007	We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxy-carbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	155-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	226-231
17764690-3	2007	Hydrogen-exchange mass spectrometry was used to study the structural and conformational changes undergone by full-length human Hsp90beta in solution upon binding of the kinase-specific co-chaperone Cdc37 and two Hsp90 ATPase inhibitors: Radicicol and the first-generation anticancer drug DMAG.	Hydrogen	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
17764690-3	2007	Hydrogen-exchange mass spectrometry was used to study the structural and conformational changes undergone by full-length human Hsp90beta in solution upon binding of the kinase-specific co-chaperone Cdc37 and two Hsp90 ATPase inhibitors: Radicicol and the first-generation anticancer drug DMAG.	monorden	237-246	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
17764690-3	2007	Hydrogen-exchange mass spectrometry was used to study the structural and conformational changes undergone by full-length human Hsp90beta in solution upon binding of the kinase-specific co-chaperone Cdc37 and two Hsp90 ATPase inhibitors: Radicicol and the first-generation anticancer drug DMAG.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	288-292	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
17764690-4	2007	Changes in hydrogen exchange pattern in the complexes in regions of Hsp90 remote to the ligand-binding site were observed indicating long-range effects.	Hydrogen	11-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
17909058-3	2007	HSP90alpha was found to associate with FLIP(S) in resting cells in a manner dependent on the ATP-binding NH2-terminal domain of HSP90alpha.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-10
17513464-5	2007	We review the various classes of HSP90 inhibitor that have been developed, including the natural products geldanamycin and radicicol and also the purine scaffold and pyrazole/isoxazole class of synthetic small molecule inhibitors.	geldanamycin	106-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17513464-5	2007	We review the various classes of HSP90 inhibitor that have been developed, including the natural products geldanamycin and radicicol and also the purine scaffold and pyrazole/isoxazole class of synthetic small molecule inhibitors.	monorden	123-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17513464-5	2007	We review the various classes of HSP90 inhibitor that have been developed, including the natural products geldanamycin and radicicol and also the purine scaffold and pyrazole/isoxazole class of synthetic small molecule inhibitors.	purine	146-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17513464-5	2007	We review the various classes of HSP90 inhibitor that have been developed, including the natural products geldanamycin and radicicol and also the purine scaffold and pyrazole/isoxazole class of synthetic small molecule inhibitors.	pyrazole	166-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17513464-5	2007	We review the various classes of HSP90 inhibitor that have been developed, including the natural products geldanamycin and radicicol and also the purine scaffold and pyrazole/isoxazole class of synthetic small molecule inhibitors.	Isoxazoles	175-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17513464-6	2007	A first-in-class HSP90 drug, the geldanamycin analog 17-AAG, has provided proof of concept for HSP90 inhibition in patients at well tolerated doses and therapeutic activity has been seen.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
17513464-6	2007	A first-in-class HSP90 drug, the geldanamycin analog 17-AAG, has provided proof of concept for HSP90 inhibition in patients at well tolerated doses and therapeutic activity has been seen.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
17513464-6	2007	A first-in-class HSP90 drug, the geldanamycin analog 17-AAG, has provided proof of concept for HSP90 inhibition in patients at well tolerated doses and therapeutic activity has been seen.	tanespimycin	53-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
17513464-6	2007	A first-in-class HSP90 drug, the geldanamycin analog 17-AAG, has provided proof of concept for HSP90 inhibition in patients at well tolerated doses and therapeutic activity has been seen.	tanespimycin	53-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
17645779-3	2007	Hsp90 inhibitors, by interacting specifically with a single molecular target, cause the destabilization and eventual degradation of Hsp90 client proteins, and the first-in-class Hsp90 inhibitor, 17-allylamino-17 demethoxygeldanamycin (17AAG), is currently in phase II clinical trials.	tanespimycin	195-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17645779-3	2007	Hsp90 inhibitors, by interacting specifically with a single molecular target, cause the destabilization and eventual degradation of Hsp90 client proteins, and the first-in-class Hsp90 inhibitor, 17-allylamino-17 demethoxygeldanamycin (17AAG), is currently in phase II clinical trials.	tanespimycin	195-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
17645779-3	2007	Hsp90 inhibitors, by interacting specifically with a single molecular target, cause the destabilization and eventual degradation of Hsp90 client proteins, and the first-in-class Hsp90 inhibitor, 17-allylamino-17 demethoxygeldanamycin (17AAG), is currently in phase II clinical trials.	tanespimycin	195-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
17645779-3	2007	Hsp90 inhibitors, by interacting specifically with a single molecular target, cause the destabilization and eventual degradation of Hsp90 client proteins, and the first-in-class Hsp90 inhibitor, 17-allylamino-17 demethoxygeldanamycin (17AAG), is currently in phase II clinical trials.	tanespimycin	235-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17909058-3	2007	HSP90alpha was found to associate with FLIP(S) in resting cells in a manner dependent on the ATP-binding NH2-terminal domain of HSP90alpha.	Adenosine Triphosphate	93-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	128-138
17942784-3	2007	In this study, the authors describe the development and optimization in a 384-well format of a novel assay for the identification of Hsp90 inhibitors using fluorescence polarization, which measures competitive binding of red-shifted fluorescently labeled geldanamycin (GM-cy3B) to Hsp90 found in the NCI-N417 small-cell lung carcinoma cells.	geldanamycin	255-267	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
23484535-2	2007	Hsp90 is a conformationally flexible protein that associates with a distinct set of cochaperones depending on ATP or ADP occupancy of an N-terminal binding pocket.	Adenosine Triphosphate	110-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23484535-2	2007	Hsp90 is a conformationally flexible protein that associates with a distinct set of cochaperones depending on ATP or ADP occupancy of an N-terminal binding pocket.	Adenosine Diphosphate	117-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
23484535-3	2007	Nucleotide exchange and ATP hydrolysis by Hsp90 itself, with the assistance of cochaperones, drive the Hsp90 chaperone machine to bind, chaperone and release client proteins.	Adenosine Triphosphate	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
23484535-3	2007	Nucleotide exchange and ATP hydrolysis by Hsp90 itself, with the assistance of cochaperones, drive the Hsp90 chaperone machine to bind, chaperone and release client proteins.	Adenosine Triphosphate	24-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
23484535-5	2007	Although ATP binding and hydrolysis have been convincingly implicated in regulating the Hsp90 cycle, growing evidence suggests that various post-translational modifications of Hsp90, including phosphorylation, acetylation and other modifications, provide an additional overlapping or parallel level of regulation.	Adenosine Triphosphate	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
23484535-5	2007	Although ATP binding and hydrolysis have been convincingly implicated in regulating the Hsp90 cycle, growing evidence suggests that various post-translational modifications of Hsp90, including phosphorylation, acetylation and other modifications, provide an additional overlapping or parallel level of regulation.	Adenosine Triphosphate	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
17942784-3	2007	In this study, the authors describe the development and optimization in a 384-well format of a novel assay for the identification of Hsp90 inhibitors using fluorescence polarization, which measures competitive binding of red-shifted fluorescently labeled geldanamycin (GM-cy3B) to Hsp90 found in the NCI-N417 small-cell lung carcinoma cells.	geldanamycin	255-267	heat shock protein 90 alpha family class A member 1	Homo sapiens	281-286
17768706-3	2007	Because geldanamycin (GA) and its derivative, 17-allylamino-17-demethoxygeldanamycin (17-AAG), exhibit anti-tumour activity by degrading HSP90 client proteins, including Akt, we investigated the effect of GA and 17-AAG on the survival of NKTL cell lines.	geldanamycin	8-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
17768706-3	2007	Because geldanamycin (GA) and its derivative, 17-allylamino-17-demethoxygeldanamycin (17-AAG), exhibit anti-tumour activity by degrading HSP90 client proteins, including Akt, we investigated the effect of GA and 17-AAG on the survival of NKTL cell lines.	geldanamycin	22-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
17768706-3	2007	Because geldanamycin (GA) and its derivative, 17-allylamino-17-demethoxygeldanamycin (17-AAG), exhibit anti-tumour activity by degrading HSP90 client proteins, including Akt, we investigated the effect of GA and 17-AAG on the survival of NKTL cell lines.	tanespimycin	46-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
17768706-3	2007	Because geldanamycin (GA) and its derivative, 17-allylamino-17-demethoxygeldanamycin (17-AAG), exhibit anti-tumour activity by degrading HSP90 client proteins, including Akt, we investigated the effect of GA and 17-AAG on the survival of NKTL cell lines.	tanespimycin	86-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
17942784-3	2007	In this study, the authors describe the development and optimization in a 384-well format of a novel assay for the identification of Hsp90 inhibitors using fluorescence polarization, which measures competitive binding of red-shifted fluorescently labeled geldanamycin (GM-cy3B) to Hsp90 found in the NCI-N417 small-cell lung carcinoma cells.	gm-cy3b	269-276	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138
17942784-4	2007	The authors demonstrate that GMcy3B binds with high affinity and specificity to cellular Hsp90.	gmcy3b	29-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
17878410-5	2007	Studies examining the interactions between NOS-3, beta-actin, and Hsp90 could potentially lead to the discovery of effective peptides for the treatment of diseases associated with impaired NOS-3 activity and nitric oxide release, such as systemic and pulmonary hypertension, atherosclerosis, and thrombotic diseases.	Nitric Oxide	208-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
18399173-1	2007	OBJECTIVE: To explore the signal transduction pathway in the differentiation and apoptosis of leukemia cells induced by heat shock protein 90 (HSP90) inhibitor 17-Allyl amide-17-demethoxygeldanamycin (17AAG).	17-allyl amide-17-demethoxygeldanamycin	160-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-141
18399173-1	2007	OBJECTIVE: To explore the signal transduction pathway in the differentiation and apoptosis of leukemia cells induced by heat shock protein 90 (HSP90) inhibitor 17-Allyl amide-17-demethoxygeldanamycin (17AAG).	17-allyl amide-17-demethoxygeldanamycin	160-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
18399173-1	2007	OBJECTIVE: To explore the signal transduction pathway in the differentiation and apoptosis of leukemia cells induced by heat shock protein 90 (HSP90) inhibitor 17-Allyl amide-17-demethoxygeldanamycin (17AAG).	tanespimycin	201-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-141
18399173-1	2007	OBJECTIVE: To explore the signal transduction pathway in the differentiation and apoptosis of leukemia cells induced by heat shock protein 90 (HSP90) inhibitor 17-Allyl amide-17-demethoxygeldanamycin (17AAG).	tanespimycin	201-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148
18399173-8	2007	Immunoprecipitation showed that 1 microM 17AAG treatment for 1 hour caused kit associated HSP90 decrease and HSP70 increase.	tanespimycin	41-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
17651857-0	2007	Intelligent biosynthetic nanobiomaterials for hyperthermic combination chemotherapy and thermal drug targeting of HSP90 inhibitor geldanamycin.	geldanamycin	130-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
17881891-3	2007	Importantly, Hsp90 inhibitors including geldanamycin analogues show anti-tumor effects.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
17662999-0	2007	Mechanistic studies on Hsp90 inhibition by ansamycin derivatives.	Rifabutin	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
17662999-2	2007	The ansamycin family of natural products and their derivatives, such as geldanamycin (GA), are well-known inhibitors of the essential ATPase activity of Hsp90.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
17662999-2	2007	The ansamycin family of natural products and their derivatives, such as geldanamycin (GA), are well-known inhibitors of the essential ATPase activity of Hsp90.	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
17662999-2	2007	The ansamycin family of natural products and their derivatives, such as geldanamycin (GA), are well-known inhibitors of the essential ATPase activity of Hsp90.	geldanamycin	86-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
17662999-3	2007	Despite structural studies on the complexes of ansamycin derivatives with the ATPase domain of Hsp90, certain aspects of their inhibitory mechanism remain unresolved.	Rifabutin	47-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
17662999-4	2007	For example, it is known that GA in solution exists in an extended conformation with a trans amide bond; however, it binds to Hsp90 in a significantly more compact conformation with a cis amide bond.	geldanamycin	30-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
17662999-4	2007	For example, it is known that GA in solution exists in an extended conformation with a trans amide bond; however, it binds to Hsp90 in a significantly more compact conformation with a cis amide bond.	Amides	188-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
17662999-7	2007	We have studied both the equilibrium binding, and the association and dissociation kinetics of GA derivative, 17-DMAG, and the fluorescently labelled analogue BDGA to both wild-type and mutant Hsp90.	geldanamycin	95-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
17662999-10	2007	Experiments with BDGA measured over a wide range of conditions, in the absence and in the presence of reducing agents, confirm recent studies that have suggested that the reduced dihydroquinone form of the drug binds to Hsp90 considerably more tightly than the non-reduced quinone species.	bdga	17-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
17662999-10	2007	Experiments with BDGA measured over a wide range of conditions, in the absence and in the presence of reducing agents, confirm recent studies that have suggested that the reduced dihydroquinone form of the drug binds to Hsp90 considerably more tightly than the non-reduced quinone species.	1,4-dihydroquinone	179-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
17662999-10	2007	Experiments with BDGA measured over a wide range of conditions, in the absence and in the presence of reducing agents, confirm recent studies that have suggested that the reduced dihydroquinone form of the drug binds to Hsp90 considerably more tightly than the non-reduced quinone species.	quinone	186-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
17855662-3	2007	In this report, we show that inhibition of Hsp90 by geldanamycin or its derivative, 17-allylamino-17-desmethoxygeldamycin, leads to activation of the Rho GTPase and a dramatic increase in actin stress fiber formation in human tumor cell lines.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
17681020-0	2007	Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol.	monorden	231-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
17681020-0	2007	Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol.	monorden	231-240	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
17569822-3	2007	Importantly, the imatinib resistance mechanism in these variants also included aberrant acetylation of nonhistone proteins such as p53, Ku70, and Hsp90 that was due to upregulation of histone deacetylases (HDACs) and down-regulation of histone acetyltransferase (HAT).	Imatinib Mesylate	17-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
17569822-6	2007	In contrast, the class II HDAC6 level was significantly decreased, and this was accompanied by an increase of Hsp90 acetylation in the imatinib-resistant variants, which was closely associated with loss of Bcr-Abl.	Imatinib Mesylate	135-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
17569822-7	2007	These results indicate that alteration of the normal balance of HATs and HDACs leads to deregulated acetylation of Hsp90, p53, and Ku70 and thereby leads to imatinib resistance, suggesting the importance of the acetylation status of apoptosis-related nonhistone proteins in Bcr-Abl-independent imatinib resistance.	Imatinib Mesylate	157-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
17569822-7	2007	These results indicate that alteration of the normal balance of HATs and HDACs leads to deregulated acetylation of Hsp90, p53, and Ku70 and thereby leads to imatinib resistance, suggesting the importance of the acetylation status of apoptosis-related nonhistone proteins in Bcr-Abl-independent imatinib resistance.	Imatinib Mesylate	294-302	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
17626164-3	2007	The C-terminus of ErbB2 can be cleaved after various stimuli, and after inhibition of HSP90 with geldanamycin this cleavage is accompanied by proteasome-dependent endocytosis of ErbB2.	geldanamycin	97-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
17876048-6	2007	LBH589 resulted in increased acetylation of Hsp90 and reduced association of Hsp90 with EGFR, Akt, and STAT3.	Panobinostat	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
17876048-6	2007	LBH589 resulted in increased acetylation of Hsp90 and reduced association of Hsp90 with EGFR, Akt, and STAT3.	Panobinostat	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17855662-3	2007	In this report, we show that inhibition of Hsp90 by geldanamycin or its derivative, 17-allylamino-17-desmethoxygeldamycin, leads to activation of the Rho GTPase and a dramatic increase in actin stress fiber formation in human tumor cell lines.	17-allylamino-17-desmethoxygeldamycin	84-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
21122290-6	2007	CONCLUSIONS: The down-regulation of HSP90 and triosephosphate isomerase may be related to the synergistic effects of NS-398 and cisplatin on human lung adenocarcinoma cells.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	117-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
17631526-3	2007	Here, we address whether elaboration of the HSP90 inhibitor monocillin I (MON) by the rhizosphere fungus Paraphaeosphaeria quadriseptata affects plant HSP90 and plant environmental responsiveness.	monocillin I	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
17631526-3	2007	Here, we address whether elaboration of the HSP90 inhibitor monocillin I (MON) by the rhizosphere fungus Paraphaeosphaeria quadriseptata affects plant HSP90 and plant environmental responsiveness.	monocillin I	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
21122290-6	2007	CONCLUSIONS: The down-regulation of HSP90 and triosephosphate isomerase may be related to the synergistic effects of NS-398 and cisplatin on human lung adenocarcinoma cells.	Cisplatin	128-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
17699868-1	2007	PURPOSE: The molecular chaperone heat shock protein (hsp)-90 maintains estrogen receptor (ER)-alpha in an active conformation, allowing it to bind 17beta-estradiol (E2) and transactivate genes, including progesterone receptor (PR)-beta and the class IIB histone deacetylase HDAC6.	Estradiol	147-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-60
17699868-2	2007	By inhibiting HDAC6, the hydroxamic acid analogue pan-HDAC inhibitors (HA-HDI; e.g., LAQ824, LBH589, and vorinostat) induce hyperacetylation of the HDAC6 substrates alpha-tubulin and hsp90.	Hydroxamic Acids	25-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
17699868-2	2007	By inhibiting HDAC6, the hydroxamic acid analogue pan-HDAC inhibitors (HA-HDI; e.g., LAQ824, LBH589, and vorinostat) induce hyperacetylation of the HDAC6 substrates alpha-tubulin and hsp90.	LAQ824	85-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
17699868-2	2007	By inhibiting HDAC6, the hydroxamic acid analogue pan-HDAC inhibitors (HA-HDI; e.g., LAQ824, LBH589, and vorinostat) induce hyperacetylation of the HDAC6 substrates alpha-tubulin and hsp90.	Panobinostat	93-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
17699868-2	2007	By inhibiting HDAC6, the hydroxamic acid analogue pan-HDAC inhibitors (HA-HDI; e.g., LAQ824, LBH589, and vorinostat) induce hyperacetylation of the HDAC6 substrates alpha-tubulin and hsp90.	Vorinostat	105-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
17721082-5	2007	For example, bortezomib(a proteasome inhibitor) induces the expression of heat shock protein 90 (hsp90) on the surface of dying human myeloma tumor cells.	Bortezomib	13-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-95
17721082-5	2007	For example, bortezomib(a proteasome inhibitor) induces the expression of heat shock protein 90 (hsp90) on the surface of dying human myeloma tumor cells.	Bortezomib	13-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
17683942-8	2007	Finally, radicicol inhibits kinase activity by binding directly to the ATP-binding pocket of PDK3, similar to Hsp90 and Topo VI from the same ATPase/kinase superfamily.	monorden	9-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
17693610-3	2007	LMB also partly abrogated ER elimination resulting from Hsp90 disruption and 17beta-estradiol (E(2))-induced ER downregulation.	leptomycin B	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
17610208-0	2007	Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells.	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
17475647-6	2007	Pharmacological intercession of Hsp90 activity with ansamycin antibiotics or depletion of BAG3 by small interfering RNA results in inhibition of virus replication.	Rifabutin	52-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
17395781-7	2007	These results provide a rationale for use of an Hsp90 inhibitor as a first-line treatment in CML by inhibiting leukemia stem cells and preventing the emergence of imatinib-resistant clones in patients.	Imatinib Mesylate	163-171	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
17488003-0	2007	Rationally designed high-affinity 2-amino-6-halopurine heat shock protein 90 inhibitors that exhibit potent antitumor activity.	2-amino-6-halopurine	34-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-76
20641498-11	2004	The binding of geldanamycin to Hsp90 inhibits the maturation and stability of HER2 and leads to degradation of the receptor.	geldanamycin	15-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
17488003-5	2007	We now report on a novel series of 2-amino-6-halopurine Hsp90 inhibitors exemplified by 2-amino-6-chloro-9-(4-iodo-3,5-dimethylpyridin-2-ylmethyl)purine (30).	2-amino-6-halopurine	35-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
17488003-5	2007	We now report on a novel series of 2-amino-6-halopurine Hsp90 inhibitors exemplified by 2-amino-6-chloro-9-(4-iodo-3,5-dimethylpyridin-2-ylmethyl)purine (30).	2-amino-6-chloro-9-(4-iodo-3,5-dimethylpyridin-2-ylmethyl)purine	88-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
17488003-7	2007	Moreover, this class of inhibitors shows higher affinity for the activated form of Hsp90 compared to our earlier 8-sulfanylpurine Hsp90 inhibitor series.	8-sulfanylpurine	113-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
17488003-7	2007	Moreover, this class of inhibitors shows higher affinity for the activated form of Hsp90 compared to our earlier 8-sulfanylpurine Hsp90 inhibitor series.	8-sulfanylpurine	113-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
17337508-2	2007	The conformational state of bound Hsp90 determines whether eNOS produces nitric oxide (NO) or superoxide (O(2)(*-)).	Nitric Oxide	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
17337508-2	2007	The conformational state of bound Hsp90 determines whether eNOS produces nitric oxide (NO) or superoxide (O(2)(*-)).	Superoxides	94-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	Acetylcholine	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	Cyclic GMP	103-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17337508-2	2007	The conformational state of bound Hsp90 determines whether eNOS produces nitric oxide (NO) or superoxide (O(2)(*-)).	Superoxides	106-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
17337508-3	2007	We determined the effects of the Hsp90 antagonists geldanamycin (GA) and radicicol (RA) on basal and ACh-stimulated changes in vessel diameter, cGMP production, and Hsp90:eNOS coimmunoprecipitation in piglet resistance level pulmonary arteries (PRA).	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17337508-3	2007	We determined the effects of the Hsp90 antagonists geldanamycin (GA) and radicicol (RA) on basal and ACh-stimulated changes in vessel diameter, cGMP production, and Hsp90:eNOS coimmunoprecipitation in piglet resistance level pulmonary arteries (PRA).	geldanamycin	65-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	geldanamycin	22-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	geldanamycin	22-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	monorden	28-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	monorden	28-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
17337508-6	2007	Hsp90 inhibition with GA or RA reduced ACh-mediated dilation, abolished the ACh-stimulated increase in cGMP, and reduced eNOS:Hsp90 coprecipitation.	Acetylcholine	39-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17804527-9	2007	In vitro experiments showed an upregulation of HSP90 expression in endothelial cells exposed to oxidative stress by treatment with H(2)O(2) and greater release of soluble HSP90 in culture supernatants from H(2)O(2)-treated cells than from untreated cells.	Hydrogen Peroxide	131-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
17804527-9	2007	In vitro experiments showed an upregulation of HSP90 expression in endothelial cells exposed to oxidative stress by treatment with H(2)O(2) and greater release of soluble HSP90 in culture supernatants from H(2)O(2)-treated cells than from untreated cells.	Hydrogen Peroxide	206-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
17442277-8	2007	To further clarify the mechanism of BPQ in regulating HIF-1alpha stability, we found that BPQ inhibited HIF-1alpha protein expression by the increase of the proteasome-dependent degradation, and by the disruption of HIF-1alpha and Hsp90 association.	benzo(a)pyrene-7,8-dione	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	231-236
17343830-1	2007	In a series of colorectal cancer cell lines, both necrosis and apoptosis were induced upon exposure to oxaliplatin, and enhanced by co-administration of the Hsp90 inhibitor 17-AAG.	tanespimycin	173-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
17327415-2	2007	Emerging evidence suggests that Hsp90 inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG), enhance DNA damage-induced cell death, suggesting that Hsp90 may regulate cellular responses to genotoxic stress.	tanespimycin	58-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
17299090-0	2007	Bortezomib enhances dendritic cell (DC)-mediated induction of immunity to human myeloma via exposure of cell surface heat shock protein 90 on dying tumor cells: therapeutic implications.	Bortezomib	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-138
17299090-4	2007	The delivery of activating signal from bortezomib-killed tumor cells to DCs depends on cell-cell contact between DCs and dying tumor cells and is mediated by bortezomib-induced exposure of heat shock protein 90 (hsp90) on the surface of dying cells.	Bortezomib	39-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-210
17299090-4	2007	The delivery of activating signal from bortezomib-killed tumor cells to DCs depends on cell-cell contact between DCs and dying tumor cells and is mediated by bortezomib-induced exposure of heat shock protein 90 (hsp90) on the surface of dying cells.	Bortezomib	39-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
17299090-4	2007	The delivery of activating signal from bortezomib-killed tumor cells to DCs depends on cell-cell contact between DCs and dying tumor cells and is mediated by bortezomib-induced exposure of heat shock protein 90 (hsp90) on the surface of dying cells.	Bortezomib	158-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	189-210
17299090-4	2007	The delivery of activating signal from bortezomib-killed tumor cells to DCs depends on cell-cell contact between DCs and dying tumor cells and is mediated by bortezomib-induced exposure of heat shock protein 90 (hsp90) on the surface of dying cells.	Bortezomib	158-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	212-217
17299090-5	2007	The combination of bortezomib and geldanamycin (an hsp90 inhibitor) leads to greater apoptosis of tumor cells but abrogates their immunogenicity.	Bortezomib	19-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
17299090-5	2007	The combination of bortezomib and geldanamycin (an hsp90 inhibitor) leads to greater apoptosis of tumor cells but abrogates their immunogenicity.	geldanamycin	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
17327415-2	2007	Emerging evidence suggests that Hsp90 inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG), enhance DNA damage-induced cell death, suggesting that Hsp90 may regulate cellular responses to genotoxic stress.	tanespimycin	58-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
17525527-3	2007	Here, we systematically evaluated the inhibitory effects of the prototypical Hsp90 inhibitor geldanamycin (GA) on cellular processes involved in invasion and angiogenesis in T24 bladder cancer cells stimulated with HGF and chemical hypoxia.	geldanamycin	93-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17525527-3	2007	Here, we systematically evaluated the inhibitory effects of the prototypical Hsp90 inhibitor geldanamycin (GA) on cellular processes involved in invasion and angiogenesis in T24 bladder cancer cells stimulated with HGF and chemical hypoxia.	geldanamycin	107-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17525527-10	2007	Thus, GA widely suppresses extrinsic stimuli-induced signaling that contribute to tumor invasion and angiogenesis in this bladder carcinoma model, suggesting the utility of Hsp90 inhibitors in preventing tumor progression and metastasis.	geldanamycin	6-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-178
17219417-0	2007	Potentiation of chemotherapeutics by the Hsp90 antagonist geldanamycin requires a steady serum condition.	geldanamycin	58-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
17563756-3	2007	Functional inhibition of Hsp90 by the anti-tumor agent geldanamycin (GA) efficiently disrupts its interaction with NIK, resulting in NIK degradation and subsequent blockage of p100 processing.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
17563756-3	2007	Functional inhibition of Hsp90 by the anti-tumor agent geldanamycin (GA) efficiently disrupts its interaction with NIK, resulting in NIK degradation and subsequent blockage of p100 processing.	geldanamycin	69-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
17219417-6	2007	In the presence of serum an at least additive effect of combining the Hsp90 inhibitor geldanamycin (GA) with 5-fluorouracil (5FU) was demonstrated.	geldanamycin	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
17219417-6	2007	In the presence of serum an at least additive effect of combining the Hsp90 inhibitor geldanamycin (GA) with 5-fluorouracil (5FU) was demonstrated.	geldanamycin	100-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
17397803-0	2007	FK228 inhibits Hsp90 chaperone function in K562 cells via hyperacetylation of Hsp70.	romidepsin	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
17502619-5	2007	Formation of this ternary complex among NOS-3, globular beta-actin, and Hsp90, in turn, results in an increase in both NOS activity and cyclic guanosine-3",5"-monophosphate, an index of bioactive NO, as well as an increased rate of Hsp90 degradation, thus limiting the duration for which NOS-3 remains activated.	Cyclic GMP	136-172	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
17397803-2	2007	In this study, we compared the effect of a class I HDAC inhibitor FK228 with the pan-HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) on the Hsp90 chaperone function of K562 cells.	Vorinostat	100-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
17397803-2	2007	In this study, we compared the effect of a class I HDAC inhibitor FK228 with the pan-HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) on the Hsp90 chaperone function of K562 cells.	Vorinostat	133-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
17397803-3	2007	We demonstrated that, although having a weaker inhibitory effect on HDAC6, FK228 mediated a similar disruption of Hsp90 chaperone function compared to SAHA.	romidepsin	75-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
17397803-5	2007	These results indicated that FK228 may disrupt the function of Hsp90 indirectly through acetylation of Hsp70 and inhibition of its function.	romidepsin	29-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
17382893-3	2007	We previously showed that inhibition of Hsp90 with Geldanamycin (GA), an inhibitor of Hsp90 increased CYP2E1 mediated toxicity in CYP2E1 over-expressing HepG2 cells (E47 cells) but not in C34-HepG2 cells devoid of CYP2E1 expression.	geldanamycin	65-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
17382893-3	2007	We previously showed that inhibition of Hsp90 with Geldanamycin (GA), an inhibitor of Hsp90 increased CYP2E1 mediated toxicity in CYP2E1 over-expressing HepG2 cells (E47 cells) but not in C34-HepG2 cells devoid of CYP2E1 expression.	geldanamycin	65-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
17382893-0	2007	Geldanamycin, an inhibitor of Hsp90 increases cytochrome P450 2E1 mediated toxicity in HepG2 cells through sustained activation of the p38MAPK pathway.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
17382893-3	2007	We previously showed that inhibition of Hsp90 with Geldanamycin (GA), an inhibitor of Hsp90 increased CYP2E1 mediated toxicity in CYP2E1 over-expressing HepG2 cells (E47 cells) but not in C34-HepG2 cells devoid of CYP2E1 expression.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
17382893-12	2007	In conclusion, the inhibition of Hsp90 with GA increases the toxicity of CYP2E1 in HepG2 cells through an early and sustained activation of the p38 MAPK pathway.	geldanamycin	44-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17382893-3	2007	We previously showed that inhibition of Hsp90 with Geldanamycin (GA), an inhibitor of Hsp90 increased CYP2E1 mediated toxicity in CYP2E1 over-expressing HepG2 cells (E47 cells) but not in C34-HepG2 cells devoid of CYP2E1 expression.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
17328573-1	2007	The DNA gyrase inhibitor, novobiocin, was recently shown to inhibit Hsp90 via a previously unrecognized C-terminal ATP-binding site.	Novobiocin	26-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
17510430-4	2007	A derivative of the antibiotic geldanamycin, 17-allylamino-17-demethoxygeldanamycin (17-AAG), interferes with proper binding of client proteins, such as survivin, to Hsp-90 and leads to misfolding of client proteins, ubiquination, and proteasome degradation.	geldanamycin	31-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-172
17510430-4	2007	A derivative of the antibiotic geldanamycin, 17-allylamino-17-demethoxygeldanamycin (17-AAG), interferes with proper binding of client proteins, such as survivin, to Hsp-90 and leads to misfolding of client proteins, ubiquination, and proteasome degradation.	tanespimycin	45-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-172
17510430-4	2007	A derivative of the antibiotic geldanamycin, 17-allylamino-17-demethoxygeldanamycin (17-AAG), interferes with proper binding of client proteins, such as survivin, to Hsp-90 and leads to misfolding of client proteins, ubiquination, and proteasome degradation.	tanespimycin	85-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-172
17510430-7	2007	Cells treated with the combination of PDT and 17-AAG exhibited decreased expression of the Hsp-90 client proteins phosphorylated survivin, phosphorylated Akt, and Bcl-2.	tanespimycin	46-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-97
17328573-1	2007	The DNA gyrase inhibitor, novobiocin, was recently shown to inhibit Hsp90 via a previously unrecognized C-terminal ATP-binding site.	Adenosine Triphosphate	115-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
17230513-2	2007	The geldanamycin derivative 17-AAG is currently tested in clinical trials and known to inhibit the function of Hsp90 and promote the proteasomal degradation of its misfolded client proteins.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
17324930-2	2007	Death-associated protein kinase (DAPK) has been found associated with HSP90, and inhibition of HSP90 with 17-alkylamino-17-demethoxygeldanamycin reduced expression of DAPK.	17-alkylamino-17-demethoxygeldanamycin	106-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
17339071-7	2007	ZEN mediated induction of oxidative DNA damage (comet assay using the repair enzymes), modulation of gluthatione (GSH), cytotoxicity (growth inhibition) and the oxidative stress responsive gene Hsp 70 and Hsp 90 were investigated with respect to concentration and time dependency.	Zearalenone	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	205-211
17276679-4	2007	We recently identified a small molecule novobiocin analogue, A4 that induces Hsp90 overexpression at low nanomolar concentrations and sought to test its neuroprotective properties.	Novobiocin	40-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17392176-7	2007	Destabilization of HIF-1alpha by the HSP90 inhibitor 17-DMAG caused an increase in tissue necrosis but reduced I/R-stimulated tumor growth by more than 70%.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
17276679-4	2007	We recently identified a small molecule novobiocin analogue, A4 that induces Hsp90 overexpression at low nanomolar concentrations and sought to test its neuroprotective properties.	a4	61-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17409432-0	2007	Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	117-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-106
17409432-1	2007	The promising antitumor activity of 17-allylamino-17-demethoxygeldanamycin (17AAG) results from inhibition of the molecular chaperone heat shock protein 90 (HSP90) and subsequent degradation of multiple oncogenic client proteins.	tanespimycin	36-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-155
17409432-1	2007	The promising antitumor activity of 17-allylamino-17-demethoxygeldanamycin (17AAG) results from inhibition of the molecular chaperone heat shock protein 90 (HSP90) and subsequent degradation of multiple oncogenic client proteins.	tanespimycin	36-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
17409432-1	2007	The promising antitumor activity of 17-allylamino-17-demethoxygeldanamycin (17AAG) results from inhibition of the molecular chaperone heat shock protein 90 (HSP90) and subsequent degradation of multiple oncogenic client proteins.	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-155
17409432-1	2007	The promising antitumor activity of 17-allylamino-17-demethoxygeldanamycin (17AAG) results from inhibition of the molecular chaperone heat shock protein 90 (HSP90) and subsequent degradation of multiple oncogenic client proteins.	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
17409432-3	2007	Comparison of results with an inactive analogue and an alternative HSP90 inhibitor radicicol indicated that increased expression of HSP72, HSC70, HSP27, HSP47, and HSP90beta at the mRNA level were on-target effects of 17AAG.	tanespimycin	218-223	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
17431102-0	2007	Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues.	pyrazole	122-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
17268519-3	2007	Cells with mutant p53 are resistant to nutlin-3, but sensitive to geldanamycin, a pharmacologic inhibitor of heat shock 90 kDa protein (HSP90), indicating that HSP90 inhibition can induce apoptosis in a p53-independent manner.	geldanamycin	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
17268519-3	2007	Cells with mutant p53 are resistant to nutlin-3, but sensitive to geldanamycin, a pharmacologic inhibitor of heat shock 90 kDa protein (HSP90), indicating that HSP90 inhibition can induce apoptosis in a p53-independent manner.	geldanamycin	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
17268519-4	2007	Conversely, cells with defects in the HSP90/nuclear factor-kappa B pathway expressing wild-type p53 are more resistant to geldanamycin, but still sensitive to nutlin-3.	geldanamycin	122-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17221841-7	2007	The hsp90 inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), inhibits basal PSA expression and disrupts the ligand-independent nuclear localization of AR at doses much lower than required to inhibit androgen-induced nuclear import.	tanespimycin	21-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17431102-0	2007	Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues.	isoxazole amide	131-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-39
17431102-1	2007	Although the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) shows clinical promise, potential limitations encourage development of alternative chemotypes.	tanespimycin	53-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-34
17431102-1	2007	Although the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) shows clinical promise, potential limitations encourage development of alternative chemotypes.	tanespimycin	53-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
17431102-1	2007	Although the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) shows clinical promise, potential limitations encourage development of alternative chemotypes.	tanespimycin	93-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-34
17431102-1	2007	Although the heat shock protein 90 (HSP90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) shows clinical promise, potential limitations encourage development of alternative chemotypes.	tanespimycin	93-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
17431102-14	2007	The results indicate the therapeutic potential of the resorcinylic pyrazole/isoxazole amide analogues as HSP90 inhibitors.	pyrazole	67-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
17431102-14	2007	The results indicate the therapeutic potential of the resorcinylic pyrazole/isoxazole amide analogues as HSP90 inhibitors.	isoxazole amide	76-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
17323946-0	2007	Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site: geldanamycin and radicicol.	geldanamycin	104-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
17323946-0	2007	Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site: geldanamycin and radicicol.	monorden	121-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
17323946-4	2007	Geldanamycin and radicicol are structurally different macrocycles determined by X-ray crystallography to bind to a common site on the cellular chaperone heat shock protein 90 (Hsp90).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-174
17323946-4	2007	Geldanamycin and radicicol are structurally different macrocycles determined by X-ray crystallography to bind to a common site on the cellular chaperone heat shock protein 90 (Hsp90).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
17323946-4	2007	Geldanamycin and radicicol are structurally different macrocycles determined by X-ray crystallography to bind to a common site on the cellular chaperone heat shock protein 90 (Hsp90).	monorden	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-174
17323946-4	2007	Geldanamycin and radicicol are structurally different macrocycles determined by X-ray crystallography to bind to a common site on the cellular chaperone heat shock protein 90 (Hsp90).	monorden	17-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
17361105-9	2007	RACK1 activity is required for the mechanism of action for the HSP90 inhibitor 17-allylaminogeldanamycin to induce HIF-1alpha degradation.	tanespimycin	79-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
17363533-2	2007	17-N-Allylamino-17-demethoxygeldanamycin (17-AAG) binds to Hsp90 and alters levels of proteins regulated by Hsp90.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
17363533-2	2007	17-N-Allylamino-17-demethoxygeldanamycin (17-AAG) binds to Hsp90 and alters levels of proteins regulated by Hsp90.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
17363534-1	2007	PURPOSE: To determine the recommended phase 2 dose, dose-limiting toxicities (DLT), pharmacokinetic profile, and pharmacodynamics of the heat shock protein (Hsp) 90 inhibitor, 17-allylaminogeldanamycin (17-AAG).	tanespimycin	176-201	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
17293044-1	2007	Geldanamycin (GA) is a specific inhibitor of the 90 kDs heat shock protein (Hsp90) in the cytoplasm of mammalian cells, which binds directly to Hsp90 and promotes proteolytic degradation of its client proteins.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
17293044-1	2007	Geldanamycin (GA) is a specific inhibitor of the 90 kDs heat shock protein (Hsp90) in the cytoplasm of mammalian cells, which binds directly to Hsp90 and promotes proteolytic degradation of its client proteins.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
17293044-1	2007	Geldanamycin (GA) is a specific inhibitor of the 90 kDs heat shock protein (Hsp90) in the cytoplasm of mammalian cells, which binds directly to Hsp90 and promotes proteolytic degradation of its client proteins.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
17293044-1	2007	Geldanamycin (GA) is a specific inhibitor of the 90 kDs heat shock protein (Hsp90) in the cytoplasm of mammalian cells, which binds directly to Hsp90 and promotes proteolytic degradation of its client proteins.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
17234420-0	2007	HSP90-like artificial chaperone activity based on indole beta-cyclodextrin.	indole	50-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17148781-7	2007	Hsp90 enhances those activities and sustains the increased abundance of TonEBP/OREBP protein in cells exposed to high NaCl.	Sodium Chloride	118-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17234420-0	2007	HSP90-like artificial chaperone activity based on indole beta-cyclodextrin.	betadex	57-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17332351-0	2007	In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors.	diaryl pyrazole resorcinol	59-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-116
17332351-2	2007	Derivatives of the natural product geldanamycin, such as 17-allylamino-17-demethoxy-geldanamycin (17-AAG), were the first HSP90 ATPase inhibitors to enter clinical trial.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
17332351-2	2007	Derivatives of the natural product geldanamycin, such as 17-allylamino-17-demethoxy-geldanamycin (17-AAG), were the first HSP90 ATPase inhibitors to enter clinical trial.	tanespimycin	98-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
17332351-4	2007	Here, we describe the biological properties of the lead compound of a new class of 3,4-diaryl pyrazole resorcinol HSP90 inhibitor (CCT018159), which we identified by high-throughput screening.	3,4-diaryl pyrazole resorcinol	83-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
17332351-4	2007	Here, we describe the biological properties of the lead compound of a new class of 3,4-diaryl pyrazole resorcinol HSP90 inhibitor (CCT018159), which we identified by high-throughput screening.	CCT018159	131-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
17332351-9	2007	The molecular signature of HSP90 inhibition, comprising increased expression of HSP72 protein and depletion of ERBB2, CDK4, C-RAF, and mutant B-RAF, was shown by Western blotting and quantified by time-resolved fluorescent-Cellisa in human cancer cell lines treated with CCT018159.	CCT018159	271-280	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
17332306-2	2007	17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), an inhibitor of the molecular chaperone heat shock protein 90 (Hsp90), inhibits growth and induces apoptosis in FLT3(+) leukemia cells.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-112
17332306-2	2007	17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), an inhibitor of the molecular chaperone heat shock protein 90 (Hsp90), inhibits growth and induces apoptosis in FLT3(+) leukemia cells.	tanespimycin	0-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
17252584-5	2007	Their apoptosis was induced by multivalent mitogen phytohemagglutinin (PHA) in the absence and presence of geldanamycin (GA), the benzoquinone ansamycin antibiotic which binds to Hsp90 (Heat Shock Protein 90) and alters its function.	geldanamycin	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
17252584-5	2007	Their apoptosis was induced by multivalent mitogen phytohemagglutinin (PHA) in the absence and presence of geldanamycin (GA), the benzoquinone ansamycin antibiotic which binds to Hsp90 (Heat Shock Protein 90) and alters its function.	geldanamycin	107-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-207
17252584-5	2007	Their apoptosis was induced by multivalent mitogen phytohemagglutinin (PHA) in the absence and presence of geldanamycin (GA), the benzoquinone ansamycin antibiotic which binds to Hsp90 (Heat Shock Protein 90) and alters its function.	geldanamycin	121-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
17252584-5	2007	Their apoptosis was induced by multivalent mitogen phytohemagglutinin (PHA) in the absence and presence of geldanamycin (GA), the benzoquinone ansamycin antibiotic which binds to Hsp90 (Heat Shock Protein 90) and alters its function.	geldanamycin	121-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-207
17252584-5	2007	Their apoptosis was induced by multivalent mitogen phytohemagglutinin (PHA) in the absence and presence of geldanamycin (GA), the benzoquinone ansamycin antibiotic which binds to Hsp90 (Heat Shock Protein 90) and alters its function.	benzoquinone ansamycin	130-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
17252584-5	2007	Their apoptosis was induced by multivalent mitogen phytohemagglutinin (PHA) in the absence and presence of geldanamycin (GA), the benzoquinone ansamycin antibiotic which binds to Hsp90 (Heat Shock Protein 90) and alters its function.	benzoquinone ansamycin	130-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	186-207
17179467-7	2007	GA eliminated the interaction between Hsp90 with GRK3 and produced a rapid, proteasome-mediated, 70% decrease in GRK3 levels within 24 h. To investigate the influence of Hsp90 on up-regulation of GRK3 expression, we examined the effect of GA on EPI-induced up-regulation.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17179467-7	2007	GA eliminated the interaction between Hsp90 with GRK3 and produced a rapid, proteasome-mediated, 70% decrease in GRK3 levels within 24 h. To investigate the influence of Hsp90 on up-regulation of GRK3 expression, we examined the effect of GA on EPI-induced up-regulation.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	170-175
17179467-6	2007	To investigate the influence of Hsp90 on GRK3 protein stability, we determined the effect of the Hsp90 inhibitor geldanamycin (GA) on cellular GRK3 levels.	geldanamycin	113-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
17131314-0	2007	Dimeric ansamycins--a new class of antitumor Hsp90 modulators with prolonged inhibitory activity.	dimeric ansamycins	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
17185395-5	2007	A GR mutation (F602S) that produces a receptor less dependent on Hsp90 for function as well as treatment with the Hsp90 inhibitor geldanamycin also increased basal GR phosphorylation at a subset of sites.	geldanamycin	130-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
17289794-4	2007	Suppression of HSP90 and treatment with geldanamycin, a specific inhibitor of HSP90, compromised p50- but not NtMEK2(DD)- or Bax-mediated cell death accompanying the reduction of NtMEK2, WIPK and SIPK activation.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
17131314-1	2007	The geldanamycin derivative 17-allyamino-17-demethoxygeldanamycin (17-AAG) is a clinical stage ATP-competitive HSP90 inhibitor that induces degradation of HSP90 client proteins.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
17131314-1	2007	The geldanamycin derivative 17-allyamino-17-demethoxygeldanamycin (17-AAG) is a clinical stage ATP-competitive HSP90 inhibitor that induces degradation of HSP90 client proteins.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
17131314-1	2007	The geldanamycin derivative 17-allyamino-17-demethoxygeldanamycin (17-AAG) is a clinical stage ATP-competitive HSP90 inhibitor that induces degradation of HSP90 client proteins.	17-allyamino-17-demethoxygeldanamycin	28-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
17131314-1	2007	The geldanamycin derivative 17-allyamino-17-demethoxygeldanamycin (17-AAG) is a clinical stage ATP-competitive HSP90 inhibitor that induces degradation of HSP90 client proteins.	17-allyamino-17-demethoxygeldanamycin	28-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
17131314-1	2007	The geldanamycin derivative 17-allyamino-17-demethoxygeldanamycin (17-AAG) is a clinical stage ATP-competitive HSP90 inhibitor that induces degradation of HSP90 client proteins.	Adenosine Triphosphate	95-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
17252137-1	2007	Synthesis and biological evaluation of ring and conformational analogues of the Hsp90 molecular chaperone inhibitor geldanamycin.	geldanamycin	116-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
17131314-1	2007	The geldanamycin derivative 17-allyamino-17-demethoxygeldanamycin (17-AAG) is a clinical stage ATP-competitive HSP90 inhibitor that induces degradation of HSP90 client proteins.	Adenosine Triphosphate	95-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
17131314-3	2007	Since active Hsp90 exists as a dimer, we hypothesized that dimeric compounds containing 2 ansamycin pharmacophores might inhibit Hsp90 function more efficiently than 17-AAG.	Rifabutin	90-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
17131314-3	2007	Since active Hsp90 exists as a dimer, we hypothesized that dimeric compounds containing 2 ansamycin pharmacophores might inhibit Hsp90 function more efficiently than 17-AAG.	Rifabutin	90-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
17012359-0	2007	Nitric oxide preconditioning regulates endothelial monolayer integrity via the heat shock protein 90-soluble guanylate cyclase pathway.	Nitric Oxide	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-100
17252137-3	2007	Thus, 19-membered ansa-lactams, simplified analogues of the naturally occurring Hsp90 molecular chaperone inhibitor geldanamycin, were obtained by concise routes, the key steps being the combination of a ring-closing metathesis to give a 17-membered ring followed by Claisen rearrangement to effect ring expansion.	membered	9-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
17252137-3	2007	Thus, 19-membered ansa-lactams, simplified analogues of the naturally occurring Hsp90 molecular chaperone inhibitor geldanamycin, were obtained by concise routes, the key steps being the combination of a ring-closing metathesis to give a 17-membered ring followed by Claisen rearrangement to effect ring expansion.	ansa-lactams	18-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
17252137-3	2007	Thus, 19-membered ansa-lactams, simplified analogues of the naturally occurring Hsp90 molecular chaperone inhibitor geldanamycin, were obtained by concise routes, the key steps being the combination of a ring-closing metathesis to give a 17-membered ring followed by Claisen rearrangement to effect ring expansion.	geldanamycin	116-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
17252137-5	2007	In ATPase enzyme assays, the synthetic ansa-quinones were weak inhibitors of Hsp90.	ansa-quinones	39-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
17173546-0	2007	BIRB 796 enhances cytotoxicity triggered by bortezomib, heat shock protein (Hsp) 90 inhibitor, and dexamethasone via inhibition of p38 mitogen-activated protein kinase/Hsp27 pathway in multiple myeloma cell lines and inhibits paracrine tumour growth.	doramapimod	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-83
17379955-0	2007	Geldanamycin, a heat-shock protein 90-binding agent, induces thymocyte apoptosis through destabilization of Lck in presence of 12-O-tetradecanoylphorbol 13-acetate.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
17379955-1	2007	Geldanamycin, a heat-shock protein 90 (Hsp90)-binding agent, modulates various cellular activities.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-37
17379955-1	2007	Geldanamycin, a heat-shock protein 90 (Hsp90)-binding agent, modulates various cellular activities.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
17173546-4	2007	The Hsp90 inhibitor 17-allylamino-17-demethoxy-geldanamycin (17-AAG) upregulated protein expression and phosphorylation of Hsp27; conversely, BIRB 796 inhibited this phosphorylation and enhanced 17-AAG-induced cytotoxicity.	doramapimod	142-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17244529-6	2007	HIF-1alpha degradation induced by the HSP90 inhibitor 17-allylaminogeldanamycin is abolished by RACK1 loss of function.	tanespimycin	54-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
17211467-6	2007	Similar molecular alterations were induced by docetaxel plus trastuzumab combination, except for that there was a transient and complete disappearance of AR and HSP90 proteins 24 h after treatment.	Docetaxel	46-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
17223712-6	2007	To understand the functional meaning of the disruption of the Src-cdc37-HSP90 complex by 17 nM geldanamycin at the cellular level, we investigated its effect on TCDD-induced anti-apoptotic action.	geldanamycin	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
17223712-0	2007	Rapid activation of c-Src kinase by dioxin is mediated by the Cdc37-HSP90 complex as part of Ah receptor signaling in MCF10A cells.	Dioxins	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
17003370-3	2007	The siRNA-mediated knockdown of Hsp90 or treatment with the novel Hsp90 inhibitor 17-DMAG attenuated the levels of STAT3 and phospho-ERK and decreased the viability of MM cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	82-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
17223712-4	2007	By dissociating the cytosolic Src-cdc37-HSP90 complex with 17 nM geldanamycin, an optimum concentration for affecting this cytosolic cdc37 complex, but not the cytosolic Ah receptor complex, we could show that the action of TCDD in activating c-Src and cdc37 was abolished, but not its action on CYP1A1.	geldanamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
17223712-4	2007	By dissociating the cytosolic Src-cdc37-HSP90 complex with 17 nM geldanamycin, an optimum concentration for affecting this cytosolic cdc37 complex, but not the cytosolic Ah receptor complex, we could show that the action of TCDD in activating c-Src and cdc37 was abolished, but not its action on CYP1A1.	Polychlorinated Dibenzodioxins	224-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
17279252-1	2007	While resorcylic acid lactones (RALs) have been known for a long time, the more recent discoveries that radicicol is a potent and selective HSP90 inhibitor while other members such as hypothemycin, LL-Z1640-2 and LL-783,277 are potent kinase inhibitors have stimulated a renewed interest in this family of natural products.	monorden	104-113	heat shock protein 90 alpha family class A member 1	Homo sapiens	140-145
17079230-2	2007	Targeting HSP90 with ansamycin antibiotics disrupts the normal processing of clients of the HSP90 complex.	Rifabutin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
17079230-2	2007	Targeting HSP90 with ansamycin antibiotics disrupts the normal processing of clients of the HSP90 complex.	Rifabutin	21-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	92-97
17079230-5	2007	Treatment of cancer cell lines expressing the PDGFRalpha with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) promotes degradation of the receptor.	tanespimycin	82-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
16799637-7	2007	DEP and the HSP90 antagonist 17-allylamino-geldanamycin (17-AAG) both triggered RUNX1-ETO degradation, but without any additive or cooperative effects.	tanespimycin	29-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
17192106-2	2007	Herbimycin A and other members of the benzoquinoid ansamycin class of natural products are known to inhibit Hsp90 activity.	herbimycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
16799637-7	2007	DEP and the HSP90 antagonist 17-allylamino-geldanamycin (17-AAG) both triggered RUNX1-ETO degradation, but without any additive or cooperative effects.	tanespimycin	57-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
17192106-2	2007	Herbimycin A and other members of the benzoquinoid ansamycin class of natural products are known to inhibit Hsp90 activity.	benzoquinoid ansamycin	38-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
16774932-5	2007	We also found that IKK-gamma strongly associates with heat shock protein 90 (Hsp90) in HCT-116 cells, and that this interaction was dramatically reduced after exposure to PMA.	Tetradecanoylphorbol Acetate	171-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
16774932-5	2007	We also found that IKK-gamma strongly associates with heat shock protein 90 (Hsp90) in HCT-116 cells, and that this interaction was dramatically reduced after exposure to PMA.	Tetradecanoylphorbol Acetate	171-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
16868182-2	2007	Because the 90-kDa heat shock protein (Hsp90) plays an important role in the LPS mediation of macrophage activation, using Hsp90 inhibitor geldanamycin A (GA), we analyzed the mechanism of Hsp90 upon LPS-transduced signaling in the regulation of IL-1 expression and determined the function of Hsp90 regarding the viability of human primary macrophages and murine macrophages cell line.	geldanamycin a	139-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
18229454-4	2007	When the 2 clients were reconstituted under identical conditions, each client folding was dose dependent for Hsp90 protein levels and was inhibited by geldanamycin.	geldanamycin	151-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
17266581-8	2007	In this review, we summarize the effects of the Hsp90 inhibitors geldanamycin and its derivatives with other anti-cancer drugs on killing cancer cells.	geldanamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
18220746-8	2007	17-AAG was the leader inhibitor to enter and successfully complete phase I clinical trials, thus demonstrating that Hsp90 constitutes a valid drug target for cancer therapy.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
16868182-5	2007	In analyzing the function of Hsp90 regarding the cytotoxicity/viability of macrophages, we found that the combination of LPS and GA increases apoptosis, as evidenced by the increased caspase-3 activity and the proportion of nuclear/chromatin condensation.	Gallium	129-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
16868182-8	2007	Furthermore, we established the mechanism of GA interference with Hsp90 function for LPS-stimulated macrophages, resulting in increased ROS production and caspase-3 activation, and consequently leading to synergistic enhancement of macrophage apoptosis.	Gallium	45-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
16868182-8	2007	Furthermore, we established the mechanism of GA interference with Hsp90 function for LPS-stimulated macrophages, resulting in increased ROS production and caspase-3 activation, and consequently leading to synergistic enhancement of macrophage apoptosis.	Reactive Oxygen Species	136-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
17804463-7	2007	Hsp90 inhibition in intact cells by geldanamycin analogs blocked hepadnavirus replication, however not completely and only at severely cytotoxic inhibitor concentrations.	geldanamycin	36-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17319785-0	2007	Hsp90 inhibitor geldanamycin increases the sensitivity of resistant ovarian adenocarcinoma cell line A2780cis to cisplatin.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17319785-0	2007	Hsp90 inhibitor geldanamycin increases the sensitivity of resistant ovarian adenocarcinoma cell line A2780cis to cisplatin.	Cisplatin	113-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
17319785-3	2007	We evaluated the effects of Hsp90 inhibitor geldanamycin (GEL) alone and in combination with cisplatin in cisplatin resistant ovarian adenocarcinoma cell line.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
17596719-4	2007	Geldanamycin, a natural substance that modulates Hsp90 function, was previously shown to induce a heat-shock response and to reduce polyQ aggregation in mammalian cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
17083915-0	2006	Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	104-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
18314631-7	2007	SiRNA-mediated knockdown of HSP90 or treatment with the novel HSP90 inhibitor 17-DMAG attenuated the levels of STAT3 and phospho-ERK and decreased the viability of MM cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	78-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
17181154-2	2006	Here we present a combined structure- and dynamics-based computational design strategy, taking the flexibility of the receptor and of a lead peptidic antagonist into account explicitly, to identify the nonpeptidic small molecule 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) as a structurally novel inhibitor of Hsp90.	acadesine	229-283	heat shock protein 90 alpha family class A member 1	Homo sapiens	329-334
17181154-2	2006	Here we present a combined structure- and dynamics-based computational design strategy, taking the flexibility of the receptor and of a lead peptidic antagonist into account explicitly, to identify the nonpeptidic small molecule 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) as a structurally novel inhibitor of Hsp90.	acadesine	285-290	heat shock protein 90 alpha family class A member 1	Homo sapiens	329-334
17083915-1	2006	In order to investigate the mechanism of radio-sensitization by an Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG), we studied repair of DNA double strand breaks (DSBs) in irradiated human cells pre-treated with 17-AAG.	tanespimycin	83-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
17054904-3	2006	Inhibition of Hsp90 function by geldanamycin (GA) induces rapid degradation of Fu through a ubiquitin-proteasome pathway.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17054904-3	2006	Inhibition of Hsp90 function by geldanamycin (GA) induces rapid degradation of Fu through a ubiquitin-proteasome pathway.	geldanamycin	46-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17132020-0	2006	Novobiocin: redesigning a DNA gyrase inhibitor for selective inhibition of hsp90.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
17132020-2	2006	Recent studies have shown that novobiocin binds to a previously unrecognized ATP-binding site at the C-terminus of Hsp90 and induces degradation of Hsp90-dependent client proteins at approximately 700 microM.	Novobiocin	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
17132020-2	2006	Recent studies have shown that novobiocin binds to a previously unrecognized ATP-binding site at the C-terminus of Hsp90 and induces degradation of Hsp90-dependent client proteins at approximately 700 microM.	Novobiocin	31-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
17132020-2	2006	Recent studies have shown that novobiocin binds to a previously unrecognized ATP-binding site at the C-terminus of Hsp90 and induces degradation of Hsp90-dependent client proteins at approximately 700 microM.	Adenosine Triphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
17132020-4	2006	These data suggested that the 4-hydroxy moiety of the coumarin ring and the 3"-carbamate of the noviose appendage were detrimental to Hsp90 inhibitory activity.	coumarin	54-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
17132020-4	2006	These data suggested that the 4-hydroxy moiety of the coumarin ring and the 3"-carbamate of the noviose appendage were detrimental to Hsp90 inhibitory activity.	3"-carbamate	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
17132020-4	2006	These data suggested that the 4-hydroxy moiety of the coumarin ring and the 3"-carbamate of the noviose appendage were detrimental to Hsp90 inhibitory activity.	noviose	96-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
17132020-8	2006	Thus, we have established the first set of compounds that clearly differentiate between the C-terminus of Hsp90 and DNA gyrase, converted a well-established gyrase inhibitor into a selective Hsp90 inhibitor, and confirmed essential structure-activity relationships for the coumermycin family of antibiotics.	coumermycin	273-284	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
17132020-8	2006	Thus, we have established the first set of compounds that clearly differentiate between the C-terminus of Hsp90 and DNA gyrase, converted a well-established gyrase inhibitor into a selective Hsp90 inhibitor, and confirmed essential structure-activity relationships for the coumermycin family of antibiotics.	coumermycin	273-284	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
17259553-5	2006	The chaperone function of HSP90 requires the formation of a multichaperone complex, which is dependent on the hydrolysis of ATP and ADP/ATP exchange.	Adenosine Triphosphate	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
17259553-5	2006	The chaperone function of HSP90 requires the formation of a multichaperone complex, which is dependent on the hydrolysis of ATP and ADP/ATP exchange.	Adenosine Diphosphate	132-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
17259553-5	2006	The chaperone function of HSP90 requires the formation of a multichaperone complex, which is dependent on the hydrolysis of ATP and ADP/ATP exchange.	Adenosine Triphosphate	136-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
17157164-0	2006	The HSP90 inhibitor 17-AAG synergizes with doxorubicin and U0126 in anaplastic large cell lymphoma irrespective of ALK expression.	tanespimycin	20-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17157164-0	2006	The HSP90 inhibitor 17-AAG synergizes with doxorubicin and U0126 in anaplastic large cell lymphoma irrespective of ALK expression.	Doxorubicin	43-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17157164-2	2006	Here we demonstrate that HSP90 is overexpressed in primary and cultured ALK-positive and ALK-negative ALCL cells, and we evaluate the potential role of the small molecule inhibitor of HSP90, 17-allylamino-17-demethoxygeldanamycin (17-AAG) in treating ALCL.	tanespimycin	231-237	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
17157164-0	2006	The HSP90 inhibitor 17-AAG synergizes with doxorubicin and U0126 in anaplastic large cell lymphoma irrespective of ALK expression.	U 0126	59-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
17157164-9	2006	CONCLUSION: Our data demonstrate that targeting HSP90 function by 17-AAG may offer a novel therapeutic strategy for ALCL, either as single-agent activity or by combining 17-AAG with conventional or targeted therapeutic schemes.	tanespimycin	66-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
17157164-9	2006	CONCLUSION: Our data demonstrate that targeting HSP90 function by 17-AAG may offer a novel therapeutic strategy for ALCL, either as single-agent activity or by combining 17-AAG with conventional or targeted therapeutic schemes.	tanespimycin	170-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
21672786-10	2006	Other environmental factors, such as biological chemicals (for example the antibiotic geldanamycin) can reduce the levels of active Hsp90 providing another mechanism for the emergence of mutant signaling pathways.	geldanamycin	86-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
17172411-7	2006	Mechanistically, TS protein was found to interact with heat shock protein (Hsp) complex, and trichostatin A treatment induced chaperonic Hsp90 acetylation and subsequently enhanced Hsp70 binding to TS, which led to the proteasomal degradation of TS protein.	trichostatin A	93-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
17233535-0	2006	Geldanamycin, an inhibitor of Hsp90, blocks cytoplasmic retention of progesterone receptors and glucocorticoid receptors via their respective ligand binding domains.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
16926059-0	2006	Lipophilic prodrugs of Hsp90 inhibitor geldanamycin for nanoencapsulation in poly(ethylene glycol)-b-poly(epsilon-caprolactone) micelles.	geldanamycin	39-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
16926059-0	2006	Lipophilic prodrugs of Hsp90 inhibitor geldanamycin for nanoencapsulation in poly(ethylene glycol)-b-poly(epsilon-caprolactone) micelles.	poly(epsilon-caprolactone)-b-poly(ethylene glycol)	77-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
16959221-0	2006	The HSP90 and DNA topoisomerase VI inhibitor radicicol also inhibits human type II DNA topoisomerase.	monorden	45-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16959221-2	2006	These drugs interact with the ATP-binding site of HSP90 which is characterized by a structural element known as the Bergerat fold, also present in type II DNA topoisomerases (Topo II).	Adenosine Triphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
17010336-8	2006	However, when Hsp90-p23 complexes are disrupted by the Hsp90 inhibitor geldanamycin, p23 moves by free diffusion while Hsp90 maintains its low mobility because it remains bound in remodeled multicomponent complexes.	geldanamycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17010336-8	2006	However, when Hsp90-p23 complexes are disrupted by the Hsp90 inhibitor geldanamycin, p23 moves by free diffusion while Hsp90 maintains its low mobility because it remains bound in remodeled multicomponent complexes.	geldanamycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
17010336-8	2006	However, when Hsp90-p23 complexes are disrupted by the Hsp90 inhibitor geldanamycin, p23 moves by free diffusion while Hsp90 maintains its low mobility because it remains bound in remodeled multicomponent complexes.	geldanamycin	71-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
17121904-0	2006	Combination mammalian target of rapamycin inhibitor rapamycin and HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin has synergistic activity in multiple myeloma.	tanespimycin	82-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
17108135-1	2006	17-Allylamino-demethoxygeldanamycin (17-AAG), currently in phase I and II clinical trials as an anticancer agent, binds to the ATP pocket of heat shock protein (Hsp90).	17-allylamino-demethoxygeldanamycin	0-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
17108135-1	2006	17-Allylamino-demethoxygeldanamycin (17-AAG), currently in phase I and II clinical trials as an anticancer agent, binds to the ATP pocket of heat shock protein (Hsp90).	Adenosine Triphosphate	127-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
17108135-11	2006	Clinical modulation of GSH may therefore enhance the efficacy of Hsp90-directed therapy.	Glutathione	23-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
17121904-3	2006	Our objective was to determine the effects of the mTOR inhibitor rapamycin and the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) on multiple myeloma cells.	tanespimycin	99-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
17121904-3	2006	Our objective was to determine the effects of the mTOR inhibitor rapamycin and the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) on multiple myeloma cells.	tanespimycin	139-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
16968706-11	2006	Treatment of cells with geldanamycin to disrupt the Hsp90 complex led to proteasomal degradation of RIP1.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
16973602-10	2006	Based on thioflavin T reactivity, the combination of Hsp70/40 and Hsp90 caused structural changes in oligomers but had little effect on fibrils.	thioflavin T	9-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
17090671-0	2006	Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90.	tanespimycin	15-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
17090671-0	2006	Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90.	tanespimycin	82-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
17090671-3	2006	17-Allylamino-17-demethoxygeldanamycin (17-AAG), the most studied agent directed against Hsp90, suffers from poor physical-chemical properties that limit its clinical potential.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
17090671-5	2006	IPI-504, the highly soluble hydroquinone hydrochloride derivative of 17-AAG, was synthesized as an Hsp90 inhibitor with favorable pharmaceutical properties.	tanespimycin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
17090671-9	2006	In conclusion, IPI-504, a potent inhibitor of Hsp90, is efficacious in cellular and animal models of myeloma.	tanespimycin	15-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
17090671-11	2006	Importantly, it was observed that IPI-504 interconverts with the known agent 17-AAG in vitro and in vivo via an oxidation-reduction equilibrium, and we demonstrate that IPI-504 is the slightly more potent inhibitor of Hsp90.	tanespimycin	34-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	218-223
17090671-11	2006	Importantly, it was observed that IPI-504 interconverts with the known agent 17-AAG in vitro and in vivo via an oxidation-reduction equilibrium, and we demonstrate that IPI-504 is the slightly more potent inhibitor of Hsp90.	tanespimycin	169-176	heat shock protein 90 alpha family class A member 1	Homo sapiens	218-223
16968702-3	2006	Geldanamycin occludes the N-terminal ATP-binding site of Hsp90, whereas novobiocin targets the C-terminal region of the chaperone.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
16968702-3	2006	Geldanamycin occludes the N-terminal ATP-binding site of Hsp90, whereas novobiocin targets the C-terminal region of the chaperone.	Adenosine Triphosphate	37-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
16968702-5	2006	Hsp90 cross-linking to preprotein and coprecipitation of Hsp90 with Tom70 were both impaired by novobiocin.	Novobiocin	96-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16968702-5	2006	Hsp90 cross-linking to preprotein and coprecipitation of Hsp90 with Tom70 were both impaired by novobiocin.	Novobiocin	96-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
16978890-5	2006	The proteomic analysis (2-D electrophoresis combined with MALDI-TOF mass spectrometry and/or Western blotting) revealed several proteins that were differentially expressed or their mobility was altered due to butyrate treatment, namely, HSP90, HSP70, p23, cyclophilin A (CYPA), prefoldin2 (PFD2) and alpha-, gamma-, epsilon-human globin chains.	Butyrates	209-217	heat shock protein 90 alpha family class A member 1	Homo sapiens	237-242
17185503-4	2006	Because numerous oncoproteins belonging to the Hsp90 client protein family are selectively degraded by Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG), a first-in-class Hsp90 inhibitor, is now under clinical trials as a novel molecular-targeted agent for a wide range of malignancies.	tanespimycin	121-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
17185503-4	2006	Because numerous oncoproteins belonging to the Hsp90 client protein family are selectively degraded by Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG), a first-in-class Hsp90 inhibitor, is now under clinical trials as a novel molecular-targeted agent for a wide range of malignancies.	tanespimycin	121-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
17185503-4	2006	Because numerous oncoproteins belonging to the Hsp90 client protein family are selectively degraded by Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG), a first-in-class Hsp90 inhibitor, is now under clinical trials as a novel molecular-targeted agent for a wide range of malignancies.	tanespimycin	121-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
17185503-5	2006	In spinal and bulbar muscular atrophy (SBMA), the pathogenic gene product is polyglutamine (polyQ)-expanded androgen receptor (AR), which belongs to the Hsp90 client protein family and is known to be degraded by 17-AAG.	polyglutamine	77-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
17185503-5	2006	In spinal and bulbar muscular atrophy (SBMA), the pathogenic gene product is polyglutamine (polyQ)-expanded androgen receptor (AR), which belongs to the Hsp90 client protein family and is known to be degraded by 17-AAG.	polyglutamine	92-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
17085670-0	2006	Schedule-dependent synergy between the heat shock protein 90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin and doxorubicin restores apoptosis to p53-mutant lymphoma cell lines.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	71-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-60
17085670-2	2006	Here, we examined the effect of the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG) on doxorubicin-induced apoptosis in lymphoma.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	76-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-57
17085670-2	2006	Here, we examined the effect of the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG) on doxorubicin-induced apoptosis in lymphoma.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	76-129	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
17085670-2	2006	Here, we examined the effect of the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG) on doxorubicin-induced apoptosis in lymphoma.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	131-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
17085670-2	2006	Here, we examined the effect of the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG) on doxorubicin-induced apoptosis in lymphoma.	Doxorubicin	140-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-57
17085670-2	2006	Here, we examined the effect of the heat shock protein 90 (HSP90) inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG) on doxorubicin-induced apoptosis in lymphoma.	Doxorubicin	140-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
17085670-11	2006	DMAG-mediated down-regulation of CHK1, a known HSP90 client, forced doxorubicin-treated cells into premature mitosis followed by apoptosis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
17085670-11	2006	DMAG-mediated down-regulation of CHK1, a known HSP90 client, forced doxorubicin-treated cells into premature mitosis followed by apoptosis.	Doxorubicin	68-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
17088896-3	2006	Here, we show that the IkappaB kinase (IKK), an essential activator of NF-kappaB, is selectively degraded by autophagy when Hsp90 is inhibited by geldanamycin (GA), a specific Hsp90 inhibitor showing highly effective anti-tumor activity.	geldanamycin	146-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
17088896-3	2006	Here, we show that the IkappaB kinase (IKK), an essential activator of NF-kappaB, is selectively degraded by autophagy when Hsp90 is inhibited by geldanamycin (GA), a specific Hsp90 inhibitor showing highly effective anti-tumor activity.	geldanamycin	146-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
17088896-3	2006	Here, we show that the IkappaB kinase (IKK), an essential activator of NF-kappaB, is selectively degraded by autophagy when Hsp90 is inhibited by geldanamycin (GA), a specific Hsp90 inhibitor showing highly effective anti-tumor activity.	geldanamycin	160-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
17088896-3	2006	Here, we show that the IkappaB kinase (IKK), an essential activator of NF-kappaB, is selectively degraded by autophagy when Hsp90 is inhibited by geldanamycin (GA), a specific Hsp90 inhibitor showing highly effective anti-tumor activity.	geldanamycin	160-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
17114002-0	2006	Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol.	monorden	139-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16832603-1	2006	The aim of this study was to determine the antitumor activity of 17-(Allylamino)-17-demethoxyge-ldanamycin (17-AAG), a heat shock protein 90(hsp90) inhibitor in patients with metastatic papillary renal cell carcinoma (RCC) or metastatic clear cell RCC.	tanespimycin	65-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
17096299-0	2006	Purine-scaffold Hsp90 inhibitors.	purine	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
17096299-2	2006	A clinical evaluation of 17-AAG, the first Hsp90 inhibitor to enter the clinic, revealed evidence of activity for the compound at a manageable level of toxicity.	tanespimycin	25-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
17096299-5	2006	This feature describes the purine-scaffold class of Hsp90 inhibitors, focusing on research efforts from the discovery stage to the clinical translation of such compounds.	purine	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
17016641-0	2006	P53-dependent radiosensitizing effects of Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin on human oral squamous cell carcinoma cell lines.	tanespimycin	58-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
17114345-9	2006	The results also show that inhibition of HSP90 with geldanamycin or 17-(allylamino)-17-demethoxygeldanamycin attenuates FGF1-induced binding of MUC1 to HSP90 and targeting of MUC1 to the mitochondrial outer membrane.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
17114345-9	2006	The results also show that inhibition of HSP90 with geldanamycin or 17-(allylamino)-17-demethoxygeldanamycin attenuates FGF1-induced binding of MUC1 to HSP90 and targeting of MUC1 to the mitochondrial outer membrane.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
17114345-9	2006	The results also show that inhibition of HSP90 with geldanamycin or 17-(allylamino)-17-demethoxygeldanamycin attenuates FGF1-induced binding of MUC1 to HSP90 and targeting of MUC1 to the mitochondrial outer membrane.	tanespimycin	68-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
17088927-7	2006	Inhibitors of HSP90, such as geldanamycin and its derivatives (17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxygeldanamycin, known as 17AAG and 17DMAG, respectively) are available and have shown activity both in vivo and in vitro.	geldanamycin	29-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16950627-3	2006	Hsf1act and the Hsp90 inhibitor, geldanamycin, induced high expression of multiple Hsps in cultured motor neurons and conferred dramatic neuroprotection against SOD1G93A in comparison to Hsp70 or Hsp25 alone.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
16950627-4	2006	Two other Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG) and radicicol, and pyrrolidine dithiocarbamate induced robust expression of Hsp70 and Hsp40 in motor neurons, but at cytotoxic concentrations.	tanespimycin	28-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
17088927-7	2006	Inhibitors of HSP90, such as geldanamycin and its derivatives (17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxygeldanamycin, known as 17AAG and 17DMAG, respectively) are available and have shown activity both in vivo and in vitro.	tanespimycin	63-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16950627-4	2006	Two other Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG) and radicicol, and pyrrolidine dithiocarbamate induced robust expression of Hsp70 and Hsp40 in motor neurons, but at cytotoxic concentrations.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
16950627-4	2006	Two other Hsp90 inhibitors, 17-allylamino-17-demethoxygeldanamycin (17-AAG) and radicicol, and pyrrolidine dithiocarbamate induced robust expression of Hsp70 and Hsp40 in motor neurons, but at cytotoxic concentrations.	monorden	80-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
17088927-7	2006	Inhibitors of HSP90, such as geldanamycin and its derivatives (17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxygeldanamycin, known as 17AAG and 17DMAG, respectively) are available and have shown activity both in vivo and in vitro.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	106-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17088927-7	2006	Inhibitors of HSP90, such as geldanamycin and its derivatives (17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxygeldanamycin, known as 17AAG and 17DMAG, respectively) are available and have shown activity both in vivo and in vitro.	tanespimycin	168-173	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17088927-7	2006	Inhibitors of HSP90, such as geldanamycin and its derivatives (17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxygeldanamycin, known as 17AAG and 17DMAG, respectively) are available and have shown activity both in vivo and in vitro.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	178-184	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17034135-3	2006	Molecular docking with two different programs (Affinity and Autodock) showed that the prodrug (17-AG-C2-Gal) was unable to bind to Hsp90; however, the product (17-AG-C2), enzymatically cleaved by beta-galactosidase conjugate, bound to Hsp90 in a similar way as geldanamycin and 17-AG.	17-amino-17-demethoxygeldanamycin -C2-galactose	95-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	235-240
16926159-7	2006	Although STAT3 coprecipitated with heat-shock protein 90 (Hsp90) in control cells, coprecipitation of the two proteins was greatly reduced after PDTC treatment or after exposure to geldanamycin, an Hsp90 inhibitor.	geldanamycin	181-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-56
16926159-7	2006	Although STAT3 coprecipitated with heat-shock protein 90 (Hsp90) in control cells, coprecipitation of the two proteins was greatly reduced after PDTC treatment or after exposure to geldanamycin, an Hsp90 inhibitor.	geldanamycin	181-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
16926159-7	2006	Although STAT3 coprecipitated with heat-shock protein 90 (Hsp90) in control cells, coprecipitation of the two proteins was greatly reduced after PDTC treatment or after exposure to geldanamycin, an Hsp90 inhibitor.	geldanamycin	181-193	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
17024179-6	2006	Treatment of HCV replicon cells with geldanamycin, an inhibitor of Hsp90, suppressed RNA replication in a dose-dependent manner.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
17034135-3	2006	Molecular docking with two different programs (Affinity and Autodock) showed that the prodrug (17-AG-C2-Gal) was unable to bind to Hsp90; however, the product (17-AG-C2), enzymatically cleaved by beta-galactosidase conjugate, bound to Hsp90 in a similar way as geldanamycin and 17-AG.	17-AG	95-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	235-240
16697713-0	2006	Bisphosphonates activate nucleotide receptors signaling and induce the expression of Hsp90 in osteoblast-like cell lines.	Diphosphonates	0-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	85-90
17020320-0	2006	Synthesis and evaluation of coumermycin A1 analogues that inhibit the Hsp90 protein folding machinery.	coumermycin	28-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
17020320-1	2006	[structure: see text] The coumarin antibiotics are not only potent inhibitors of DNA gyrase but also represent the most effective C-terminal inhibitors of 90 kDa heat shock proteins (Hsp90) reported thus far.	coumarin	26-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
16887805-5	2006	Here we demonstrate that Hsp60, Hsp70, and Hsp90 both alone and in combination provide differential protection against intracellular beta-amyloid stress through the maintenance of mitochondrial oxidative phosphorylation and functionality of tricarboxylic acid cycle enzymes.	Tricarboxylic Acids	241-259	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
17010675-5	2006	Validating this prediction, we demonstrate that celastrol and gedunin inhibit HSP90 activity and HSP90 clients, including AR.	celastrol	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
17010675-5	2006	Validating this prediction, we demonstrate that celastrol and gedunin inhibit HSP90 activity and HSP90 clients, including AR.	celastrol	48-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
16697713-6	2006	Differential proteomics analysis identified Hsp90 upregulation as a result of risedronate effect on HOBIT and MG-63 cells.	Risedronic Acid	78-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
16697713-8	2006	In fact, functional inactivation of Hsp90 by the specific inhibitor 17-AAG prevents the bisphosphonate-induced mitogenic effects in osteoblasts.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
16697713-8	2006	In fact, functional inactivation of Hsp90 by the specific inhibitor 17-AAG prevents the bisphosphonate-induced mitogenic effects in osteoblasts.	Diphosphonates	88-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
16697713-9	2006	These findings show that bisphosphonates, by inducing ATP release, may also act through nucleotide receptors signaling leading to ERKs activation and may exert their mitogenic role on osteoblasts through the involvement of Hsp90.	Diphosphonates	25-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
16697713-9	2006	These findings show that bisphosphonates, by inducing ATP release, may also act through nucleotide receptors signaling leading to ERKs activation and may exert their mitogenic role on osteoblasts through the involvement of Hsp90.	Adenosine Triphosphate	54-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	223-228
16741950-0	2006	Nucleotide receptors stimulation by extracellular ATP controls Hsp90 expression through APE1/Ref-1 in thyroid cancer cells: a novel tumorigenic pathway.	Adenosine Triphosphate	50-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
16741950-7	2006	Among other proteins, Hsp90 was found upregulated upon ATP stimulation.	Adenosine Triphosphate	55-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
16741950-8	2006	Pretreatment with suramin completely blocked the ATP-induced Hsp90 activation, confirming the involvement of cell-surface P2 nucleotide receptors in the ATP-mediated activation of ARO cells.	Suramin	18-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
16741950-8	2006	Pretreatment with suramin completely blocked the ATP-induced Hsp90 activation, confirming the involvement of cell-surface P2 nucleotide receptors in the ATP-mediated activation of ARO cells.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
16741950-8	2006	Pretreatment with suramin completely blocked the ATP-induced Hsp90 activation, confirming the involvement of cell-surface P2 nucleotide receptors in the ATP-mediated activation of ARO cells.	Adenosine Triphosphate	153-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
16741950-9	2006	Treatment of proliferating ARO cells with suramin and apyrase significantly reduced the intracellular levels of Hsp90, suggesting an autocrine/paracrine mechanism of control on Hsp90 expression by extracellular ATP.	Suramin	42-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
16741950-9	2006	Treatment of proliferating ARO cells with suramin and apyrase significantly reduced the intracellular levels of Hsp90, suggesting an autocrine/paracrine mechanism of control on Hsp90 expression by extracellular ATP.	Suramin	42-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
16741950-9	2006	Treatment of proliferating ARO cells with suramin and apyrase significantly reduced the intracellular levels of Hsp90, suggesting an autocrine/paracrine mechanism of control on Hsp90 expression by extracellular ATP.	Adenosine Triphosphate	211-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
16741950-9	2006	Treatment of proliferating ARO cells with suramin and apyrase significantly reduced the intracellular levels of Hsp90, suggesting an autocrine/paracrine mechanism of control on Hsp90 expression by extracellular ATP.	Adenosine Triphosphate	211-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
16741950-10	2006	The influence of Hsp90 on ATP-induced cell proliferation was also demonstrated by its specific inhibition with 17-AAG.	Adenosine Triphosphate	26-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
16741950-10	2006	The influence of Hsp90 on ATP-induced cell proliferation was also demonstrated by its specific inhibition with 17-AAG.	tanespimycin	111-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
16741950-11	2006	The molecular pathway by which ATP stimulates cell proliferation was further investigated by siRNA strategies showing that Hsp90 is a target of APE1/Ref-1 functional activation.	Adenosine Triphosphate	31-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
16825487-1	2006	We have previously evaluated the role of NAD(P)H:quinone oxidoreductase 1 (NQO1) in the bioreductive metabolism of 17-(allylamino)-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone, a more potent 90-kDa heat shock protein (Hsp90) inhibitor.	17-(allylamino)-demethoxygeldanamycin	115-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	237-242
16825487-1	2006	We have previously evaluated the role of NAD(P)H:quinone oxidoreductase 1 (NQO1) in the bioreductive metabolism of 17-(allylamino)-demethoxygeldanamycin (17AAG) to the corresponding hydroquinone, a more potent 90-kDa heat shock protein (Hsp90) inhibitor.	tanespimycin	154-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	237-242
16825487-9	2006	In conclusion, these studies show that the reduction of this series of benzoquinone ansamycins by NQO1 generates the corresponding hydroquinone ansamycins, which exhibit enhanced Hsp90 inhibition.	benzoquinone ansamycins	71-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
16825487-9	2006	In conclusion, these studies show that the reduction of this series of benzoquinone ansamycins by NQO1 generates the corresponding hydroquinone ansamycins, which exhibit enhanced Hsp90 inhibition.	hydroquinone ansamycins	131-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	179-184
17073714-3	2006	Recently, it was determined that Hsp90 bound to a client protein in a co-chaperone complex has a higher ATPase activity and binds to the geldanamycin inhibitor with over 100-fold higher affinity than the low-ATPase form.	geldanamycin	137-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	geldanamycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	tanespimycin	119-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	130-137	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	monorden	153-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	purine	180-186	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	Pyrazoles	209-218	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-5	2006	Numerous classes of Hsp90 inhibitors have recently been developed, such as the anasamysin geldanamycin and derivatives 17-AAG and 17-DMAG; the macrolide radicicol and derivatives; purine-scaffold derivatives; pyrazoles; and shepherdins that bind to the N-terminal high-affinity ATP-binding domain of Hsp90.	Adenosine Triphosphate	278-281	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
17073714-6	2006	Other inhibitors have recently been shown to bind to the C-terminal dimerization domain of Hsp90, such as cisplatin and novobiocin, or modify Hsp90 postranslationally, such as histone deacetylase or proteasome inhibitors.	Cisplatin	106-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
17073714-6	2006	Other inhibitors have recently been shown to bind to the C-terminal dimerization domain of Hsp90, such as cisplatin and novobiocin, or modify Hsp90 postranslationally, such as histone deacetylase or proteasome inhibitors.	Novobiocin	120-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	Imatinib Mesylate	276-284	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
16995666-2	2006	Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site.	monorden	62-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
16995666-2	2006	Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site.	geldanamycin	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
16995666-2	2006	Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site.	Adenosine Triphosphate	136-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
16995666-3	2006	The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed.	monorden	161-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
16995666-3	2006	The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed.	geldanamycin	175-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
16995666-4	2006	A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.	monorden	35-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
16995666-4	2006	A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
16938294-3	2006	IKK activation pathways normally require heat shock protein 90 (Hsp90), a chaperone that regulates the stability and activity of signalling molecules and can be blocked by the benzoquinone ansamycin compound geldanamycin (GA).	benzoquinone ansamycin	176-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
16938294-3	2006	IKK activation pathways normally require heat shock protein 90 (Hsp90), a chaperone that regulates the stability and activity of signalling molecules and can be blocked by the benzoquinone ansamycin compound geldanamycin (GA).	benzoquinone ansamycin	176-198	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16938294-3	2006	IKK activation pathways normally require heat shock protein 90 (Hsp90), a chaperone that regulates the stability and activity of signalling molecules and can be blocked by the benzoquinone ansamycin compound geldanamycin (GA).	geldanamycin	208-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
16938294-3	2006	IKK activation pathways normally require heat shock protein 90 (Hsp90), a chaperone that regulates the stability and activity of signalling molecules and can be blocked by the benzoquinone ansamycin compound geldanamycin (GA).	geldanamycin	208-220	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16938294-3	2006	IKK activation pathways normally require heat shock protein 90 (Hsp90), a chaperone that regulates the stability and activity of signalling molecules and can be blocked by the benzoquinone ansamycin compound geldanamycin (GA).	geldanamycin	222-224	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
16938294-3	2006	IKK activation pathways normally require heat shock protein 90 (Hsp90), a chaperone that regulates the stability and activity of signalling molecules and can be blocked by the benzoquinone ansamycin compound geldanamycin (GA).	geldanamycin	222-224	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16982758-0	2006	Heat shock protein 90 inhibition in imatinib-resistant gastrointestinal stromal tumor.	Imatinib Mesylate	36-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	tanespimycin	204-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	tanespimycin	204-210	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	Imatinib Mesylate	219-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	Imatinib Mesylate	219-227	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	gist882	254-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	Imatinib Mesylate	276-284	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
16982758-3	2006	Heat shock protein 90 (HSP90) protects KIT oncoproteins from proteasome-mediated degradation, and we therefore did preclinical validations of the HSP90 inhibitor, 17-allylamino-18-demethoxy-geldanamycin (17-AAG), in an imatinib-sensitive GIST cell line (GIST882) and in novel imatinib-resistant GIST lines that are either dependent on (GIST430 and GIST48) or independent of (GIST62) KIT oncoproteins.	gist882	254-261	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
16982758-8	2006	The dramatic inactivation of imatinib-resistant KIT oncoproteins suggests that HSP90 inhibition provides a therapeutic solution to the challenge of heterogeneous imatinib resistance mutations in GIST patients.	Imatinib Mesylate	29-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
16982758-8	2006	The dramatic inactivation of imatinib-resistant KIT oncoproteins suggests that HSP90 inhibition provides a therapeutic solution to the challenge of heterogeneous imatinib resistance mutations in GIST patients.	Imatinib Mesylate	162-170	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-84
16854979-8	2006	Mutation studies indicate that client binding, interactions between Hsp40 and Hsp70, plus ATP hydrolysis by Hsp70 are all required to promote conformational maturation of PR via the Hsp90 pathway.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
16840783-0	2006	The isoflavone Equol mediates rapid vascular relaxation: Ca2+-independent activation of endothelial nitric-oxide synthase/Hsp90 involving ERK1/2 and Akt phosphorylation in human endothelial cells.	Isoflavones	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
16797988-1	2006	The synthesis of a red-shifted cy3B-GM ligand and its evaluation as a fluorescence polarization probe for Hsp90 is presented.	cy3b-gm	31-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
17064567-8	2006	Significantly, berbamine also down-regulated chaperone Hsp90 protein, and the amount of Hsp90 protein in the leukemia cells treated with berbamine at 8 microg/ml for 48 h accounted for 18.37% of that of the untreated leukemia cells.	berbamine	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
16311509-2	2006	By depleting Hsp90-client oncoproteins, geldanamycin (GA) and 17-allylamino-17-demethoxy-GA (17-AAG) (heat-shock protein-90-active drugs) render certain oncoprotein-addictive cancer cells sensitive to chemotherapy.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
16311509-2	2006	By depleting Hsp90-client oncoproteins, geldanamycin (GA) and 17-allylamino-17-demethoxy-GA (17-AAG) (heat-shock protein-90-active drugs) render certain oncoprotein-addictive cancer cells sensitive to chemotherapy.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
16311509-2	2006	By depleting Hsp90-client oncoproteins, geldanamycin (GA) and 17-allylamino-17-demethoxy-GA (17-AAG) (heat-shock protein-90-active drugs) render certain oncoprotein-addictive cancer cells sensitive to chemotherapy.	tanespimycin	62-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
16966435-0	2006	Endoplasmic reticulum vacuolization and valosin-containing protein relocalization result from simultaneous hsp90 inhibition by geldanamycin and proteasome inhibition by velcade.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
16966435-2	2006	Geldanamycin interrupts Hsp90 chaperone activity and causes down-regulation of its many client proteins by the ubiquitin-proteasome pathway; Velcade is a specific proteasome inhibitor.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
16966435-4	2006	Cotreatment of cells with geldanamycin and Velcade prevents destruction of destabilized, ubiquitinated Hsp90 client proteins, causing them to accumulate.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
16966435-4	2006	Cotreatment of cells with geldanamycin and Velcade prevents destruction of destabilized, ubiquitinated Hsp90 client proteins, causing them to accumulate.	Bortezomib	43-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
17064567-8	2006	Significantly, berbamine also down-regulated chaperone Hsp90 protein, and the amount of Hsp90 protein in the leukemia cells treated with berbamine at 8 microg/ml for 48 h accounted for 18.37% of that of the untreated leukemia cells.	berbamine	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
17064567-10	2006	CONCLUSION: (1) Berbamine induces caspase-3-mediated apoptosis of Ph+ leukemia cells through inhibiting phosphorylation of p210 bcr/abl protein and down-regulating its chaperone Hsp90 protein.	berbamine	16-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	178-183
16884307-0	2006	Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors.	8-aryl-sulfanyl adenine	43-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
16751245-10	2006	Thus, tertiary structural changes resulting from the site-specific oxidation of a single methionine (i.e., Met145) promote the degradation of CaM by the proteasome/Hsp90, suggesting a mechanism to regulate cellular metabolism through the targeted modulation of CaM abundance in response to oxidative stress.	Methionine	89-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	Water	37-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	Water	37-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-183
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	8-aryl-sulfanyl adenine	51-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	8-aryl-sulfanyl adenine	51-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-183
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	Plutonium	102-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	Plutonium	102-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-183
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	Plutonium	117-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
16884307-2	2006	We report here the structures of the water soluble 8-aryl-sulfanyl adenine class Hsp90 inhibitors, 1 (PU-H71) and 2 (PU-H64), in complex with the N-terminal domain of human Hsp90alpha.	Plutonium	117-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-183
16884307-3	2006	The conformation of 1 when bound to Hsp90 differs from previously reported 8-aryl adenine Hsp90 inhibitors including 3 (PU24FCl).	8-aryl adenine	75-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
16884307-3	2006	The conformation of 1 when bound to Hsp90 differs from previously reported 8-aryl adenine Hsp90 inhibitors including 3 (PU24FCl).	PU24FCl	120-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
16884307-3	2006	The conformation of 1 when bound to Hsp90 differs from previously reported 8-aryl adenine Hsp90 inhibitors including 3 (PU24FCl).	PU24FCl	120-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
16884307-5	2006	This difference explains the opposing trends in Hsp90 inhibitory activity for the 2"-halo derivatives of the 3",4",5"-trimethoxy series where Cl &gt; Br &gt; I compared to the 4",5"-methylenedioxy series where I &gt; Br &gt; Cl.	Halodrol	85-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
16884307-5	2006	This difference explains the opposing trends in Hsp90 inhibitory activity for the 2"-halo derivatives of the 3",4",5"-trimethoxy series where Cl &gt; Br &gt; I compared to the 4",5"-methylenedioxy series where I &gt; Br &gt; Cl.	3",4",5"-trimethoxy	109-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
16844778-4	2006	Here, we show that the prototypical Hsp90 inhibitor geldanamycin induces Akt and Erk activation that is independent of PTEN status and is mediated by transient activation of Src kinase.	geldanamycin	52-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
16912198-0	2006	Taxotere-induced inhibition of human endothelial cell migration is a result of heat shock protein 90 degradation.	Docetaxel	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	79-100
16912198-3	2006	Here, we show that Taxotere caused the ubiquitination and subsequent proteasomal degradation of heat shock protein 90 (Hsp90) in HUVEC.	Docetaxel	19-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-117
16912198-3	2006	Here, we show that Taxotere caused the ubiquitination and subsequent proteasomal degradation of heat shock protein 90 (Hsp90) in HUVEC.	Docetaxel	19-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
16912198-5	2006	Taxotere prevented the VEGF-induced phosphorylation of focal adhesion kinase, Akt, and endothelial nitric oxide synthase (eNOS), all of which are Hsp90 client proteins.	Docetaxel	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	146-151
16912198-8	2006	Furthermore, overexpression of Hsp90 rescued HUVEC from the inhibition of VEGF-induced migration by Taxotere.	Docetaxel	100-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
16740632-5	2006	Gene silencing shows that CHIP activity is necessary to mediate Ron degradation upon cell treatment with Hsp90 inhibitors geldanamycins.	geldanamycin	122-135	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
16740632-9	2006	These data highlight a novel mechanism for Ron degradation and propose Hsp90 antagonists like geldanamycins as suitable pharmacological agents for therapy of cancers where altered Ron signaling is involved.	geldanamycin	94-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
16882944-11	2006	Shepherdin[79-83] made contact with unique residues in the ATP pocket of Hsp90 (Ile-96, Asp-102, and Phe-138), did not increase Hsp70 levels in AML cells, disrupted mitochondrial function within 2 minutes of treatment, and eliminated the expression of Hsp90 client proteins.	Adenosine Triphosphate	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
16882944-11	2006	Shepherdin[79-83] made contact with unique residues in the ATP pocket of Hsp90 (Ile-96, Asp-102, and Phe-138), did not increase Hsp70 levels in AML cells, disrupted mitochondrial function within 2 minutes of treatment, and eliminated the expression of Hsp90 client proteins.	Isoleucine	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
16882944-11	2006	Shepherdin[79-83] made contact with unique residues in the ATP pocket of Hsp90 (Ile-96, Asp-102, and Phe-138), did not increase Hsp70 levels in AML cells, disrupted mitochondrial function within 2 minutes of treatment, and eliminated the expression of Hsp90 client proteins.	Aspartic Acid	88-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
16882944-11	2006	Shepherdin[79-83] made contact with unique residues in the ATP pocket of Hsp90 (Ile-96, Asp-102, and Phe-138), did not increase Hsp70 levels in AML cells, disrupted mitochondrial function within 2 minutes of treatment, and eliminated the expression of Hsp90 client proteins.	Phenylalanine	101-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
16687576-3	2006	We find that Hsp90 forms a complex with guanine nucleotide dissociation inhibitor (GDI) to direct recycling of the client substrate Rab1 required for endoplasmic reticulum (ER)-to-Golgi transport.	Guanine Nucleotides	40-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
16687576-4	2006	ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol.	geldanamycin	66-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
16687576-4	2006	ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol.	geldanamycin	80-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
16687576-4	2006	ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	85-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
16687576-4	2006	ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	140-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
16687576-4	2006	ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol.	monorden	154-163	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
16854066-0	2006	Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90.	hydroquinone	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
16854066-0	2006	Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90.	17-Amino-17-demethoxygeldanamycin	76-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
16854066-0	2006	Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90.	Water	121-126	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
16854066-1	2006	17-Allylamino-17-demethoxygeldanamycin (17-AAG)1 is a semisynthetic inhibitor of the 90 kDa heat shock protein (Hsp90) currently in clinical trials for the treatment of cancer.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
16854066-1	2006	17-Allylamino-17-demethoxygeldanamycin (17-AAG)1 is a semisynthetic inhibitor of the 90 kDa heat shock protein (Hsp90) currently in clinical trials for the treatment of cancer.	tanespimycin	40-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
16844778-6	2006	We show that geldanamycin rapidly disrupts Src association with Hsp90, suggesting that Src activation results directly from dissociation of the chaperone.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16714764-5	2006	We also report that hsp90 inhibitors geldanamycin and novobiocin inhibit recombinant telomerase even after telomerase is assembled.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
16714764-5	2006	We also report that hsp90 inhibitors geldanamycin and novobiocin inhibit recombinant telomerase even after telomerase is assembled.	Novobiocin	54-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
16714764-6	2006	Inhibition by geldanamycin could be overcome by allowing telomerase to first bind its primer, suggesting a role for hsp90 in loading telomerase onto the telomere.	geldanamycin	14-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
16501598-0	2006	17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
16501598-0	2006	17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation.	tanespimycin	83-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
16501598-1	2006	The Hsp90 inhibitor 17-allylaminogeldanamycin (17-AAG), which is currently in clinical trials, is thought to exert antitumor activity by simultaneously targeting several oncogenic signaling pathways.	tanespimycin	20-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16501598-1	2006	The Hsp90 inhibitor 17-allylaminogeldanamycin (17-AAG), which is currently in clinical trials, is thought to exert antitumor activity by simultaneously targeting several oncogenic signaling pathways.	tanespimycin	47-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16501598-2	2006	Here we report a novel mechanism by which 17-AAG inhibits cell proliferation, and we provide the first evidence that HSP90 is required for the assembly of kinetochore protein complexes in humans.	tanespimycin	42-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
16501598-5	2006	We found that HSP90 associates with SGT1 (suppressor of G2 allele of skp1; SUGT1) in human cells and that depletion of SGT1 sensitizes HeLa cells to 17-AAG.	tanespimycin	149-155	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16501598-8	2006	Furthermore, time-course experiments revealed that transient treatment with 17-AAG between late S and G2/M phases causes substantial delocalization of CENP-H and CENP-I, a finding that strongly suggests that HSP90 participates in kinetochore assembly in a cell cycle-dependent manner.	tanespimycin	76-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-213
16489110-8	2006	Similarly to their effects on NO-donor-induced relaxation, 15-h exposure to RA, but not to GA, decreased hsp90-bound sGC protein expression and NTG-stimulated cGMP formation in aortic rings, whereas RA more than GA reduced SNN-stimulated cGMP formation.	monorden	76-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	105-110
16489110-9	2006	We conclude that RA, much more so than GA, selectively inhibits sGC-dependent relaxations of aortic rings by reducing sGC expression, disrupting sGC-hsp90 complex formation and decreasing cGMP formation.	monorden	17-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
17163756-2	2006	They spotlight the higher affinity of ansamycins" hydroquinone over the quinone form for Hsp90 and further discuss its possible contribution to ansamycins" tumor selectivity.	Lactams, Macrocyclic	38-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
16846475-6	2006	We showed that overexpression of activating transcription factor 3 (ATF3), ATF4, ATF5, c-Jun, JunD and caspase-3 is associated with sensitivity to bortezomib-induced apoptosis, whereas overexpression of heat shock protein (HSP)27, HSP70, HSP90 and T-cell factor 4 is associated with bortezomib resistance.	Bortezomib	147-157	heat shock protein 90 alpha family class A member 1	Homo sapiens	238-243
16923571-2	2006	Recent studies utilizing 17-allylamino-17-demethoxygeldanamycin (17-AAG), an inhibitor of HSP90, demonstrated an antitumor effect in solid tumors.	tanespimycin	25-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	90-95
17147113-8	2006	Cabamazepine treatment could induce a higher acetylation level of HSP90 and destroy its chaperon function.	cabamazepine	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
17163756-2	2006	They spotlight the higher affinity of ansamycins" hydroquinone over the quinone form for Hsp90 and further discuss its possible contribution to ansamycins" tumor selectivity.	hydroquinone	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
17163756-2	2006	They spotlight the higher affinity of ansamycins" hydroquinone over the quinone form for Hsp90 and further discuss its possible contribution to ansamycins" tumor selectivity.	quinone	55-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
17163756-2	2006	They spotlight the higher affinity of ansamycins" hydroquinone over the quinone form for Hsp90 and further discuss its possible contribution to ansamycins" tumor selectivity.	Lactams, Macrocyclic	144-154	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
16503144-3	2006	Purine-based compounds have found new applications as inducers of interferon and lineage-committed cell dedifferentiation, agonists and antagonists of adenosine receptors, ligands of corticotropin-releasing hormone receptors, and as inhibitors of HSP90, Src kinase, p38alpha MAP kinase, sulfotransferases, phosphodiesterases, and Cdks.	purine	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	247-252
16682002-2	2006	Here, we report that F(1)F(0)-ATP synthase, the enzyme responsible for the mitochondrial production of ATP, is a co-chaperone of Hsp90.	Adenosine Triphosphate	30-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
16723087-0	2006	Down-regulation of p210(bcr/abl) by curcumin involves disrupting molecular chaperone functions of Hsp90.	Curcumin	36-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
16641196-7	2006	Mutation of a proline residue within this sequence to glutamic acid reduces its interaction with Hsp90, inhibits homodimer formation, and reduces its half-life to 4 h. These findings implicate Hsp90 in the stabilization of LIMK1 by promoting homodimer formation and transphosphorylation.	Proline	14-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
16641196-7	2006	Mutation of a proline residue within this sequence to glutamic acid reduces its interaction with Hsp90, inhibits homodimer formation, and reduces its half-life to 4 h. These findings implicate Hsp90 in the stabilization of LIMK1 by promoting homodimer formation and transphosphorylation.	Proline	14-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
16385570-7	2006	The Hsp90 inhibitors geldanamycin, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and radicicol significantly enhanced the activity of the topoisomerase II poisons etoposide and mitoxantrone in vitro and in vivo.	geldanamycin	21-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16641196-7	2006	Mutation of a proline residue within this sequence to glutamic acid reduces its interaction with Hsp90, inhibits homodimer formation, and reduces its half-life to 4 h. These findings implicate Hsp90 in the stabilization of LIMK1 by promoting homodimer formation and transphosphorylation.	Glutamic Acid	54-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
16385570-7	2006	The Hsp90 inhibitors geldanamycin, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and radicicol significantly enhanced the activity of the topoisomerase II poisons etoposide and mitoxantrone in vitro and in vivo.	tanespimycin	35-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16385570-7	2006	The Hsp90 inhibitors geldanamycin, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and radicicol significantly enhanced the activity of the topoisomerase II poisons etoposide and mitoxantrone in vitro and in vivo.	tanespimycin	43-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16641196-7	2006	Mutation of a proline residue within this sequence to glutamic acid reduces its interaction with Hsp90, inhibits homodimer formation, and reduces its half-life to 4 h. These findings implicate Hsp90 in the stabilization of LIMK1 by promoting homodimer formation and transphosphorylation.	Glutamic Acid	54-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
16385570-7	2006	The Hsp90 inhibitors geldanamycin, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and radicicol significantly enhanced the activity of the topoisomerase II poisons etoposide and mitoxantrone in vitro and in vivo.	monorden	87-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16513847-0	2006	Geldanamycin, an inhibitor of Hsp90, potentiates cytochrome P4502E1-mediated toxicity in HepG2 cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
16385570-7	2006	The Hsp90 inhibitors geldanamycin, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and radicicol significantly enhanced the activity of the topoisomerase II poisons etoposide and mitoxantrone in vitro and in vivo.	Etoposide	165-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16385570-7	2006	The Hsp90 inhibitors geldanamycin, 17-AAG (17-allylamino-17-demethoxygeldanamycin) and radicicol significantly enhanced the activity of the topoisomerase II poisons etoposide and mitoxantrone in vitro and in vivo.	Mitoxantrone	179-191	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16495075-7	2006	ALA-PDT led to the perturbation of the Hsp90/p23 multichaperone complex of which the Bcr-Abl is the client protein.	5-amino levulinic acid	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
16513847-6	2006	An enhanced loss of E47 cell viability was also observed using two different inhibitors of Hsp90, herbimycin A and radicicol.	herbimycin	98-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
16513847-6	2006	An enhanced loss of E47 cell viability was also observed using two different inhibitors of Hsp90, herbimycin A and radicicol.	monorden	115-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
16698020-5	2006	In this study, we show that heat shock protein 90 physically interacts with HGTD-P and that suppression of Hsp90 activity by low concentrations of geldanamycin reduced HGTD-P-induced mitochondrial catastrophe through inhibition of mitochondrial translocation of HGTD-P.	geldanamycin	147-159	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
16731965-1	2006	The structural basis for the coupling of ATP binding and hydrolysis to chaperone activity remains a central question in Hsp90 biology.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
16731965-2	2006	By analogy to MutL, ATP binding to Hsp90 is thought to promote intramolecular N-terminal dimerization, yielding a molecular clamp functioning in substrate protein activation.	Adenosine Triphosphate	20-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
16565516-3	2006	Titration of p23 with Hsp90 results in the selective broadening of certain cross-peaks in the 15N-1H heteronuclear single quantum correlation (HSQC) spectrum.	15n	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
16565516-3	2006	Titration of p23 with Hsp90 results in the selective broadening of certain cross-peaks in the 15N-1H heteronuclear single quantum correlation (HSQC) spectrum.	Hydrogen	98-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
16684877-0	2006	A biochemical rationale for the anticancer effects of Hsp90 inhibitors: slow, tight binding inhibition by geldanamycin and its analogues.	geldanamycin	106-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
16684877-2	2006	Two analogues of the Hsp90 inhibitor geldanamycin are currently in clinical trials.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	21-26
16684877-3	2006	Geldanamycin (GA) and its analogues have been reported to bind purified Hsp90 with low micromolar potency, in stark contrast to their low nanomolar antiproliferative activity in cell culture and their potent antitumor activity in animal models.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
16684877-3	2006	Geldanamycin (GA) and its analogues have been reported to bind purified Hsp90 with low micromolar potency, in stark contrast to their low nanomolar antiproliferative activity in cell culture and their potent antitumor activity in animal models.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
16684877-9	2006	Therefore, our results indicate that the high potency of GA in cell culture and in vivo can be accounted for by its time-dependent, tight binding to Hsp90 alone.	geldanamycin	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	149-154
16634649-2	2006	The ansamycins, geldanamycin (GA) and its derivative, 17-allylaminogeldanamycin (17-AAG), inhibit Hsp90.	Lactams, Macrocyclic	4-14	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
16619024-5	2006	We propose that Toc64 acts as an initial docking site for Hsp90 associated precursor proteins.	toc64	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
16634649-2	2006	The ansamycins, geldanamycin (GA) and its derivative, 17-allylaminogeldanamycin (17-AAG), inhibit Hsp90.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
16634649-2	2006	The ansamycins, geldanamycin (GA) and its derivative, 17-allylaminogeldanamycin (17-AAG), inhibit Hsp90.	geldanamycin	30-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
16634649-2	2006	The ansamycins, geldanamycin (GA) and its derivative, 17-allylaminogeldanamycin (17-AAG), inhibit Hsp90.	tanespimycin	54-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
16634649-4	2006	GA and 17-AAG potently inhibit tumor cell proliferation and survival but have been reported to bind weakly to Hsp90 in vitro.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
16634649-5	2006	Recent studies have suggested that the in vitro potency of ansamycins against Hsp90 may be enhanced in the presence of cochaperones.	Lactams, Macrocyclic	59-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
16634649-5	2006	Recent studies have suggested that the in vitro potency of ansamycins against Hsp90 may be enhanced in the presence of cochaperones.	cochaperones	119-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
16480864-0	2006	4-Amino derivatives of the Hsp90 inhibitor CCT018159.	CCT018159	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16804017-6	2006	Furthermore, the preincubation of human keratinocytes at 43 degrees C for 1 h, followed by 24-h treatment with 3 microM curcumin, led to an increase in heat-shock protein (hsp70 and hsp90) levels by 24% and 19%, respectively, and the effect was sustained at concentrations up to 10 microM.	Curcumin	120-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
16827123-3	2006	We have previously reported that geldanamycin (GA), an Hsp90 inhibitor, decreases Raf-1 and Akt protein expressions and induces apoptosis in neuroblastoma cells.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
16827123-3	2006	We have previously reported that geldanamycin (GA), an Hsp90 inhibitor, decreases Raf-1 and Akt protein expressions and induces apoptosis in neuroblastoma cells.	geldanamycin	47-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
16464590-1	2006	Radicicol and geldanamycin are potent inhibitors of the Hsp90 protein folding machinery, which is an emerging target for the development of cancer chemotherapeutics.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
16464590-1	2006	Radicicol and geldanamycin are potent inhibitors of the Hsp90 protein folding machinery, which is an emerging target for the development of cancer chemotherapeutics.	geldanamycin	14-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
16480864-1	2006	Novel piperazinyl, morpholino and piperidyl derivatives of the pyrazole-based Hsp90 inhibitor CCT018159 are described.	pyrazole	63-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
16213582-2	2006	The benzoquinone ansamycin geldanamycin has been shown to bind to Hsp90 and to specifically inhibit this chaperone"s function, resulting in client protein destabilization.	geldanamycin	27-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
16691504-9	2006	A 1.4-1.6-fold increase in HSP-70 and HSP-90 expression was also observed in 8Br-cAMP treated cells.	8-Bromo Cyclic Adenosine Monophosphate	77-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-44
16385472-3	2006	The Hsp90-mediated protein folding process is dependent upon ATP, and when inhibitors of ATP are present, the Hsp90 machinery is unable to fold client proteins into their biologically active form, which results in the degradation of protein substrates via the ubiquitin-proteasome pathway.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16213582-0	2006	The Hsp90 inhibitor 17-allylamide-17-demethoxygeldanamycin induces apoptosis and differentiation of Kasumi-1 harboring the Asn822Lys KIT mutation and down-regulates KIT protein level.	17-allylamide-17-demethoxygeldanamycin	20-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16213582-2	2006	The benzoquinone ansamycin geldanamycin has been shown to bind to Hsp90 and to specifically inhibit this chaperone"s function, resulting in client protein destabilization.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
16550610-4	2006	Because the heat shock protein (HSP) is involved in the conformational maturation of a number of signaling proteins critical to the proliferation of malignant glioma cells, we hypothesized that the HSP90 inhibitor 17-AAG would potentiate ZD 1839-mediated glioma cytotoxicity by decreasing the activation status of EGF receptor, as well as down regulating the levels of other relevant signaling effectors.	Gefitinib	238-245	heat shock protein 90 alpha family class A member 1	Homo sapiens	198-203
16385472-3	2006	The Hsp90-mediated protein folding process is dependent upon ATP, and when inhibitors of ATP are present, the Hsp90 machinery is unable to fold client proteins into their biologically active form, which results in the degradation of protein substrates via the ubiquitin-proteasome pathway.	Adenosine Triphosphate	61-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
16385472-3	2006	The Hsp90-mediated protein folding process is dependent upon ATP, and when inhibitors of ATP are present, the Hsp90 machinery is unable to fold client proteins into their biologically active form, which results in the degradation of protein substrates via the ubiquitin-proteasome pathway.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16385472-3	2006	The Hsp90-mediated protein folding process is dependent upon ATP, and when inhibitors of ATP are present, the Hsp90 machinery is unable to fold client proteins into their biologically active form, which results in the degradation of protein substrates via the ubiquitin-proteasome pathway.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	110-115
16731752-2	2006	The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) depletes some proteins involved in PI3K/AKT signaling, e.g., ERBB2, epidermal growth factor receptor (EGFR), and phosphorylated AKT (p-AKT).	tanespimycin	60-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16731752-0	2006	Potentiation of paclitaxel activity by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin in human ovarian carcinoma cell lines with high levels of activated AKT.	Paclitaxel	16-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
16731752-9	2006	17-AAG induced a decrease in HSP90 client proteins (e.g., C-RAF, ERBB2, and p-AKT) or in downstream markers of their activity (e.g., phosphorylated extracellular signal-regulated kinase or p-AKT) in SKOV-3, IGROV-1, and CH1 cells at IC(50) concentrations.	tanespimycin	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
16731752-0	2006	Potentiation of paclitaxel activity by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin in human ovarian carcinoma cell lines with high levels of activated AKT.	tanespimycin	59-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
16384610-3	2006	Geldanamycin and its derivative 17-AAG are potential antitumor agents capable of downregulating client proteins of Hsp90, including ErbB2.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
16731752-2	2006	The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) depletes some proteins involved in PI3K/AKT signaling, e.g., ERBB2, epidermal growth factor receptor (EGFR), and phosphorylated AKT (p-AKT).	tanespimycin	20-58	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16731758-1	2006	The selective heat shock protein 90 (HSP90) inhibitor 17-allyamino-17-demethoxygeldanamycin (17-AAG) is currently in phase I/II clinical studies at numerous institutions.	17-allyamino-17-demethoxygeldanamycin	54-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-35
16731758-1	2006	The selective heat shock protein 90 (HSP90) inhibitor 17-allyamino-17-demethoxygeldanamycin (17-AAG) is currently in phase I/II clinical studies at numerous institutions.	17-allyamino-17-demethoxygeldanamycin	54-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
16611982-0	2006	Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases.	Glycine	25-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
16611982-2	2006	Phage display technology and liquid chromatography-tandem mass spectrometry (which identifies a total of 33 proteins) consistently identify a unique sequence, GXFG, as a Cdc37-interacting motif that occurs in the canonical glycine-rich loop (GXGXXG) of protein kinases, regardless of their dependence on Hsp90 or Cdc37.	Glycine	223-230	heat shock protein 90 alpha family class A member 1	Homo sapiens	304-309
16495214-4	2006	We found that low concentrations of the specific Hsp90 inhibitors, geldanamycin and radicicol, completely blocked the translocation of FGF-1 and FGF-2 to the cytosol and the nucleus.	geldanamycin	67-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
16495214-4	2006	We found that low concentrations of the specific Hsp90 inhibitors, geldanamycin and radicicol, completely blocked the translocation of FGF-1 and FGF-2 to the cytosol and the nucleus.	monorden	84-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
16552710-1	2006	The heat shock protein (HSP) Hsp90 is known to chaperone cytosolic peptides for MHC class I (MHCI)-restricted antigen presentation to T lymphocytes.	Peptides	67-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	29-34
16552710-3	2006	Treatment of mouse antigen-presenting cells (APC) with the pharmacological Hsp90 inhibitor, geldanamycin, inhibited MHCII-mediated presentation of endocytosed and cytosolic proteins as well as synthetic peptides to specific T cells.	geldanamycin	92-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
16552710-3	2006	Treatment of mouse antigen-presenting cells (APC) with the pharmacological Hsp90 inhibitor, geldanamycin, inhibited MHCII-mediated presentation of endocytosed and cytosolic proteins as well as synthetic peptides to specific T cells.	Peptides	203-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
16415178-7	2006	Low concentrations of laulimalide substantially blocked subsequent VEGFR-2 downstream events, as did docetaxel, including the phosphorylation of the Tyr397 and Tyr407 residues of focal adhesion kinase (FAK), the association of VEGFR-2 with FAK and Hsp90, and the Tyr31 phosphorylation of paxillin.	laulimalide	22-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	248-253
16464956-3	2006	The HSP90 inhibitors reduced levels of tau phosphorylated at proline-directed Ser/Thr sites (pS202/T205, pS396/S404) and conformationally altered (MC-1) tau species, an epitope that is immeasurable by standard Western blot techniques.	Proline	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16464956-3	2006	The HSP90 inhibitors reduced levels of tau phosphorylated at proline-directed Ser/Thr sites (pS202/T205, pS396/S404) and conformationally altered (MC-1) tau species, an epitope that is immeasurable by standard Western blot techniques.	Serine	78-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16464956-3	2006	The HSP90 inhibitors reduced levels of tau phosphorylated at proline-directed Ser/Thr sites (pS202/T205, pS396/S404) and conformationally altered (MC-1) tau species, an epitope that is immeasurable by standard Western blot techniques.	Threonine	82-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16508638-7	2006	Treatment with the hsp-90 inhibitor novobiocin dissociated hsp90 and hTERT as revealed by immunoprecipitation and immunoblot analysis and reduced telomerase activity.	Novobiocin	36-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-25
16482209-0	2006	Targeting Hsp90 by 17-AAG in leukemia cells: mechanisms for synergistic and antagonistic drug combinations with arsenic trioxide and Ara-C.	Arsenic Trioxide	112-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
16482209-0	2006	Targeting Hsp90 by 17-AAG in leukemia cells: mechanisms for synergistic and antagonistic drug combinations with arsenic trioxide and Ara-C.	Cytarabine	133-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
16508638-7	2006	Treatment with the hsp-90 inhibitor novobiocin dissociated hsp90 and hTERT as revealed by immunoprecipitation and immunoblot analysis and reduced telomerase activity.	Novobiocin	36-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-64
16554484-0	2006	An analog of a dipeptide-like structure of FK506 increases glial cell line-derived neurotrophic factor expression through cAMP response element-binding protein activated by heat shock protein 90/Akt signaling pathway.	Dipeptides	15-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-194
16554484-6	2006	Leu-Ile stimulated Akt phosphorylation, which was attenuated significantly by heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA).	H-LEU-ILE-OH	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
16554484-0	2006	An analog of a dipeptide-like structure of FK506 increases glial cell line-derived neurotrophic factor expression through cAMP response element-binding protein activated by heat shock protein 90/Akt signaling pathway.	Tacrolimus	43-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	173-194
16554484-6	2006	Leu-Ile stimulated Akt phosphorylation, which was attenuated significantly by heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA).	H-LEU-ILE-OH	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16554484-6	2006	Leu-Ile stimulated Akt phosphorylation, which was attenuated significantly by heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA).	geldanamycin	118-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
16421106-0	2006	Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization.	Novobiocin	64-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
16554484-6	2006	Leu-Ile stimulated Akt phosphorylation, which was attenuated significantly by heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA).	geldanamycin	118-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16554484-6	2006	Leu-Ile stimulated Akt phosphorylation, which was attenuated significantly by heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA).	geldanamycin	132-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99
16554484-6	2006	Leu-Ile stimulated Akt phosphorylation, which was attenuated significantly by heat shock protein 90 (Hsp90) inhibitor geldanamycin (GA).	geldanamycin	132-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16554484-8	2006	Leu-Ile elicited an increase in cAMP response element binding protein (CREB) phosphorylation, which was inhibited by GA, indicating that CREB is a downstream target of Hsp90/Akt signaling.	H-LEU-ILE-OH	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
16554484-12	2006	In conclusion, Leu-Ile activates Hsp90/Akt/CREB signaling, which contributes to the upregulation of GDNF expression.	H-LEU-ILE-OH	15-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
16421106-2	2006	An alpha-helical region, upstream of the MEEVD peptide, helps form the dimerization interface and includes a hydrophobic microdomain that contributes to the Hsp90 interaction with the immunophilin cochaperones and corresponds to the binding site for novobiocin, a coumarin-related Hsp90 inhibitor.	coumarin	264-272	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
16421106-4	2006	Prior incubation of the Hsp90 fragment with novobiocin led to a direct blockade of immunophilin cochaperone binding.	Novobiocin	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
16421106-4	2006	Prior incubation of the Hsp90 fragment with novobiocin led to a direct blockade of immunophilin cochaperone binding.	cochaperone	96-107	heat shock protein 90 alpha family class A member 1	Homo sapiens	24-29
16421106-7	2006	Novobiocin also precluded the interaction of full-length Hsp90 with the p50(cdc37) cochaperone, which targets the N-terminal nucleotide-binding domain, and is prevalent in Hsp90 complexes with protein kinase substrates.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
16421106-7	2006	Novobiocin also precluded the interaction of full-length Hsp90 with the p50(cdc37) cochaperone, which targets the N-terminal nucleotide-binding domain, and is prevalent in Hsp90 complexes with protein kinase substrates.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
16421106-8	2006	Novobiocin therefore acts locally and allosterically to induce conformational changes within multiple regions of the Hsp90 protein.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
16421106-9	2006	We provide evidence that coumermycin A1, a coumarin structurally related to novobiocin, interferes with dimerization of the Hsp90 C-terminal domain.	coumermycin	25-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
16421106-0	2006	Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization.	coumarin	124-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
16421106-9	2006	We provide evidence that coumermycin A1, a coumarin structurally related to novobiocin, interferes with dimerization of the Hsp90 C-terminal domain.	coumarin	43-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
16421106-9	2006	We provide evidence that coumermycin A1, a coumarin structurally related to novobiocin, interferes with dimerization of the Hsp90 C-terminal domain.	Novobiocin	76-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
16421106-0	2006	Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization.	coumarin	124-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
16421106-10	2006	Coumarin-based inhibitors then may antagonize Hsp90 function by inducing a conformation favoring separation of the C-terminal domains and release of substrate.	coumarin	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
16421106-2	2006	An alpha-helical region, upstream of the MEEVD peptide, helps form the dimerization interface and includes a hydrophobic microdomain that contributes to the Hsp90 interaction with the immunophilin cochaperones and corresponds to the binding site for novobiocin, a coumarin-related Hsp90 inhibitor.	Novobiocin	250-260	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
16421106-2	2006	An alpha-helical region, upstream of the MEEVD peptide, helps form the dimerization interface and includes a hydrophobic microdomain that contributes to the Hsp90 interaction with the immunophilin cochaperones and corresponds to the binding site for novobiocin, a coumarin-related Hsp90 inhibitor.	Novobiocin	250-260	heat shock protein 90 alpha family class A member 1	Homo sapiens	281-286
16478993-5	2006	GCUNC-45 binds to the ATP-binding domain of hsp90 to prevent the activation of its ATPase activity by the cochaperone Aha1.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
16551874-11	2006	Because heat shock protein 90 (Hsp90) substrates are depleted by ritonavir, ritonavir effects on Hsp90 were tested.	Ritonavir	76-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
16551874-12	2006	Ritonavir binds Hsp90 (K(D), 7.8 micromol/L) and partially inhibits its chaperone function.	Ritonavir	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	16-21
16551874-13	2006	Ritonavir blocks association of Hsp90 with Akt and, with sustained exposure, notably depletes Hsp90.	Ritonavir	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
16551874-13	2006	Ritonavir blocks association of Hsp90 with Akt and, with sustained exposure, notably depletes Hsp90.	Ritonavir	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
16551874-14	2006	Stably expressed Hsp90alpha short hairpin RNA also depletes Hsp90, inhibiting proliferation and sensitizing breast cancer cells to low ritonavir concentrations.	Ritonavir	135-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-27
16551874-14	2006	Stably expressed Hsp90alpha short hairpin RNA also depletes Hsp90, inhibiting proliferation and sensitizing breast cancer cells to low ritonavir concentrations.	Ritonavir	135-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
16551874-15	2006	CONCLUSIONS: Ritonavir inhibits breast cancer growth in part by inhibiting Hsp90 substrates, including Akt.	Ritonavir	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
16551874-16	2006	Ritonavir may be of interest for breast cancer therapeutics and its efficacy may be increased by sustained exposure or Hsp90 RNA interference.	Ritonavir	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	119-124
16478993-7	2006	These findings reveal a new cochaperone binding site near the N terminus of hsp90, add insight on the role of FKBP52, and identify GCUNC-45 as a novel regulator of the PR signaling pathway.	cochaperone	28-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
16394098-7	2006	Alternatively, Hsp90-specific inhibitor geldanamycin (GA) dramatically reduces expression of IRF3-regulated interferon-stimulated genes and abolishes the cytoplasm-to-nucleus translocation and DNA binding activity of IRF3 in Sendai virus-infected cells.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
16394098-7	2006	Alternatively, Hsp90-specific inhibitor geldanamycin (GA) dramatically reduces expression of IRF3-regulated interferon-stimulated genes and abolishes the cytoplasm-to-nucleus translocation and DNA binding activity of IRF3 in Sendai virus-infected cells.	geldanamycin	54-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
16403413-2	2006	This function of Hsp90 has been proposed to be governed by conformational changes driven by ATP binding and hydrolysis.	Adenosine Triphosphate	92-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
16546966-0	2006	Benzoquinone ansamycin heat shock protein 90 inhibitors modulate multiple functions required for tumor angiogenesis.	benzoquinone ansamycin	0-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-44
16546966-3	2006	The benzoquinone ansamycin Hsp90 inhibitors geldanamycin and/or its derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin inhibited production of vascular endothelial growth factor (VEGF)-A by tumor cells and blocked proliferative responses of human endothelial cells at nanomolar concentrations.	benzoquinone ansamycin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16546966-3	2006	The benzoquinone ansamycin Hsp90 inhibitors geldanamycin and/or its derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin inhibited production of vascular endothelial growth factor (VEGF)-A by tumor cells and blocked proliferative responses of human endothelial cells at nanomolar concentrations.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16546966-3	2006	The benzoquinone ansamycin Hsp90 inhibitors geldanamycin and/or its derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin inhibited production of vascular endothelial growth factor (VEGF)-A by tumor cells and blocked proliferative responses of human endothelial cells at nanomolar concentrations.	tanespimycin	80-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16546966-3	2006	The benzoquinone ansamycin Hsp90 inhibitors geldanamycin and/or its derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin inhibited production of vascular endothelial growth factor (VEGF)-A by tumor cells and blocked proliferative responses of human endothelial cells at nanomolar concentrations.	dimethylaminoethylamino)	136-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16546966-3	2006	The benzoquinone ansamycin Hsp90 inhibitors geldanamycin and/or its derivatives 17-allylamino-17-demethoxygeldanamycin (17-AAG) and 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin inhibited production of vascular endothelial growth factor (VEGF)-A by tumor cells and blocked proliferative responses of human endothelial cells at nanomolar concentrations.	17-demethoxygeldanamycin	94-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16403413-5	2006	We demonstrate that human p23 interacts with Hsp90 in both the absence and presence of nucleotide with a higher affinity in the presence of the ATP analogue AMP-PNP.	Adenosine Triphosphate	144-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16403413-5	2006	We demonstrate that human p23 interacts with Hsp90 in both the absence and presence of nucleotide with a higher affinity in the presence of the ATP analogue AMP-PNP.	Adenylyl Imidodiphosphate	157-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16403413-9	2006	Complex formation between Hsp90 and p23 increased the apparent affinity of Hsp90 for AMP-PNP and completely inhibited the ATPase activity.	Adenosine Monophosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
16403413-9	2006	Complex formation between Hsp90 and p23 increased the apparent affinity of Hsp90 for AMP-PNP and completely inhibited the ATPase activity.	Adenosine Monophosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
16403413-10	2006	We propose a model where the role of p23 is to lock individual subunits of Hsp90 in an ATP-dependent conformational state that has a high affinity for client proteins.	Adenosine Triphosphate	87-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	75-80
16210473-10	2006	Similar results were obtained with an inhibitor of HSP90 heterocomplex formation, geldanmycin.	geldanmycin	82-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-56
16234364-1	2006	We show that multiple myeloma (MM), the second most commonly diagnosed hematologic malignancy, is responsive to hsp90 inhibitors in vitro and in a clinically relevant orthotopic in vivo model, even though this disease does not depend on HER2/neu, bcr/abl, androgen or estrogen receptors, or other hsp90 chaperoning clients which are hallmarks of tumor types traditionally viewed as attractive clinical settings for use of hsp90 inhibitors, such as the geldanamycin analog 17-AAG.	geldanamycin	452-464	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
16234364-1	2006	We show that multiple myeloma (MM), the second most commonly diagnosed hematologic malignancy, is responsive to hsp90 inhibitors in vitro and in a clinically relevant orthotopic in vivo model, even though this disease does not depend on HER2/neu, bcr/abl, androgen or estrogen receptors, or other hsp90 chaperoning clients which are hallmarks of tumor types traditionally viewed as attractive clinical settings for use of hsp90 inhibitors, such as the geldanamycin analog 17-AAG.	tanespimycin	472-478	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
16234364-3	2006	These pleiotropic proapoptotic effects allow hsp90 inhibitors to abrogate bone marrow stromal cell-derived protection on MM tumor cells, and sensitize them to other anticancer agents, including cytotoxic chemotherapy and the proteasome inhibitor bortezomib.	Bortezomib	246-256	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16443786-6	2006	Finally, incubation of BAECs with clinically relevant concentrations of metformin dramatically attenuated high-glucose (30 mmol/l)-induced reduction in the association of hsp90 with eNOS, which resulted in increased NO bioactivity with a reduction in overexpression of adhesion molecules and endothelial apoptosis caused by high-glucose exposure.	Metformin	72-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
16452239-10	2006	This compound, which we called emunin, strongly sensitized myeloma cells to proteasome and Hsp90 inhibitors and prostate carcinoma cells to proteasome inhibitors.	emunin	31-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
16429323-5	2006	Many of the proteins phosphorylated by and/or associated with G-CK belong to the category of chaperonines, including HSP90, GRP-94 and -78, and various isoforms of protein disulfide isomerases, suggesting a global role of this kinase in the modulation of protein folding.	chaperonines	93-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-122
16377176-6	2006	For example, a stable peptide inhibitor of the Hsp90 ATP-binding pocket killed a wide range of tumors in vitro and in vivo, and a peptide inhibitor of the BCL6 oncoprotein was active in B-cell lymphomas; both peptides functioned without toxicity to normal tissues.	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
16443786-3	2006	Exposure of cultured bovine aortic endothelial cells (BAECs) to clinically relevant concentrations of metformin (50-500 micromol/l) dose-dependently increased serine-1179 (Ser1179) phosphorylation (equal to human Ser1179) of endothelial nitric oxide (NO) synthase (eNOS) as well as its association with heat shock protein (hsp)-90, resulting in increased activation of eNOS and NO bioactivity (cyclic GMP).	Metformin	102-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	303-330
16443786-3	2006	Exposure of cultured bovine aortic endothelial cells (BAECs) to clinically relevant concentrations of metformin (50-500 micromol/l) dose-dependently increased serine-1179 (Ser1179) phosphorylation (equal to human Ser1179) of endothelial nitric oxide (NO) synthase (eNOS) as well as its association with heat shock protein (hsp)-90, resulting in increased activation of eNOS and NO bioactivity (cyclic GMP).	Serine	159-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	303-330
16443786-6	2006	Finally, incubation of BAECs with clinically relevant concentrations of metformin dramatically attenuated high-glucose (30 mmol/l)-induced reduction in the association of hsp90 with eNOS, which resulted in increased NO bioactivity with a reduction in overexpression of adhesion molecules and endothelial apoptosis caused by high-glucose exposure.	Glucose	111-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
16443786-6	2006	Finally, incubation of BAECs with clinically relevant concentrations of metformin dramatically attenuated high-glucose (30 mmol/l)-induced reduction in the association of hsp90 with eNOS, which resulted in increased NO bioactivity with a reduction in overexpression of adhesion molecules and endothelial apoptosis caused by high-glucose exposure.	Glucose	329-336	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
16443786-7	2006	Taken together, our results indicate that metformin might improve vascular endothelial functions in diabetes by increasing AMPK-dependent, hsp90-mediated eNOS activation.	Metformin	42-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
16428504-3	2006	The objective of this study was to determine the role of HSP90 in promoting growth and survival of Hodgkin"s lymphoma and to determine the molecular consequences of inhibiting HSP90 function by the small-molecule 17-allylamino-17-demethoxy-geldanamycin (17-AAG) in Hodgkin"s lymphoma.	tanespimycin	254-260	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
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
16289154-2	2006	It binds and stabilizes the ATP-bound dimeric form of Hsp90.	Adenosine Triphosphate	28-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
16289154-3	2006	Since Hsp90 binds protein substrates in the ATP conformation, p23 has been proposed to stabilize Hsp90-substrate complexes.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	6-11
16289154-3	2006	Since Hsp90 binds protein substrates in the ATP conformation, p23 has been proposed to stabilize Hsp90-substrate complexes.	Adenosine Triphosphate	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-102
16289154-8	2006	When the Hsp90 interaction is disrupted either with the Hsp90 inhibitor geldanamycin or by introduction of point mutations into p23, the mobility of p23 is greatly accelerated.	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	9-14
16289154-8	2006	When the Hsp90 interaction is disrupted either with the Hsp90 inhibitor geldanamycin or by introduction of point mutations into p23, the mobility of p23 is greatly accelerated.	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
16424045-3	2006	In this study, we showed that the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) was synergistic with TNF to induce apoptotic cell death in a panel of lung tumor-derived cell lines.	tanespimycin	50-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
16424045-3	2006	In this study, we showed that the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) was synergistic with TNF to induce apoptotic cell death in a panel of lung tumor-derived cell lines.	tanespimycin	90-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	34-39
16428504-9	2006	Inhibition of HSP90 function by 17-AAG showed a time- and dose-dependent growth inhibition of Hodgkin"s lymphoma cell lines.	tanespimycin	32-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16392823-3	2006	The PU-class, a purine-scaffold Hsp90 inhibitor series, has been reported to be potent and selective against Hsp90 both in vitro and in vivo models of cancer.	purine	16-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
16278218-0	2006	Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding.	Serine	62-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
16278218-6	2006	A potential mechanism for MK2-induced HSF1 inactivation is suggested by the findings that phosphorylation of serine 121 enhances HSF1 binding to HSP90, a major repressor of HSF1.	Serine	109-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
16049054-6	2006	Inhibition of Hsp90 by two specific inhibitors, geldanamycin or radicicol, did not affect total amounts of ClC-2 but did reduce plasma membrane channel abundance.	geldanamycin	48-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16278218-7	2006	Dephosphorylation of serine 121 in cells exposed to non-steroidal anti-inflammatory drugs leads to HSP90 dissociation from HSF1, which then forms active DNA binding trimers.	Serine	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	99-104
16371460-4	2006	Exposure of melanoma cells and tumors to the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in the degradation of mutant B-Raf, inhibition of mitogen-activated protein kinase activation and cell proliferation, induction of apoptosis, and antitumor activity.	tanespimycin	61-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16860662-3	2006	The HSP90-based chaperone machine is driven by the hydrolysis of ATP and ADP/ATP nucleotide exchange.	Adenosine Triphosphate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16860662-3	2006	The HSP90-based chaperone machine is driven by the hydrolysis of ATP and ADP/ATP nucleotide exchange.	Adenosine Diphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16860662-3	2006	The HSP90-based chaperone machine is driven by the hydrolysis of ATP and ADP/ATP nucleotide exchange.	Adenosine Triphosphate	77-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16860662-5	2006	The first-in-class HSP90 inhibitor in clinical trials is the geldanamycin analog, 17-allylamino, 17-demethoxygeldanamycin (17-AAG).	geldanamycin	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
16860662-5	2006	The first-in-class HSP90 inhibitor in clinical trials is the geldanamycin analog, 17-allylamino, 17-demethoxygeldanamycin (17-AAG).	17-allylamino	82-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
16860662-5	2006	The first-in-class HSP90 inhibitor in clinical trials is the geldanamycin analog, 17-allylamino, 17-demethoxygeldanamycin (17-AAG).	17-demethoxygeldanamycin	97-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
16049054-6	2006	Inhibition of Hsp90 by two specific inhibitors, geldanamycin or radicicol, did not affect total amounts of ClC-2 but did reduce plasma membrane channel abundance.	monorden	64-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16842150-6	2006	Several non-protein kinase purine utilizing proteins are established drug targets such as HMG CoA reductase, dihydrofolate reductase, phosphodiesterase and HSP90.	purine	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	156-161
16842153-6	2006	Identification of benzoquinone ansamycins as the first Hsp90 inhibitors allowed investigators to determine the biologic effects, at first in vitro and then in vivo, of pharmacologic inhibition of Hsp90.	benzoquinone ansamycins	18-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
16842153-6	2006	Identification of benzoquinone ansamycins as the first Hsp90 inhibitors allowed investigators to determine the biologic effects, at first in vitro and then in vivo, of pharmacologic inhibition of Hsp90.	benzoquinone ansamycins	18-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	196-201
16842153-7	2006	These studies rapidly enhanced our understanding of Hsp90 function and led to the identification of radicicol as a structurally distinct Hsp90 inhibitor.	monorden	100-109	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
16842153-8	2006	Additional target-based screening uncovered novobiocin as a third structurally distinct small molecule with Hsp90 inhibitory properties.	Novobiocin	44-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	108-113
16842154-0	2006	Geldanamycin, radicicol, and chimeric inhibitors of the Hsp90 N-terminal ATP binding site.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
16842154-0	2006	Geldanamycin, radicicol, and chimeric inhibitors of the Hsp90 N-terminal ATP binding site.	Adenosine Triphosphate	73-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
16842154-2	2006	Since Whitesell and Neckers" original discovery that geldanamycin does not directly inhibit v-Src, but instead manifests its biological activity through inhibition of the Hsp90 molecular chaperone, additional natural products and natural product derivatives have been identified and developed to inhibit the Hsp90 protein folding machinery.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	171-176
16842154-2	2006	Since Whitesell and Neckers" original discovery that geldanamycin does not directly inhibit v-Src, but instead manifests its biological activity through inhibition of the Hsp90 molecular chaperone, additional natural products and natural product derivatives have been identified and developed to inhibit the Hsp90 protein folding machinery.	geldanamycin	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	308-313
16842154-4	2006	Recent work has produced improved radicicol analogues that show promising Hsp90 inhibitory activity in vitro.	monorden	34-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
16842155-0	2006	Discovery and development of purine-scaffold Hsp90 inhibitors.	purine	29-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16842155-4	2006	Two natural product derivatives, 17-allylamino-17-desmethoxy-geldanamycin (17AAG) and 17-dimethylaminoethylamino-17-desmethoxy-geldanamycin (17DMAG) have further entered clinical trials, proving that Hsp90 may be modulated pharmacologically without causing target related toxicities in humans.	tanespimycin	75-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
16842155-4	2006	Two natural product derivatives, 17-allylamino-17-desmethoxy-geldanamycin (17AAG) and 17-dimethylaminoethylamino-17-desmethoxy-geldanamycin (17DMAG) have further entered clinical trials, proving that Hsp90 may be modulated pharmacologically without causing target related toxicities in humans.	17DMAG	141-147	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
16842156-0	2006	Discovery and development of pyrazole-scaffold Hsp90 inhibitors.	pyrazole	29-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	47-52
16842156-1	2006	This review explains why the chaperone Hsp90 is an exciting protein target for the discovery of new drugs to treat cancer in the clinic, and summarises the properties of natural product derived inhibitors before relating the discovery and current state of development of synthetic pyrazole compounds.	pyrazole	281-289	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
16842156-3	2006	Hsp90 has an ATPase domain that is necessary for its Hsp chaperone function, and X-ray crystallography has shown that natural product inhibitors (geldanamycin, radicicol) of Hsp90 function bind to this domain.	geldanamycin	146-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16842156-3	2006	Hsp90 has an ATPase domain that is necessary for its Hsp chaperone function, and X-ray crystallography has shown that natural product inhibitors (geldanamycin, radicicol) of Hsp90 function bind to this domain.	geldanamycin	146-158	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
16842156-3	2006	Hsp90 has an ATPase domain that is necessary for its Hsp chaperone function, and X-ray crystallography has shown that natural product inhibitors (geldanamycin, radicicol) of Hsp90 function bind to this domain.	monorden	160-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16842156-3	2006	Hsp90 has an ATPase domain that is necessary for its Hsp chaperone function, and X-ray crystallography has shown that natural product inhibitors (geldanamycin, radicicol) of Hsp90 function bind to this domain.	monorden	160-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
16842157-6	2006	Based on these data, 17-AAG, an ansamycin antibiotic inhibitor of Hsp90, is being tested extensively in clinical trials in patients with advanced cancer.	Rifabutin	32-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
16610363-3	2006	One Hsp90 inhibitor, 17-AAG, has completed Phase I clinical trial and several Phase II trials of this agent are in progress.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16610357-2	2006	In an ATP-dependent process where hsp70 and hsp90 act as essential chaperones and Hop, hsp40, and p23 act as nonessential co-chaperones, the machinery assembles complexes between the ligand binding domain of the GR and hsp90.	Adenosine Triphosphate	6-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
16610357-2	2006	In an ATP-dependent process where hsp70 and hsp90 act as essential chaperones and Hop, hsp40, and p23 act as nonessential co-chaperones, the machinery assembles complexes between the ligand binding domain of the GR and hsp90.	Adenosine Triphosphate	6-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	219-224
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
16428328-0	2006	Suppression of the mTOR-raptor signaling pathway by the inhibitor of heat shock protein 90 geldanamycin.	geldanamycin	91-103	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-90
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
16610363-0	2006	Chaperoning oncogenes: Hsp90 as a target of geldanamycin.	geldanamycin	44-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
17065038-10	2006	Inhibition of Hsp90 by GA resulted in an increase in superoxide generation and a decrease in eNOs protein expression.	geldanamycin	23-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
17065038-10	2006	Inhibition of Hsp90 by GA resulted in an increase in superoxide generation and a decrease in eNOs protein expression.	Superoxides	53-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16428328-3	2006	Geldanamycin, a potent inhibitor of Hsp90, disrupted the in vivo binding of Hsp90 to raptor without affecting the association of raptor and mTOR, and suppressed the phosphorylation by mTOR of the downstream translational regulators p70 S6 kinase (S6K) and eukaryotic initiation factor 4E-binding protein 1 (4E-BP1).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
16428328-3	2006	Geldanamycin, a potent inhibitor of Hsp90, disrupted the in vivo binding of Hsp90 to raptor without affecting the association of raptor and mTOR, and suppressed the phosphorylation by mTOR of the downstream translational regulators p70 S6 kinase (S6K) and eukaryotic initiation factor 4E-binding protein 1 (4E-BP1).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
16428328-5	2006	These results indicate that Hsp90 is involved in the regulation of protein translation by facilitating the phosphorylation reaction of 4E-BP1 and S6K catalyzed by the mTOR/raptor complex through the association with raptor, and that the mTOR signaling pathway is a novel target of geldanamycin.	geldanamycin	281-293	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-33
16352662-2	2006	However, ErbB2 can be downregulated by the HSP-90 inhibitor geldanamycin, but the underlying cellular mechanisms are uncertain.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-49
16173045-1	2006	Both geldanamycin (GA) and radicicol (RA) are HSP90 binding agents that possess antitumour activities.	geldanamycin	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
16173045-1	2006	Both geldanamycin (GA) and radicicol (RA) are HSP90 binding agents that possess antitumour activities.	geldanamycin	19-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
16432176-0	2006	Sensitization of TRAIL-resistant cells by inhibition of heat shock protein 90 with low-dose geldanamycin.	geldanamycin	92-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-77
16173045-1	2006	Both geldanamycin (GA) and radicicol (RA) are HSP90 binding agents that possess antitumour activities.	monorden	27-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
16173045-1	2006	Both geldanamycin (GA) and radicicol (RA) are HSP90 binding agents that possess antitumour activities.	monorden	38-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
16328963-0	2006	HSP90 protects apoptotic cleavage of vimentin in geldanamycin-induced apoptosis.	geldanamycin	49-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16328963-2	2006	Geldanamycin, a specific antagonist of HSP90, binds directly to HSP90 and promotes proteolytic degradation of client proteins of HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
16328963-2	2006	Geldanamycin, a specific antagonist of HSP90, binds directly to HSP90 and promotes proteolytic degradation of client proteins of HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16328963-2	2006	Geldanamycin, a specific antagonist of HSP90, binds directly to HSP90 and promotes proteolytic degradation of client proteins of HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16328963-3	2006	The aim of the present study was to identify novel client proteins of HSP90 and to elucidate HSP90 function through inhibition of HSP90 binding to its client proteins, by using of geldanamycin.	geldanamycin	180-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
16328963-3	2006	The aim of the present study was to identify novel client proteins of HSP90 and to elucidate HSP90 function through inhibition of HSP90 binding to its client proteins, by using of geldanamycin.	geldanamycin	180-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
16328963-3	2006	The aim of the present study was to identify novel client proteins of HSP90 and to elucidate HSP90 function through inhibition of HSP90 binding to its client proteins, by using of geldanamycin.	geldanamycin	180-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
16328963-10	2006	Changes of HSP90 level by antisense treatment or transfection of HSP90-overexpressing vector affected geldanamycin-induced cleavage of vimentin.	geldanamycin	102-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	11-16
16328963-10	2006	Changes of HSP90 level by antisense treatment or transfection of HSP90-overexpressing vector affected geldanamycin-induced cleavage of vimentin.	geldanamycin	102-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
16328963-11	2006	These results suggest that HSP90 protects vimentin by physical interaction in the geldanamycin-induced apoptotic pathway.	geldanamycin	82-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
16432176-3	2006	However, some cancer cells are resistant to TRAIL, and at the dose required for inducing apoptosis, geldanamycin, a drug that inhibits HSP90 function, has shown adverse effects.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
16432176-5	2006	Treatment of LNCaP with 250 nmol/L geldanamycin inhibited HSP90 function but did not induce significant apoptosis.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
16432177-4	2006	We evaluated the effect of small interfering RNA (siRNA)-mediated inhibition of survivin on the proliferative potential of prostate cancer cells and their sensitivity to the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	190-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	174-179
16331994-3	2005	We show here that treatment of transformed human skin fibroblasts stably expressing CYP2E1 with the hsp90 inhibitor radicicol results in CYP2E1 degradation that is inhibited by the proteasome inhibitor lactacystin.	monorden	116-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
16920739-0	2006	Structural basis for topoisomerase VI inhibition by the anti-Hsp90 drug radicicol.	monorden	72-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
16920739-1	2006	Members of the GHL ATPase superfamily, including type II topoisomerases, Hsp90-class chaperones, and MutL, all share a common GHKL-type ATP-binding fold and act as nucleotide-controlled "molecular clamps".	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
16920739-2	2006	These enzymes" ATP-binding sites have proven to be rich drug targets, and certain inhibitors of type II topoisomerases and Hsp90 bind to this region and competitively inhibit these enzymes.	Adenosine Triphosphate	15-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
16920739-3	2006	Recently, it was found that radicicol, a drug known to block Hsp90 function, also inhibits the archaeal type IIB topoisomerase topo VI.	monorden	28-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
16920739-4	2006	Here, we use X-ray crystallography to show that despite low sequence identity ( approximately 10-12%) between topo VI and Hsp90, radicicol binds to the ATPase sites of these two enzymes in an equivalent manner.	monorden	129-138	heat shock protein 90 alpha family class A member 1	Homo sapiens	122-127
16432534-1	2006	Geldanamycin (GA), a benzoquinone ansamycin, is a naturally occurring inhibitor of heat shock protein (Hsp90), which regulates the transcription activity of hypoxia-inducible factor 1 (HIF-1alpha).	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
16432534-1	2006	Geldanamycin (GA), a benzoquinone ansamycin, is a naturally occurring inhibitor of heat shock protein (Hsp90), which regulates the transcription activity of hypoxia-inducible factor 1 (HIF-1alpha).	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
16432534-1	2006	Geldanamycin (GA), a benzoquinone ansamycin, is a naturally occurring inhibitor of heat shock protein (Hsp90), which regulates the transcription activity of hypoxia-inducible factor 1 (HIF-1alpha).	benzoquinone ansamycin	21-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
16331994-3	2005	We show here that treatment of transformed human skin fibroblasts stably expressing CYP2E1 with the hsp90 inhibitor radicicol results in CYP2E1 degradation that is inhibited by the proteasome inhibitor lactacystin.	lactacystin	202-213	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
16331994-8	2005	Our observations lead to a general model of how substrates, such as ethanol, can regulate the interaction of CYP2E1 with the chaperones hsp90 and hsp70 to profoundly alter enzyme turnover.	Ethanol	68-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	136-141
16321010-0	2005	Concise synthesis of pochonin A, an HSP90 inhibitor.	pochonin A	21-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
16321010-3	2005	This natural product is closely related to radicicol and was shown to be a 90 nM inhibitor of HSP90.	monorden	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
16202589-1	2005	Docking-based virtual screening identified 1-(2-phenol)-2-naphthol compounds as a new class of Hsp90 inhibitors of low to sub-micromolar potency.	1-(2-phenol)-2-naphthol compounds	43-76	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
16322212-0	2005	Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin.	tanespimycin	83-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
16322212-2	2005	The benzoquinone ansamysin 17-allylamino-17-demethoxygeldanamycin (17-AAG) is an anticancer drug that disrupts Hsp90 binding to its clients, causing their degradation through the ubiquitin-dependent proteasomal pathway.	benzoquinone ansamysin	4-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
16322212-2	2005	The benzoquinone ansamysin 17-allylamino-17-demethoxygeldanamycin (17-AAG) is an anticancer drug that disrupts Hsp90 binding to its clients, causing their degradation through the ubiquitin-dependent proteasomal pathway.	tanespimycin	27-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
16322259-3	2005	Surprisingly, low-dose (5-30 nmol/L) treatment of HeLa cells with three different HSP90 inhibitors (17-AAG, 17-DMAG, and geldanamycin) increased HIF-1-dependent reporter gene activity, whereas higher doses (1-3 micromol/L) resulted in a reduction of hypoxia-induced HIF-1 activity.	tanespimycin	100-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
16322259-3	2005	Surprisingly, low-dose (5-30 nmol/L) treatment of HeLa cells with three different HSP90 inhibitors (17-AAG, 17-DMAG, and geldanamycin) increased HIF-1-dependent reporter gene activity, whereas higher doses (1-3 micromol/L) resulted in a reduction of hypoxia-induced HIF-1 activity.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	108-115	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
16322259-3	2005	Surprisingly, low-dose (5-30 nmol/L) treatment of HeLa cells with three different HSP90 inhibitors (17-AAG, 17-DMAG, and geldanamycin) increased HIF-1-dependent reporter gene activity, whereas higher doses (1-3 micromol/L) resulted in a reduction of hypoxia-induced HIF-1 activity.	geldanamycin	121-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
16202589-3	2005	A high resolution crystal structure of the most potent compound reveals its binding mode in the ATP binding site of Hsp90, providing a rationale for the observed activity of the series and suggesting strategies for developing compounds with improved properties.	Adenosine Triphosphate	96-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
16213716-0	2005	3-(5-Chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides as inhibitors of the Hsp90 molecular chaperone.	3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides	0-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-83
16213716-1	2005	Information from X-ray crystal structures of Hsp90 inhibitors bound to the human Hsp90 molecular chaperone was used to assist in the design of 3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides as novel inhibitors of Hsp90.	3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides	143-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16213716-1	2005	Information from X-ray crystal structures of Hsp90 inhibitors bound to the human Hsp90 molecular chaperone was used to assist in the design of 3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides as novel inhibitors of Hsp90.	3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides	143-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
16213716-1	2005	Information from X-ray crystal structures of Hsp90 inhibitors bound to the human Hsp90 molecular chaperone was used to assist in the design of 3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides as novel inhibitors of Hsp90.	3-(5-chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides	143-199	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
16273226-0	2005	Presence of MLH1 protein aggravates the potential of the HSP90 inhibitor radicicol to sensitize tumor cells to cisplatin.	monorden	73-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
16228978-4	2005	Hsp90 inhibitors like geldanamycin therefore have the potential to target tumor-cell survival by at least two mechanisms, compromising the accumulation of HIF-1alpha and cell proliferation.	geldanamycin	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16307487-3	2005	17-allylamino-17-demethoxygeldanamycin (17-AAG), a selective inhibitor of Hsp90, is currently under clinical investigation in advanced malignancies in which Hsp90 client proteins are implicated.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
16307487-3	2005	17-allylamino-17-demethoxygeldanamycin (17-AAG), a selective inhibitor of Hsp90, is currently under clinical investigation in advanced malignancies in which Hsp90 client proteins are implicated.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
16273226-9	2005	But they may point to a possible functional relationship between HSP90 and MLH1, where HSP90 might affect the function of MLH1 in a way that this leads to the counter-regulation of cytotoxic pathways initiated by MMR as a consequence of the presence of DNA damage introduced by cisplatin.	Cisplatin	278-287	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
16273226-9	2005	But they may point to a possible functional relationship between HSP90 and MLH1, where HSP90 might affect the function of MLH1 in a way that this leads to the counter-regulation of cytotoxic pathways initiated by MMR as a consequence of the presence of DNA damage introduced by cisplatin.	Cisplatin	278-287	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
16273226-0	2005	Presence of MLH1 protein aggravates the potential of the HSP90 inhibitor radicicol to sensitize tumor cells to cisplatin.	Cisplatin	111-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
16273226-3	2005	Radicicol is a novel specific inhibitor for heat shock protein 90 (HSP90) and structurally unrelated to geldanamycin.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-65
16273226-3	2005	Radicicol is a novel specific inhibitor for heat shock protein 90 (HSP90) and structurally unrelated to geldanamycin.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
16037132-12	2005	Furthermore, the ERalpha-CHIP interaction was stimulated by the Hsp90 inhibitor geldanamycin (GA), resulting in enhanced ERalpha degradation; this GA effect was further augmented by CHIP overexpression but was abolished by CHIP depletion.	geldanamycin	80-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16037132-12	2005	Furthermore, the ERalpha-CHIP interaction was stimulated by the Hsp90 inhibitor geldanamycin (GA), resulting in enhanced ERalpha degradation; this GA effect was further augmented by CHIP overexpression but was abolished by CHIP depletion.	geldanamycin	94-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	64-69
16165354-1	2005	The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules.	7-carbamate	4-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
16620576-1	2005	OBJECTIVE: To explore the effect of 17-allylamide-17-demethoxygeldanamycin (17AAG), a heat shock protein 90 (HSP90) inhibitor, on the growth, differentiation and apoptosis of leukemic Kasumi-1 cells.	17-allylamide-17-demethoxygeldanamycin	36-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-107
16620576-1	2005	OBJECTIVE: To explore the effect of 17-allylamide-17-demethoxygeldanamycin (17AAG), a heat shock protein 90 (HSP90) inhibitor, on the growth, differentiation and apoptosis of leukemic Kasumi-1 cells.	17-allylamide-17-demethoxygeldanamycin	36-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
16620576-1	2005	OBJECTIVE: To explore the effect of 17-allylamide-17-demethoxygeldanamycin (17AAG), a heat shock protein 90 (HSP90) inhibitor, on the growth, differentiation and apoptosis of leukemic Kasumi-1 cells.	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-107
16620576-1	2005	OBJECTIVE: To explore the effect of 17-allylamide-17-demethoxygeldanamycin (17AAG), a heat shock protein 90 (HSP90) inhibitor, on the growth, differentiation and apoptosis of leukemic Kasumi-1 cells.	tanespimycin	76-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
16285732-3	2005	Treatment of K562 cells with the Hsp90 inhibitor, geldanamycin, caused a 75% reduction in Cdk2 levels and reduced the levels of its activating kinase, Cdk7, by more than 60%, suggesting that both of these kinases may be Hsp90 clients.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
16285732-3	2005	Treatment of K562 cells with the Hsp90 inhibitor, geldanamycin, caused a 75% reduction in Cdk2 levels and reduced the levels of its activating kinase, Cdk7, by more than 60%, suggesting that both of these kinases may be Hsp90 clients.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	220-225
16285732-4	2005	Using classical pull-down assays and the Hsp90 inhibitory agents geldanamycin and molybdate, Cdk2 is shown to be a genuine client of the Hsp90 chaperone complex.	geldanamycin	65-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
16285732-4	2005	Using classical pull-down assays and the Hsp90 inhibitory agents geldanamycin and molybdate, Cdk2 is shown to be a genuine client of the Hsp90 chaperone complex.	molybdate	82-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142
16285732-6	2005	Mutant constructs containing deletions of secondary structural elements from the N- and C-termini of Cdk2 were prepared and assayed for their ability to coadsorb Hsp90 and Cdc37 in a salt-stable high-affinity manner with and without the addition of molybdate.	Salts	183-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
16165354-1	2005	The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
16165354-1	2005	The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules.	17-(2-dimethylaminoethyl)amino-17-demethoxy	47-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
16165354-1	2005	The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	103-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
16165354-1	2005	The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules.	Hydrogen	177-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
16165354-1	2005	The 7-carbamate groups of geldanamycin and its 17-(2-dimethylaminoethyl)amino-17-demethoxy derivative (17-DMAG) bind the N-terminal domain of Hsp90 by establishing a network of hydrogen bonds which involve four buried water molecules.	Water	218-223	heat shock protein 90 alpha family class A member 1	Homo sapiens	142-147
16165354-4	2005	Modeling of Hsp90-ligand interactions suggested that the hydroxamate was not able to displace the buried water molecules, while bulkier substituents able to do so proved inactive.	hydroxamate	57-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	12-17
16340449-0	2005	Chronic ethanol exposure stimulates endothelial cell nitric oxide production through PI-3 kinase-and hsp90-dependent mechanisms.	Ethanol	8-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16288046-0	2005	Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin.	17-allylamino-demethoxy geldanamycin	129-165	heat shock protein 90 alpha family class A member 1	Homo sapiens	97-118
16288046-1	2005	17-Allylamino-demethoxy geldanamycin (17-AAG) inhibits the chaperone association of heat shock protein 90 (hsp90) with the heat shock factor-1 (HSF-1), which induces the mRNA and protein levels of hsp70.	17-allylamino-demethoxy geldanamycin	0-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-105
16288046-1	2005	17-Allylamino-demethoxy geldanamycin (17-AAG) inhibits the chaperone association of heat shock protein 90 (hsp90) with the heat shock factor-1 (HSF-1), which induces the mRNA and protein levels of hsp70.	17-allylamino-demethoxy geldanamycin	0-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
16340449-0	2005	Chronic ethanol exposure stimulates endothelial cell nitric oxide production through PI-3 kinase-and hsp90-dependent mechanisms.	Nitric Oxide	53-65	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
16340449-7	2005	EtOH stimulation also increased eNOS interaction with heat shock protein (hsp90), a molecular chaperone known to enhance eNOS activity.	Ethanol	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
16340449-8	2005	Geldanamycin, an hsp90 inhibitor, attenuated chronic EtOH-mediated increases in NO production.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
16340449-8	2005	Geldanamycin, an hsp90 inhibitor, attenuated chronic EtOH-mediated increases in NO production.	Ethanol	53-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
16340449-9	2005	CONCLUSIONS: These results indicate that chronic EtOH exposure increases endothelial NO production by increasing eNOS protein levels through PI3 K-dependent up regulation of eNOS gene transcription and by increasing interactions between eNOS and hsp90.	Ethanol	49-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	246-251
16211252-4	2005	Here, we show that brief exposure to methyl jasmonate (MeJA), but not to jasmonic acid, induces heat shock protein 72 (HSP72), but not HSP73 and HSP90, via heat shock factor I (HSF1) activation in C6 glioma cells without affecting cell viability.	methyl jasmonate	37-53	heat shock protein 90 alpha family class A member 1	Homo sapiens	145-150
16267026-15	2005	The ability of 17-AAG and 17-AAGH2 to inhibit purified yeast and human Hsp90 ATPase activity was examined.	17-aagh2	26-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
16267026-17	2005	Molecular modeling studies also showed that due to increased hydrogen bonding between the hydroquinone and the Hsp90 protein, 17-AAGH2 was bound more tightly to the ATP-binding site in both yeast and human Hsp90 models.	hydroquinone	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
16267026-17	2005	Molecular modeling studies also showed that due to increased hydrogen bonding between the hydroquinone and the Hsp90 protein, 17-AAGH2 was bound more tightly to the ATP-binding site in both yeast and human Hsp90 models.	Adenosine Triphosphate	165-168	heat shock protein 90 alpha family class A member 1	Homo sapiens	206-211
16087666-7	2005	hsp90 from HDAC6 knockdown cytosol has decreased ATP-binding affinity, and it does not assemble stable GR.hsp90 heterocomplexes when it is a component of a purified five-protein assembly system.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16324248-4	2005	The dose- and time-related effect of estradiol benzoate and ICI 182780 on the cell growth was measured by mononuclear cell direct cytotoxicity assay (methyl thiazolyl tetrazolium assay), and that on the expression of HSP70 and HSP90 in normal endometrial glandular epithelial cell in vitro was measured by immunohistochemical analysis and computerized image analysis system.	estradiol 3-benzoate	37-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	227-232
16324248-7	2005	Estradiol benzoate treatment resulted in a time- and dose-dependent increase of the expression of HSP90 and decrease of HSP70 in human endometrial glandular epithelial cell.	estradiol 3-benzoate	0-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-103
16324248-8	2005	The expression of HSP90 in 10(-9), 10(-8), 10(-7), 10(-6) mol/L estradiol benzoate for 24 hours were (64.8 +/- 10.7)%, (75.9 +/- 12.6)%, (80.4 +/- 8.2)%, (83.2 +/- 7.6)%, which were significantly higher than that of the control [(28.0 +/- 3.3)%, (29.0 +/- 5.6)%, (29.0 +/- 5.0)%, (30.0 +/- 6.4)%, P &lt; 0.05] and that of estradiol benzoate + ICI 182780 for 24 hours [(28.2 +/- 2.1)%, (29.7 +/- 3.2)%, (35.0 +/- 4.7)%, (34.7 +/- 6.5)%, P &lt; 0.05].	estradiol 3-benzoate	64-82	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
16324248-8	2005	The expression of HSP90 in 10(-9), 10(-8), 10(-7), 10(-6) mol/L estradiol benzoate for 24 hours were (64.8 +/- 10.7)%, (75.9 +/- 12.6)%, (80.4 +/- 8.2)%, (83.2 +/- 7.6)%, which were significantly higher than that of the control [(28.0 +/- 3.3)%, (29.0 +/- 5.6)%, (29.0 +/- 5.0)%, (30.0 +/- 6.4)%, P &lt; 0.05] and that of estradiol benzoate + ICI 182780 for 24 hours [(28.2 +/- 2.1)%, (29.7 +/- 3.2)%, (35.0 +/- 4.7)%, (34.7 +/- 6.5)%, P &lt; 0.05].	estradiol 3-benzoate	322-340	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
16324248-11	2005	CONCLUSIONS: The effects of estradiol benzoate on the cell growth and HSP90 expression are estrogen receptor-dependent and the expression of HSP90 may be beneficial to the cell growth.	estradiol 3-benzoate	28-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
16324248-11	2005	CONCLUSIONS: The effects of estradiol benzoate on the cell growth and HSP90 expression are estrogen receptor-dependent and the expression of HSP90 may be beneficial to the cell growth.	estradiol 3-benzoate	28-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
16118214-4	2005	When Hsp90alpha was inhibited by geldanamycin (GA, a specific inhibitor of the Hsp90 family) or by siRNA of Hsp90alpha (to block its activity or to knockdown protein levels), respectively, luciferase activity (driven by the 12(S)-lipoxygenase promoter) and both mRNA and protein levels of 12(S)-lipoxygenase were reduced significantly in cells.	geldanamycin	33-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-15
16118214-4	2005	When Hsp90alpha was inhibited by geldanamycin (GA, a specific inhibitor of the Hsp90 family) or by siRNA of Hsp90alpha (to block its activity or to knockdown protein levels), respectively, luciferase activity (driven by the 12(S)-lipoxygenase promoter) and both mRNA and protein levels of 12(S)-lipoxygenase were reduced significantly in cells.	geldanamycin	47-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-15
16129430-7	2005	Also, several HSPs (Hsp90, Hsc70, Hsp70, Hsp60, Hsp47, Hsp40, and Hsp27) were detected outside of the cells after the treatment with acrylamide, indicating that these HSPs are released from necrotically dead cells.	Acrylamide	133-143	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
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
16203796-0	2005	Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models.	17-allylamino	106-119	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
16203796-0	2005	Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models.	17-demethoxygeldanamycin	121-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
16203796-1	2005	PURPOSE: To establish the pharmacokinetic and pharmacodynamic profile of the heat shock protein 90 (HSP90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in ovarian cancer xenograft models.	17-allylamino	117-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-98
16203796-1	2005	PURPOSE: To establish the pharmacokinetic and pharmacodynamic profile of the heat shock protein 90 (HSP90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in ovarian cancer xenograft models.	17-allylamino	117-130	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
15972449-4	2005	Treatment with Hsp90 inhibitors such as 17-AAG and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) induced ZAP-70 degradation and apoptosis in CLL cells but not in T cells, and also impaired B-cell receptor signaling in leukemia cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	51-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
16203796-1	2005	PURPOSE: To establish the pharmacokinetic and pharmacodynamic profile of the heat shock protein 90 (HSP90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in ovarian cancer xenograft models.	17-demethoxygeldanamycin	132-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-98
15972449-4	2005	Treatment with Hsp90 inhibitors such as 17-AAG and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) induced ZAP-70 degradation and apoptosis in CLL cells but not in T cells, and also impaired B-cell receptor signaling in leukemia cells.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	104-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
16203796-1	2005	PURPOSE: To establish the pharmacokinetic and pharmacodynamic profile of the heat shock protein 90 (HSP90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in ovarian cancer xenograft models.	17-demethoxygeldanamycin	132-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
15972449-7	2005	Additionally, ZAP-70 expression in CLL cells confers markedly heightened sensitivity to 17-AAG or 17-DMAG, suggesting that these or other Hsp90 inhibitors could be valuable therapeutically in patients with aggressive CLL.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	98-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
16203796-1	2005	PURPOSE: To establish the pharmacokinetic and pharmacodynamic profile of the heat shock protein 90 (HSP90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in ovarian cancer xenograft models.	tanespimycin	158-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
16203796-11	2005	Pharmacodynamic biomarker changes consistent with HSP90 inhibition were shown in human PBLs exposed ex vivo to 17-AAG but not to selected cytotoxic drugs.	tanespimycin	111-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
16203796-1	2005	PURPOSE: To establish the pharmacokinetic and pharmacodynamic profile of the heat shock protein 90 (HSP90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in ovarian cancer xenograft models.	tanespimycin	158-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-98
16099423-3	2005	In this report, we analyzed the mechanisms of Chk1 regulation in U87MG glioblastoma cells using Geldanamycin (GA), which interferes with the function of Hsp90.	geldanamycin	96-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
16218955-3	2005	Treatment of cells with several benzoquinone ansamycin inhibitors of Hsp90 (geldanamycin, herbimycin A) activated a heat shock response in the absence of heat shock, as reported previously.	benzoquinone ansamycin	32-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
16218955-3	2005	Treatment of cells with several benzoquinone ansamycin inhibitors of Hsp90 (geldanamycin, herbimycin A) activated a heat shock response in the absence of heat shock, as reported previously.	geldanamycin	76-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
16218955-3	2005	Treatment of cells with several benzoquinone ansamycin inhibitors of Hsp90 (geldanamycin, herbimycin A) activated a heat shock response in the absence of heat shock, as reported previously.	herbimycin	90-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
16099423-3	2005	In this report, we analyzed the mechanisms of Chk1 regulation in U87MG glioblastoma cells using Geldanamycin (GA), which interferes with the function of Hsp90.	geldanamycin	110-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
16159253-0	2005	Hsp90 inhibitors identified from a library of novobiocin analogues.	Novobiocin	46-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16159253-1	2005	Novobiocin is a C-terminal inhibitor of the Hsp90 protein folding machinery, which is responsible for the conformational maturation of numerous proteins involved in cancer growth and survival.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
16159253-3	2005	In this study, a parallel library of 20 novobiocin derivatives was prepared and the biological activity of each evaluated by Western blot analysis of Hsp90 client proteins.	Novobiocin	40-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	150-155
15967517-9	2005	Immunoprecipitation with anti-HIF1alpha antibody co-precipitates HSP90 in an oxygen-dependent manner, more at high pO2 than at low pO2.	Oxygen	77-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
15967517-9	2005	Immunoprecipitation with anti-HIF1alpha antibody co-precipitates HSP90 in an oxygen-dependent manner, more at high pO2 than at low pO2.	PO-2	115-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
15967517-9	2005	Immunoprecipitation with anti-HIF1alpha antibody co-precipitates HSP90 in an oxygen-dependent manner, more at high pO2 than at low pO2.	PO-2	131-134	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
15967517-10	2005	Cadmium-treated samples also show high amounts of co-immunoprecipitated HSP90, independent of oxygen concentration.	Cadmium	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
16144943-1	2005	PURPOSE: We determined the effects of suberoylanilide hydroxamic acid (SAHA), a histone deacetylase inhibitor, on hsp90 and its client proteins Her-2, AKT, and c-Raf, as well as evaluated the cytotoxic effects of co-treatment of SAHA with trastuzumab or docetaxel in human breast cancer BT-474 and SKBR-3 cells containing amplification of Her-2.	Vorinostat	38-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
16145048-4	2005	The specific roles of the ubiquitin-mediated proteasome machinery, mitogen-activated protein kinase (MAPK) and Akt pathways, and heat shock protein 90 (Hsp90) in the SCH66336-mediated degradation of hypoxia-inducible factor 1alpha (HIF-1alpha) were assessed with ubiquitin inhibitors and adenoviral vectors that express constitutively active MAP kinase kinase (MEK)1, constitutively active Akt, or Hsp90.	lonafarnib	166-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-150
16145048-4	2005	The specific roles of the ubiquitin-mediated proteasome machinery, mitogen-activated protein kinase (MAPK) and Akt pathways, and heat shock protein 90 (Hsp90) in the SCH66336-mediated degradation of hypoxia-inducible factor 1alpha (HIF-1alpha) were assessed with ubiquitin inhibitors and adenoviral vectors that express constitutively active MAP kinase kinase (MEK)1, constitutively active Akt, or Hsp90.	lonafarnib	166-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	152-157
16145048-4	2005	The specific roles of the ubiquitin-mediated proteasome machinery, mitogen-activated protein kinase (MAPK) and Akt pathways, and heat shock protein 90 (Hsp90) in the SCH66336-mediated degradation of hypoxia-inducible factor 1alpha (HIF-1alpha) were assessed with ubiquitin inhibitors and adenoviral vectors that express constitutively active MAP kinase kinase (MEK)1, constitutively active Akt, or Hsp90.	lonafarnib	166-174	heat shock protein 90 alpha family class A member 1	Homo sapiens	398-403
16145048-7	2005	SCH66336 inhibited the interaction between HIF-1alpha and Hsp90.	lonafarnib	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
16145048-9	2005	CONCLUSIONS: SCH66336 appears to inhibit angiogenic activities of NSCLC and HNSCC cells by decreasing hypoxia- or IGF-stimulated HIF-1alpha expression and to inhibit VEGF production by inhibiting the interaction between HIF-1alpha and Hsp90, resulting in the proteasomal degradation of HIF-1alpha.	lonafarnib	13-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	235-240
16144943-1	2005	PURPOSE: We determined the effects of suberoylanilide hydroxamic acid (SAHA), a histone deacetylase inhibitor, on hsp90 and its client proteins Her-2, AKT, and c-Raf, as well as evaluated the cytotoxic effects of co-treatment of SAHA with trastuzumab or docetaxel in human breast cancer BT-474 and SKBR-3 cells containing amplification of Her-2.	Vorinostat	71-75	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
16144943-7	2005	SAHA treatment induced acetylation of hsp90.	Vorinostat	0-4	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
16170022-8	2005	LAQ824 induced Hsp90 acetylation in LNCaP cells, which resulted in inhibition of its ATP-binding activity, dissociation of Hsp90-androgen receptor complex, and proteasome-mediated degradation of androgen receptor.	LAQ824	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
16170022-8	2005	LAQ824 induced Hsp90 acetylation in LNCaP cells, which resulted in inhibition of its ATP-binding activity, dissociation of Hsp90-androgen receptor complex, and proteasome-mediated degradation of androgen receptor.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
16170022-5	2005	Although LAQ824 may exert its effect through multiple mechanisms, several lines of evidence suggest that inactivation of the heat shock protein-90 (Hsp90) molecular chaperone is involved in LAQ824-induced androgen receptor depletion.	LAQ824	9-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-146
16170022-5	2005	Although LAQ824 may exert its effect through multiple mechanisms, several lines of evidence suggest that inactivation of the heat shock protein-90 (Hsp90) molecular chaperone is involved in LAQ824-induced androgen receptor depletion.	LAQ824	9-15	heat shock protein 90 alpha family class A member 1	Homo sapiens	148-153
15951571-2	2005	GRP94, the endoplasmic reticulum paralog of Hsp90, is regulated by adenosine nucleotides that bind to its N-terminal regulatory domain.	adenosine nucleotides	67-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	44-49
16170022-7	2005	Another Hsp90 inhibitor, 17-allyamino-17-demethoxygeldanamycin (17-AAG), also induced androgen receptor diminution.	17-allyamino-17-demethoxygeldanamycin	25-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
16170022-7	2005	Another Hsp90 inhibitor, 17-allyamino-17-demethoxygeldanamycin (17-AAG), also induced androgen receptor diminution.	tanespimycin	64-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
16170022-8	2005	LAQ824 induced Hsp90 acetylation in LNCaP cells, which resulted in inhibition of its ATP-binding activity, dissociation of Hsp90-androgen receptor complex, and proteasome-mediated degradation of androgen receptor.	LAQ824	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
15993848-3	2005	We have shown that the Hsp90 inhibitor 17-AAG enhances the cytotoxicity of oxaliplatin in colon cancer cell lines through inhibition of NF-kappaB.	Oxaliplatin	75-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
15841378-3	2005	The geldanamycin analog 17AAG has been shown to inhibit Hsp90 and associated proteins.	geldanamycin	4-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
15841378-3	2005	The geldanamycin analog 17AAG has been shown to inhibit Hsp90 and associated proteins.	tanespimycin	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
15841378-12	2005	The depletion of Hsp90 was more pronounced in cells exposed to 17DMAG than in those treated with 17AAG.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	63-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
15841378-12	2005	The depletion of Hsp90 was more pronounced in cells exposed to 17DMAG than in those treated with 17AAG.	tanespimycin	97-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
15754340-8	2005	Conversely, the inhibition of Erk activity induced by 12 h exposure to 10 mM Mek-1 inhibitor U0126 antagonized the effects induced by HSP90 transfection on apoptosis caused by MW-EMF.	U 0126	93-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	134-139
16061682-2	2005	Towards this end, we have investigated the effects of a representative Hsp90 inhibitor, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17DMAG), on the radiosensitivity of a panel of human tumor cell lines.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	88-141	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
16061682-2	2005	Towards this end, we have investigated the effects of a representative Hsp90 inhibitor, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17DMAG), on the radiosensitivity of a panel of human tumor cell lines.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	143-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
16061882-0	2005	Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin prevents synovial sarcoma proliferation via apoptosis in in vitro models.	tanespimycin	16-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16051866-7	2005	Geldanamycin, an inhibitor of Hsp90, results in decreased HSV-1 yields and blocks viral DNA synthesis.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
15784732-0	2005	Heat shock protein 90 inhibition sensitizes acute myelogenous leukemia cells to cytarabine.	Cytarabine	80-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
15937340-1	2005	The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90.	Hydroxamic Acids	4-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-221
15937340-1	2005	The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90.	Hydroxamic Acids	21-24	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-221
15937340-1	2005	The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90.	LAQ824	84-90	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-221
15937340-1	2005	The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90.	Panobinostat	95-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-221
15937340-6	2005	Depletion of HDAC6 levels also inhibited the binding of HSP90 to ATP, reduced the chaperone association of HSP90 with its client proteins, e.g. Bcr-Abl, and induced polyubiquitylation and partial depletion of Bcr-Abl.	Adenosine Triphosphate	65-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
15937340-7	2005	Conversely, the ectopic overexpression of HDAC6 inhibited LAQ824-induced acetylation of HSP90 and alpha-tubulin and reduced LAQ824-mediated depletion of Bcr-Abl, AKT, and c-Raf.	LAQ824	58-64	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
15955698-0	2005	The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors.	3,4-diarylpyrazole	102-120	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
15955698-1	2005	High-throughput screening identified the 3,4-diarylpyrazole CCT018159 as a novel and potent (7.1 microM) inhibitor of Hsp90 ATPase activity.	3,4-diarylpyrazole	41-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
15955698-1	2005	High-throughput screening identified the 3,4-diarylpyrazole CCT018159 as a novel and potent (7.1 microM) inhibitor of Hsp90 ATPase activity.	CCT018159	60-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	118-123
15784732-2	2005	Recent results also demonstrated that Chk1 is depleted when cells are treated with heat shock protein 90 (Hsp90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	123-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
15784732-2	2005	Recent results also demonstrated that Chk1 is depleted when cells are treated with heat shock protein 90 (Hsp90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG).	tanespimycin	123-161	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-104
15974572-1	2005	The crystal structure of a previously reported screening hit 1 (CCT018159) bound to the N terminal domain of molecular chaperone Hsp90 has been used to design 5-amide analogues.	Amides	161-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	129-134
15937123-3	2005	In this work, we show by a variety of methods (ozone chemiluminescence, biotin switch, and mass spectrometry) that the molecular chaperone Hsp90 is a target of S-nitrosylation and identify a susceptible cysteine residue in the region of the C-terminal domain that interacts with endothelial nitric oxide synthase (eNOS).	Biotin	72-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
15883021-3	2005	Here we describe associations between Hsp90 chaperone machinery and another chaperone, the 97-kDa valosin-containing protein VCP.	valosin	98-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
15937123-3	2005	In this work, we show by a variety of methods (ozone chemiluminescence, biotin switch, and mass spectrometry) that the molecular chaperone Hsp90 is a target of S-nitrosylation and identify a susceptible cysteine residue in the region of the C-terminal domain that interacts with endothelial nitric oxide synthase (eNOS).	Cysteine	203-211	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
15782121-2	2005	In the present study, we show that Hsp90 inhibits hydrogen peroxide (H(2)O(2))-induced ASK1-p38 activation in endothelial cells (EC).	Hydrogen Peroxide	50-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
15782121-2	2005	In the present study, we show that Hsp90 inhibits hydrogen peroxide (H(2)O(2))-induced ASK1-p38 activation in endothelial cells (EC).	Hydrogen Peroxide	69-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40
15782121-7	2005	However, Akt is released from the N-terminal domain concomitant with binding to the C-terminal domain of ASK1 in response to ASK1 activator H(2)O(2), inhibitor of Hsp90 17-AAG and Akt inhibitor LY294002, leading to a more stable Hsp90-Akt-ASK1 complex.	Hydrogen Peroxide	140-148	heat shock protein 90 alpha family class A member 1	Homo sapiens	229-234
15782121-4	2005	Thus, inhibition of Hsp90 by 17-allyamino-17-demethoxygeldanamycin (17-AAG) or phosphatidylinositol 3-kinase (PI3K) LY294002 induced and synergized ASK1 activation and ASK1-mediated EC apoptosis.	17-allyamino-17-demethoxygeldanamycin	29-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15782121-4	2005	Thus, inhibition of Hsp90 by 17-allyamino-17-demethoxygeldanamycin (17-AAG) or phosphatidylinositol 3-kinase (PI3K) LY294002 induced and synergized ASK1 activation and ASK1-mediated EC apoptosis.	tanespimycin	68-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15782121-4	2005	Thus, inhibition of Hsp90 by 17-allyamino-17-demethoxygeldanamycin (17-AAG) or phosphatidylinositol 3-kinase (PI3K) LY294002 induced and synergized ASK1 activation and ASK1-mediated EC apoptosis.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	116-124	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15971989-7	2005	Their utility for confirming the mechanism of action of Hsp90 inhibition in secondary cell-based assays has been shown and applied to the novel Hsp90 inhibitor CCT018159.	CCT018159	160-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
15971989-7	2005	Their utility for confirming the mechanism of action of Hsp90 inhibition in secondary cell-based assays has been shown and applied to the novel Hsp90 inhibitor CCT018159.	CCT018159	160-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
15930313-7	2005	The HSP90 inhibitor geldanamycin enhances the degradation of IKKalpha and blocks 3-Cl-AHPC activation of NF-kappaB and 3-Cl-AHPC-mediated apoptosis.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
16004589-4	2005	The natural product geldanamycin, a potent ansamycin Hsp90 inhibitor, has served as a lead compound for the development of several derivatives that are currently undergoing clinical trials.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
15977996-5	2005	This paper presents data on how hsp90 is important to fungi and what role it might play in human disease with possible interactions with interleukin 6 and nitric oxide.	Nitric Oxide	155-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
16004589-4	2005	The natural product geldanamycin, a potent ansamycin Hsp90 inhibitor, has served as a lead compound for the development of several derivatives that are currently undergoing clinical trials.	Rifabutin	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	53-58
16004589-5	2005	Inhibition of Hsp90 with geldanamycin simultaneously depletes Hsp90-associated clients and impairs numerous signalling cascades that depend on chaperone function.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
16004589-5	2005	Inhibition of Hsp90 with geldanamycin simultaneously depletes Hsp90-associated clients and impairs numerous signalling cascades that depend on chaperone function.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
15890922-7	2005	Furthermore, Hsp90 inhibition with either geldanamycin or RNAi-mediated chaperone downregulation suppressed protein A accumulation in the absence of viral RNA replication.	geldanamycin	42-54	heat shock protein 90 alpha family class A member 1	Homo sapiens	13-18
16019471-12	2005	Early results of phase I studies indicate that 17-allylamino-17-demethoxygeldamycin (17-AAG), capable of binding and disrupting the function of HSP90, results in an acceptable toxicity profile while achieving in vivo disruption of multiple oncogenic client proteins.	17-allylamino-17-demethoxygeldamycin	47-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
16020198-8	2005	Acute exposure to Cd was found to trigger the upregulation of genes encoding the chaperone proteins HSP90A, HSP27, HSP40, GRP78, HSP72, and HO-1 in S-cells.	Cadmium	18-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-106
15782129-2	2005	Geldanamycins (GA) are antitumor drugs that bind and inhibit HSP90 chaperone activity at nanomolar concentrations (nM-GAi) by preventing proper folding and functioning of certain oncoproteins.	geldanamycin	0-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
15782129-2	2005	Geldanamycins (GA) are antitumor drugs that bind and inhibit HSP90 chaperone activity at nanomolar concentrations (nM-GAi) by preventing proper folding and functioning of certain oncoproteins.	geldanamycin	15-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
15782129-6	2005	We also examined the effect of Radicicol (RA), a drug with higher affinity than GA for HSP90.	monorden	42-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
15901158-2	2005	The antitumor antibiotics radicicol and geldanamycin are potent inhibitors of the Hsp90 protein folding machinery.	monorden	26-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
15901158-2	2005	The antitumor antibiotics radicicol and geldanamycin are potent inhibitors of the Hsp90 protein folding machinery.	geldanamycin	40-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
15897590-2	2005	The ansamycin-based Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in phase I/II clinical testing.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15897590-2	2005	The ansamycin-based Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in phase I/II clinical testing.	tanespimycin	36-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15897590-9	2005	These results suggest that this novel ansamycin-based Hsp90 inhibitor affects multiple pathways involved in tumor development and progression and may represent a new strategy for the treatment of HNSCC patients.	Rifabutin	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
15737995-2	2005	Besides acting as an allosteric enhancer, Hsp90 was shown to serve as a module recruiting Akt to phosphorylate the serine 1179/1177 (bovine/human) residue of eNOS.	Serine	115-121	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-47
15737995-11	2005	Moreover, overexpression of PDK1, but not Akt, reversed Hsp90 inhibition-induced loss of eNOS serine 1179 phosphorylation and salvaged enzymatic activity.	Serine	94-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
15737995-6	2005	Both geldanamycin and radicicol, two structurally different Hsp90 inhibitors, selectively reduced serine 1179-phosphorylated eNOS, leading to decreased enzyme activity.	geldanamycin	5-17	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
15737995-13	2005	Inhibition of Hsp90 function resulted in PDK1 depletion and thus triggered a cascade of Akt deactivation, loss of eNOS serine 1179 phosphorylation, and decrease of enzyme function.	Serine	119-125	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
15737995-6	2005	Both geldanamycin and radicicol, two structurally different Hsp90 inhibitors, selectively reduced serine 1179-phosphorylated eNOS, leading to decreased enzyme activity.	monorden	22-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
15737995-6	2005	Both geldanamycin and radicicol, two structurally different Hsp90 inhibitors, selectively reduced serine 1179-phosphorylated eNOS, leading to decreased enzyme activity.	Serine	98-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
15900503-7	2005	Essential steps in this adaptive mechanism include AhR binding of ligand in the cytoplasm of cells associated with two molecules of chaperone heatshock protein (Hsp90) and AhR interactive protein, translocation of the receptor to the nucleus, dimerization with the Ah receptor nuclear translocator, and binding of this heterodimeric transcription factor (present in CYP1A) to dioxin-responsive elements upstream of promoters that regulate the expression of genes involved in xenobiotic metabolism.	Dioxins	376-382	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
15796919-1	2005	Geldanamycin (GA) and herbimycin A are benzoquinone ansamycins (BAs) that inhibit the molecular chaperone HSP90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
15796919-1	2005	Geldanamycin (GA) and herbimycin A are benzoquinone ansamycins (BAs) that inhibit the molecular chaperone HSP90.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
15796919-1	2005	Geldanamycin (GA) and herbimycin A are benzoquinone ansamycins (BAs) that inhibit the molecular chaperone HSP90.	herbimycin	22-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
15796919-1	2005	Geldanamycin (GA) and herbimycin A are benzoquinone ansamycins (BAs) that inhibit the molecular chaperone HSP90.	benzoquinone ansamycins	39-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
15796919-1	2005	Geldanamycin (GA) and herbimycin A are benzoquinone ansamycins (BAs) that inhibit the molecular chaperone HSP90.	Benanserin hydrochloride	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	106-111
15584899-1	2005	The ATP-dependent molecular chaperone Hsp90 (heat-shock protein 90) is essential for the maturation of hormone receptors and protein kinases.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
15584899-1	2005	The ATP-dependent molecular chaperone Hsp90 (heat-shock protein 90) is essential for the maturation of hormone receptors and protein kinases.	Adenosine Triphosphate	4-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-66
15867239-0	2005	Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers.	tanespimycin	49-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-153
15867239-1	2005	PURPOSE: 17-(Allylamino)-17-demethoxygeldanamycin (17AAG), a benzoquinone antibiotic, down-regulates oncoproteins by binding specifically to heat shock protein 90 (HSP90).	tanespimycin	9-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-162
15867239-1	2005	PURPOSE: 17-(Allylamino)-17-demethoxygeldanamycin (17AAG), a benzoquinone antibiotic, down-regulates oncoproteins by binding specifically to heat shock protein 90 (HSP90).	tanespimycin	9-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
15867239-1	2005	PURPOSE: 17-(Allylamino)-17-demethoxygeldanamycin (17AAG), a benzoquinone antibiotic, down-regulates oncoproteins by binding specifically to heat shock protein 90 (HSP90).	tanespimycin	51-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-162
15867239-1	2005	PURPOSE: 17-(Allylamino)-17-demethoxygeldanamycin (17AAG), a benzoquinone antibiotic, down-regulates oncoproteins by binding specifically to heat shock protein 90 (HSP90).	tanespimycin	51-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
15867239-1	2005	PURPOSE: 17-(Allylamino)-17-demethoxygeldanamycin (17AAG), a benzoquinone antibiotic, down-regulates oncoproteins by binding specifically to heat shock protein 90 (HSP90).	quinone	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-162
15867239-1	2005	PURPOSE: 17-(Allylamino)-17-demethoxygeldanamycin (17AAG), a benzoquinone antibiotic, down-regulates oncoproteins by binding specifically to heat shock protein 90 (HSP90).	quinone	61-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
15843522-7	2005	In addition, radicicol, an inhibitor of heat shock protein 90 (Hsp90), and rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR), blocked IL-2-induced hTERT activity and nuclear translocation of hTERT but not hTERT mRNA expression.	monorden	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-61
15843522-7	2005	In addition, radicicol, an inhibitor of heat shock protein 90 (Hsp90), and rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR), blocked IL-2-induced hTERT activity and nuclear translocation of hTERT but not hTERT mRNA expression.	monorden	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
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
15592683-7	2005	The treatment with 100 nM geldanamycin for 24 h combined with ionizing radiation (1-5 Gy) during the first hour of drug exposure reduced cellular survival by 1.5-2 logs depending on radiation-energy dose level, while no changes in cell survival were detectable with equimolar geldampicin, a benzoquinone-ansamycin known not to inhibit Hsp90.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	335-340
15696546-0	2005	Transactivation of hsp70-1/2 in geldanamycin-treated human non-small cell lung cancer H460 cells: involvement of intracellular calcium and protein kinase C. Geldanamycin is an antitumor drug that binds HSP90 and induces a wide range of heat shock proteins, including HSP70s.	geldanamycin	32-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	202-207
15828828-3	2005	One of such inhibitors, the purine-scaffold class, has been reported to be potent and selective against Hsp90 both in vitro and in vivo models of cancer.	purine	28-34	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
15828828-7	2005	The study identifies derivative 11v as the most potent Hsp90 inhibitor of the purine-scaffold series published to date (EC(50) = 30 nM), and also as the compound of this class with highest selectivity for tumor vs normal cell Hsp90 (700 to 3000-fold).	purine	78-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
15696546-0	2005	Transactivation of hsp70-1/2 in geldanamycin-treated human non-small cell lung cancer H460 cells: involvement of intracellular calcium and protein kinase C. Geldanamycin is an antitumor drug that binds HSP90 and induces a wide range of heat shock proteins, including HSP70s.	geldanamycin	157-169	heat shock protein 90 alpha family class A member 1	Homo sapiens	202-207
15699047-7	2005	Additional experiments demonstrated that the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin, which down-regulates Chk1, also sensitized a variety of human carcinoma cell lines to SN-38.	tanespimycin	61-99	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
15699047-7	2005	Additional experiments demonstrated that the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin, which down-regulates Chk1, also sensitized a variety of human carcinoma cell lines to SN-38.	Irinotecan	187-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	45-50
16555999-5	2005	Since tumor cells frequently overexpress the active form of HSP90, which is more susceptible to inhibition by small molecules such as geldanamycin and its analogs, HSP90 became an attractive target for cancer therapy.	geldanamycin	134-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
15794642-7	2005	Affinity chromatography experiments implicate an indirect mechanism of action involving direct binding of EGCG to the AhR chaperone protein, hsp90.	epigallocatechin gallate	106-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	141-146
15794642-10	2005	These data implicate a model in which EGCG inhibits release of hsp90 from the AhR, stabilizing the complex in an intermediary state associated with XAP2.	epigallocatechin gallate	38-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
15794642-11	2005	This is the first time EGCG has been demonstrated to directly bind hsp90 and the first indication that GT may exert its chemopreventive effects through an interaction with the common chaperone hsp90.	epigallocatechin gallate	23-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	67-72
15794642-11	2005	This is the first time EGCG has been demonstrated to directly bind hsp90 and the first indication that GT may exert its chemopreventive effects through an interaction with the common chaperone hsp90.	epigallocatechin gallate	23-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
16555999-5	2005	Since tumor cells frequently overexpress the active form of HSP90, which is more susceptible to inhibition by small molecules such as geldanamycin and its analogs, HSP90 became an attractive target for cancer therapy.	geldanamycin	134-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	164-169
16555999-6	2005	This paper will review the recent advances in HSP90-biology and will discuss the emerging role of the HSP90 inhibitors such as 17-allylamino-17 demethoxy-geldanamycin and other HSP-90-directed small molecules in cancer therapy.	tanespimycin	127-166	heat shock protein 90 alpha family class A member 1	Homo sapiens	102-107
15671027-2	2005	The chaperone activity of Hsp90 requires ATP, which binds with approximately 10-fold lower affinity than ADP.	Adenosine Triphosphate	41-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
15671027-2	2005	The chaperone activity of Hsp90 requires ATP, which binds with approximately 10-fold lower affinity than ADP.	Adenosine Diphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	26-31
15671027-3	2005	This suggests that Hsp90 may be a physiological ATP sensor, regulating the stability of growth signaling cascades in relation to cellular energy charge.	Adenosine Triphosphate	48-51	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
15671027-4	2005	Here we show that lowering ATP concentration by inhibiting glycolysis or mitochondrial respiration in isolated myocytes triggers rapid dissociation of Hsp90 from ErbB2 and degradation of ErbB2 along with other client proteins.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	151-156
15671027-5	2005	The effect of disrupting Hsp90 chaperone activity by ATP depletion was similar to the effect of the pharmacological Hsp90 inhibitor geldanamycin.	Adenosine Triphosphate	53-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	25-30
15671027-5	2005	The effect of disrupting Hsp90 chaperone activity by ATP depletion was similar to the effect of the pharmacological Hsp90 inhibitor geldanamycin.	geldanamycin	132-144	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-121
15671027-6	2005	ATP depletion-induced disruption of Hsp90 chaperone activity was associated with cellular resistance to growth factor activation of intracellular signaling.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
15671027-8	2005	These results support a role for Hsp90 as an ATP sensor that modulates tissue growth factor responsiveness under metabolically stressed conditions and provide a novel mechanism by which cellular responsiveness to growth factor stimulation is modulated by cellular energy charge.	Adenosine Triphosphate	45-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
15625278-1	2005	Interactions between the histone deacetylase (HDAC) inhibitors suberanoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino 17-demethoxygeldanamycin (17-AAG) have been examined in Bcr-Abl(+) human leukemia cells (K562 and LAMA84), including those sensitive and resistant to STI571 (imatinib mesylate).	suberanoylanilide hydroxamic acid	63-96	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
15625278-1	2005	Interactions between the histone deacetylase (HDAC) inhibitors suberanoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino 17-demethoxygeldanamycin (17-AAG) have been examined in Bcr-Abl(+) human leukemia cells (K562 and LAMA84), including those sensitive and resistant to STI571 (imatinib mesylate).	Vorinostat	98-102	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
15777846-0	2005	Hsp90 inhibitor geldanamycin increases hsp70 mRNA stabilisation but fails to activate HSF1 in cells exposed to hydrostatic pressure.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15625278-1	2005	Interactions between the histone deacetylase (HDAC) inhibitors suberanoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino 17-demethoxygeldanamycin (17-AAG) have been examined in Bcr-Abl(+) human leukemia cells (K562 and LAMA84), including those sensitive and resistant to STI571 (imatinib mesylate).	Butyric Acid	125-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
15625278-1	2005	Interactions between the histone deacetylase (HDAC) inhibitors suberanoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino 17-demethoxygeldanamycin (17-AAG) have been examined in Bcr-Abl(+) human leukemia cells (K562 and LAMA84), including those sensitive and resistant to STI571 (imatinib mesylate).	tanespimycin	176-214	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
15625278-1	2005	Interactions between the histone deacetylase (HDAC) inhibitors suberanoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino 17-demethoxygeldanamycin (17-AAG) have been examined in Bcr-Abl(+) human leukemia cells (K562 and LAMA84), including those sensitive and resistant to STI571 (imatinib mesylate).	Imatinib Mesylate	340-346	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
15625278-1	2005	Interactions between the histone deacetylase (HDAC) inhibitors suberanoylanilide hydroxamic acid (SAHA) and sodium butyrate (SB) and the heat shock protein (Hsp) 90 antagonist 17-allylamino 17-demethoxygeldanamycin (17-AAG) have been examined in Bcr-Abl(+) human leukemia cells (K562 and LAMA84), including those sensitive and resistant to STI571 (imatinib mesylate).	Imatinib Mesylate	348-365	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-164
15777846-3	2005	In HeLa cells, both HP and Hsp90 inhibitor geldanamycin (GA) up-regulated Hsp70 expression through mRNA stabilisation.	geldanamycin	43-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
15777846-3	2005	In HeLa cells, both HP and Hsp90 inhibitor geldanamycin (GA) up-regulated Hsp70 expression through mRNA stabilisation.	geldanamycin	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
15713410-1	2005	A series of dihydroxyphenylpyrazole compounds were identified as a unique class of reversible Hsp90 inhibitors.	dihydroxyphenylpyrazole	12-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15644312-5	2005	We identify that Hsp90 is involved in delivery of the Tom40 precursor to mitochondria in an ATP-dependent manner.	Adenosine Triphosphate	92-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
15713410-0	2005	Crystal structures of human HSP90alpha-complexed with dihydroxyphenylpyrazoles.	dihydroxyphenylpyrazoles	54-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	28-38
15713410-2	2005	The crystal structures for two of the identified compounds complexed with the N-terminal ATP binding domain of human Hsp90alpha were determined.	Adenosine Triphosphate	89-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	117-127
15713410-4	2005	The pyrazole ring forms hydrogen bonds to the backbone carbonyl of Gly97, the hydroxyl group of Thr184 and to a water molecule, which is present in all of the published HSP90 structures.	pyrazole	4-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
15713410-4	2005	The pyrazole ring forms hydrogen bonds to the backbone carbonyl of Gly97, the hydroxyl group of Thr184 and to a water molecule, which is present in all of the published HSP90 structures.	Hydrogen	24-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
15713410-4	2005	The pyrazole ring forms hydrogen bonds to the backbone carbonyl of Gly97, the hydroxyl group of Thr184 and to a water molecule, which is present in all of the published HSP90 structures.	Water	112-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	169-174
15514006-1	2005	Present studies show that LBH589, a novel cinnamic hydroxamic acid analog histone deacetylase inhibitor, induces acetylation of histone H3 and H4 and of heat shock protein 90 (hsp90), increases p21 levels, as well as induces cell-cycle G(1) phase accumulation and apoptosis of the human chronic myeloid leukemia blast crisis (CML-BC) K562 cells and acute leukemia MV4-11 cells with the activating length mutation of FLT-3.	Panobinostat	26-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-174
15798097-5	2005	The Hsp90 inhibitor geldanamycin prevented the stabilization of Pim-1 by heat shock.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15613472-7	2005	Mutant reactivation is enhanced by simultaneous treatment with agents that stabilize the reactivated protein and is blocked by geldanamycin, a specific inhibitor of Hsp90 activity, indicating that Hsp90 antagonist therapy and therapies that act to reactivate mutant p53 will be incompatible.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	165-170
15613472-7	2005	Mutant reactivation is enhanced by simultaneous treatment with agents that stabilize the reactivated protein and is blocked by geldanamycin, a specific inhibitor of Hsp90 activity, indicating that Hsp90 antagonist therapy and therapies that act to reactivate mutant p53 will be incompatible.	geldanamycin	127-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	197-202
15514006-5	2005	The hsp90 inhibitor 17-allyl-amino-demethoxy geldanamycin (17-AAG) also induced polyubiquitylation and proteasomal degradation of FLT-3 and Bcr-Abl by reducing their chaperone association with hsp90.	17-allyl-amino-demethoxy geldanamycin	20-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	193-198
15514006-1	2005	Present studies show that LBH589, a novel cinnamic hydroxamic acid analog histone deacetylase inhibitor, induces acetylation of histone H3 and H4 and of heat shock protein 90 (hsp90), increases p21 levels, as well as induces cell-cycle G(1) phase accumulation and apoptosis of the human chronic myeloid leukemia blast crisis (CML-BC) K562 cells and acute leukemia MV4-11 cells with the activating length mutation of FLT-3.	Panobinostat	26-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181
15514006-5	2005	The hsp90 inhibitor 17-allyl-amino-demethoxy geldanamycin (17-AAG) also induced polyubiquitylation and proteasomal degradation of FLT-3 and Bcr-Abl by reducing their chaperone association with hsp90.	17-allyl-amino-demethoxy geldanamycin	20-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15661225-6	2005	METHODS: We tested two HSP90 inhibitors, 17-AAG and 17-DMAG, against gynecologic cancer cell lines (four endometrial, one cervical, one ovarian, and one breast cancer line).	tanespimycin	41-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
15723656-0	2005	STI571 (Glivec) inhibits the interaction between c-KIT and heat shock protein 90 of the gastrointestinal stromal tumor cell line, GIST-T1.	Imatinib Mesylate	0-6	heat shock protein 90 alpha family class A member 1	Homo sapiens	59-80
15723656-3	2005	Furthermore, STI571 prevents the interaction between c-KIT and the molecular chaperone, heat shock protein 90 (Hsp90).	Imatinib Mesylate	13-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-109
15723656-3	2005	Furthermore, STI571 prevents the interaction between c-KIT and the molecular chaperone, heat shock protein 90 (Hsp90).	Imatinib Mesylate	13-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	111-116
15723656-4	2005	Geldanamycin, an inhibitor of Hsp90, also prevents interaction between c-KIT and Hsp90, and inhibits tyrosine phosphorylation of c-KIT.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
15723656-4	2005	Geldanamycin, an inhibitor of Hsp90, also prevents interaction between c-KIT and Hsp90, and inhibits tyrosine phosphorylation of c-KIT.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	81-86
15643424-2	2005	Although targeting Hsp90 with the antibiotic inhibitor geldanamycin (GA) may be a promising approach for cancer treatment, little is known about the determinants of Hsp90 interaction with its client proteins.	geldanamycin	55-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
15757409-3	2005	Several chemically distinct Hsp90 inhibitors have shown encouraging antitumour activity in multiple preclinical model systems, and one Hsp90 inhibitor, the benzoquinone ansamycin 17-allylamino, 17-demethoxygeldanamycin, has completed five Phase I clinical trials, with a number of Phase II trials soon to be underway or in progress.	benzoquinone ansamycin	156-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
15757409-3	2005	Several chemically distinct Hsp90 inhibitors have shown encouraging antitumour activity in multiple preclinical model systems, and one Hsp90 inhibitor, the benzoquinone ansamycin 17-allylamino, 17-demethoxygeldanamycin, has completed five Phase I clinical trials, with a number of Phase II trials soon to be underway or in progress.	17-demethoxygeldanamycin	194-218	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
15862952-2	2005	All hsp90 ligands induced an E(2)- and MG132-inhibited decrease of both ER cell content.	Estradiol	29-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15862952-2	2005	All hsp90 ligands induced an E(2)- and MG132-inhibited decrease of both ER cell content.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	39-44	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15643424-2	2005	Although targeting Hsp90 with the antibiotic inhibitor geldanamycin (GA) may be a promising approach for cancer treatment, little is known about the determinants of Hsp90 interaction with its client proteins.	geldanamycin	69-71	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
15383005-3	2005	Incubation of cells with arachidonic acid or the microtubule-depolymerizing agent, nocodazole, causes loss of interaction of Hsp70 and Hsp90 with FLAG-tagged Ppp5 and increase of Ppp5 activity.	Arachidonic Acid	25-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
15455381-0	2005	Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin.	Cisplatin	137-146	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15455381-7	2005	Combined exposure also abrogated the ability of GA to induce a cytoprotective heat shock response and resulted in Hsp90 adduct formation.	geldanamycin	48-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	114-119
15383005-3	2005	Incubation of cells with arachidonic acid or the microtubule-depolymerizing agent, nocodazole, causes loss of interaction of Hsp70 and Hsp90 with FLAG-tagged Ppp5 and increase of Ppp5 activity.	Nocodazole	83-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
16333984-7	2005	The necessity of Ile296, Thr298, and Arg299, which are replaced by Leu, Met/Leu, and Lys, respectively, in some eukaryotic Hsp90, was dependent on the mAbs, and K41110 and K41116C could react with Hsp90s carrying these substitutions.	Leucine	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
16333984-7	2005	The necessity of Ile296, Thr298, and Arg299, which are replaced by Leu, Met/Leu, and Lys, respectively, in some eukaryotic Hsp90, was dependent on the mAbs, and K41110 and K41116C could react with Hsp90s carrying these substitutions.	Leucine	67-70	heat shock protein 90 alpha family class A member 1	Homo sapiens	197-202
16333984-7	2005	The necessity of Ile296, Thr298, and Arg299, which are replaced by Leu, Met/Leu, and Lys, respectively, in some eukaryotic Hsp90, was dependent on the mAbs, and K41110 and K41116C could react with Hsp90s carrying these substitutions.	Lysine	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
16333984-7	2005	The necessity of Ile296, Thr298, and Arg299, which are replaced by Leu, Met/Leu, and Lys, respectively, in some eukaryotic Hsp90, was dependent on the mAbs, and K41110 and K41116C could react with Hsp90s carrying these substitutions.	Leucine	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	123-128
16333984-7	2005	The necessity of Ile296, Thr298, and Arg299, which are replaced by Leu, Met/Leu, and Lys, respectively, in some eukaryotic Hsp90, was dependent on the mAbs, and K41110 and K41116C could react with Hsp90s carrying these substitutions.	Lysine	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	197-202
15853661-0	2005	Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
16333984-8	2005	From these data taken together, we propose that the pentapeptide Pro295-Ile-Trp-Thr-Arg299 of hHsp90 functions as an immunodominant epitope common to all eukaryotic Hsp90.	Tryptophan	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-100
16333984-8	2005	From these data taken together, we propose that the pentapeptide Pro295-Ile-Trp-Thr-Arg299 of hHsp90 functions as an immunodominant epitope common to all eukaryotic Hsp90.	Tryptophan	76-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
16333984-8	2005	From these data taken together, we propose that the pentapeptide Pro295-Ile-Trp-Thr-Arg299 of hHsp90 functions as an immunodominant epitope common to all eukaryotic Hsp90.	Threonine	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-100
16333984-8	2005	From these data taken together, we propose that the pentapeptide Pro295-Ile-Trp-Thr-Arg299 of hHsp90 functions as an immunodominant epitope common to all eukaryotic Hsp90.	Threonine	80-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
15853661-3	2005	Geldanamycin neither bind nor inhibit oncogene kinases directly, but specifically binds and inhibits a major molecular chaperone, Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	130-135
15853661-7	2005	Hsp90 functions in an ATP-dependent manner in cooperation with other molecular chaperones such as Cdc37 and FKBP52.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15853661-8	2005	Geldanamycin specifically inhibits the essential ATPase activity of Hsp90.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
15853661-9	2005	Thus, treatment of cells with geldanamycin results in inactivation, destabilization, and degradation of Hsp90 client proteins.	geldanamycin	30-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-109
15853661-10	2005	Because Hsp90 client proteins play important roles in the regulation of the cell cycle, cell growth, cell survival, apoptosis, and oncogenesis, geldanamycin obstructs the proliferation of cancer cells and shows anti-cancer activity in experimental animals.	geldanamycin	144-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	8-13
15962764-0	2005	Heat shock protein 90 (Hsp90) chaperone complex inhibitor, radicicol, potentiated radiation-induced cell killing in a hormone-sensitive prostate cancer cell line through degradation of the androgen receptor.	monorden	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
15962764-0	2005	Heat shock protein 90 (Hsp90) chaperone complex inhibitor, radicicol, potentiated radiation-induced cell killing in a hormone-sensitive prostate cancer cell line through degradation of the androgen receptor.	monorden	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
15962764-3	2005	In addition, the study also examined how a heat shock protein 90 (Hsp90) chaperone complex inhibitor modified the effect of DHT on the radiosensitivity of the cells, because binding of the androgen receptor (AR) to Hsp90 is required to maintain the stability and functioning of AR.	Dihydrotestosterone	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
15962764-5	2005	Radicicol was used as one of the known Hsp90 chaperone complex inhibitors, and the cells were incubated in the presence of this compound at a concentration of 500 nM.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
15611262-6	2005	Treatment of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90) function, also resulted in IKK detergent insolubility and proteasome-mediated degradation of the IKK complex.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-75
15526284-0	2005	Up-regulation of the association between heat shock protein 90 and endothelial nitric oxide synthase prevents high glucose-induced apoptosis in human endothelial cells.	Glucose	115-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-62
15526284-6	2005	The present study was designed to determine the involvement of protein interactions between eNOS and HSP90 in high glucose-induced endothelial cell apoptosis.	Glucose	115-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106
15526284-8	2005	The results showed that the protein interactions between eNOS and HSP90 and between eNOS and Akt and the phosphorylation of eNOS were up-regulated by high glucose exposure for 2-4 h. With longer exposures, these effects decreased gradually.	Glucose	155-162	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
15526284-9	2005	During early hours of exposure, the protein interactions of eNOS/HSP90 and eNOS/Akt and the phosphorylation of eNOS were all inhibited by geldanamycin, an HSP90 inhibitor.	geldanamycin	138-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	65-70
15526284-9	2005	During early hours of exposure, the protein interactions of eNOS/HSP90 and eNOS/Akt and the phosphorylation of eNOS were all inhibited by geldanamycin, an HSP90 inhibitor.	geldanamycin	138-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	155-160
15526284-11	2005	LY294002, a phosphatidylinositol 3 (PI3) kinase inhibitor, inhibited the association of eNOS/Akt and the phosphorylation of eNOS but had no effect on the interaction between eNOS and HSP90 during early hours of exposure.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	0-8	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
15526284-12	2005	From our results we propose that, in HUVECs, during early phase of high glucose exposure, apoptosis can be prevented by enhancement of eNOS activity through augmentation of the protein interaction between eNOS and HSP90 and recruitment of the activated Akt.	Glucose	72-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	214-219
15611262-6	2005	Treatment of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90) function, also resulted in IKK detergent insolubility and proteasome-mediated degradation of the IKK complex.	geldanamycin	24-36	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
15344906-7	2004	Furthermore, we show that the treatment of cells with the Hsp90-specific inhibitor geldanamycin leads to ubiquitination and enhanced degradation of both CDK11p110 and CDK11p46 through a proteasome-dependent pathway.	geldanamycin	83-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	58-63
15466438-1	2004	ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to the N-terminal domain in the Hsp90 dimer.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
15466438-1	2004	ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to the N-terminal domain in the Hsp90 dimer.	Adenosine Triphosphate	0-3	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
15466438-1	2004	ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to the N-terminal domain in the Hsp90 dimer.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
15466438-1	2004	ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to the N-terminal domain in the Hsp90 dimer.	Adenosine Triphosphate	113-116	heat shock protein 90 alpha family class A member 1	Homo sapiens	157-162
15466438-12	2004	These data indicated that Sba1 and Aha1 regulate Hsp90 by influencing the conformational state of the "ATP lid" and consequent N-terminal dimerization, whereas Sti1 does not.	Adenosine Triphosphate	103-106	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-54
15539946-3	2004	Since Hsp90 is also expressed at high levels in many normal tissues, it was unclear why Hsp90 inhibitors such as 17-allylamino-geldanamycin (17-AAG) have selective antitumor activity in animals and are well tolerated clinically.	tanespimycin	113-139	heat shock protein 90 alpha family class A member 1	Homo sapiens	88-93
15501066-1	2004	Novobiocin was recently shown to inhibit Hsp90 through a previously unrecognized C-terminal ATP binding site.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
15501066-1	2004	Novobiocin was recently shown to inhibit Hsp90 through a previously unrecognized C-terminal ATP binding site.	Adenosine Triphosphate	92-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	41-46
15501066-3	2004	In an effort to elucidate the C-terminal binding site of Hsp90, four photolabile analogues of novobiocin were prepared.	Novobiocin	94-104	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
15585643-0	2004	Enhanced tumor cell radiosensitivity and abrogation of G2 and S phase arrest by the Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	100-153	heat shock protein 90 alpha family class A member 1	Homo sapiens	84-89
15585643-2	2004	Therefore, we have investigated the effects of the orally bioavailable Hsp90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) on the radiosensitivity of human tumor cells in vitro and grown as tumor xenografts.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	87-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-76
15389545-1	2004	Geldanamycin (GA) binds to heat shock protein 90 (Hsp90) and interferes with its function which is to protect various cellular proteins involved in signaling, growth control, and survival from ubiquitination and subsequent degradation by the proteasome.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-48
15744362-0	2004	N-formyl-Met-Leu-Phe-induced oxidative burst in DMSO-differentiated HL-60 cells requires active Hsp90, but not intact microtubules.	Dimethyl Sulfoxide	48-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
15744362-1	2004	In this study we examined whether microtubules and heat shock protein 90 (Hsp90) are involved in phorbol myristate acetate (PMA) and N-formyl-Met-Leu-Phe (fMLP)-induced oxidative burst in DMSO-differentiated HL-60 cells.	Tetradecanoylphorbol Acetate	97-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	51-72
15744362-1	2004	In this study we examined whether microtubules and heat shock protein 90 (Hsp90) are involved in phorbol myristate acetate (PMA) and N-formyl-Met-Leu-Phe (fMLP)-induced oxidative burst in DMSO-differentiated HL-60 cells.	Tetradecanoylphorbol Acetate	97-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
15744362-1	2004	In this study we examined whether microtubules and heat shock protein 90 (Hsp90) are involved in phorbol myristate acetate (PMA) and N-formyl-Met-Leu-Phe (fMLP)-induced oxidative burst in DMSO-differentiated HL-60 cells.	Tetradecanoylphorbol Acetate	124-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
15744362-1	2004	In this study we examined whether microtubules and heat shock protein 90 (Hsp90) are involved in phorbol myristate acetate (PMA) and N-formyl-Met-Leu-Phe (fMLP)-induced oxidative burst in DMSO-differentiated HL-60 cells.	Dimethyl Sulfoxide	188-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	74-79
15744362-3	2004	In contrast, radicicol, an inhibitor of Hsp90, inhibited fMLP-induced oxidative burst in time and concentration-dependent manner where IC50 value for 30 min pre-incubation was 16.5 +/- 3.5 microM radicicol.	monorden	13-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
15744362-3	2004	In contrast, radicicol, an inhibitor of Hsp90, inhibited fMLP-induced oxidative burst in time and concentration-dependent manner where IC50 value for 30 min pre-incubation was 16.5 +/- 3.5 microM radicicol.	monorden	196-205	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-45
15744362-4	2004	We conclude that both PMA and fMLP-induced oxidative burst in DMSO-differentiated HL-60 cells is microtubule-independent while the latter requires Hsp90 activity.	Dimethyl Sulfoxide	62-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	147-152
15389545-1	2004	Geldanamycin (GA) binds to heat shock protein 90 (Hsp90) and interferes with its function which is to protect various cellular proteins involved in signaling, growth control, and survival from ubiquitination and subsequent degradation by the proteasome.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
15389545-1	2004	Geldanamycin (GA) binds to heat shock protein 90 (Hsp90) and interferes with its function which is to protect various cellular proteins involved in signaling, growth control, and survival from ubiquitination and subsequent degradation by the proteasome.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-48
15389545-1	2004	Geldanamycin (GA) binds to heat shock protein 90 (Hsp90) and interferes with its function which is to protect various cellular proteins involved in signaling, growth control, and survival from ubiquitination and subsequent degradation by the proteasome.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
15385631-4	2004	These models have contrasting implications for how ErbB2 exerts its biological function and how cancer therapies might down-regulate surface ErbB2, such as the antibody trastuzumab (Herceptin) or the Hsp90 inhibitor geldanamycin.	geldanamycin	216-228	heat shock protein 90 alpha family class A member 1	Homo sapiens	200-205
15501584-2	2004	As shown by immunofluorescence staining and immunoblot analysis, the Hsp90 inhibitor radicicol induced a rapid (within hours) depletion of estrogen receptor-alpha (ER) in MCF-7 and IBEP-2 breast carcinoma cells.	monorden	85-94	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
15483679-7	2004	The Hsp90 inhibitor geldanamycin enhanced caspase-dependent p23 cleavage both in vitro and in intact cells.	geldanamycin	20-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15358769-2	2004	We show that geldanamycin or radicicol, specific inhibitors of Hsp90, diminish specific wild-type p53 binding to the p21 promoter sequence.	geldanamycin	13-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
15358769-2	2004	We show that geldanamycin or radicicol, specific inhibitors of Hsp90, diminish specific wild-type p53 binding to the p21 promoter sequence.	monorden	29-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
15358769-10	2004	Interestingly, Hsp90 in an ATP-dependent manner can positively modulate p53 DNA binding after incubation at physiological temperature of 37 degrees C. Other recombinant human chaperones from Hsp70 and Hsp40 families were not able to efficiently substitute Hsp90 in this reaction.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
15358769-10	2004	Interestingly, Hsp90 in an ATP-dependent manner can positively modulate p53 DNA binding after incubation at physiological temperature of 37 degrees C. Other recombinant human chaperones from Hsp70 and Hsp40 families were not able to efficiently substitute Hsp90 in this reaction.	Adenosine Triphosphate	27-30	heat shock protein 90 alpha family class A member 1	Homo sapiens	256-261
15358769-11	2004	Consistent with our in vivo results, geldanamycin can suppress Hsp90 ability to regulate in vitro p53 DNA binding to the promoter sequence.	geldanamycin	37-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
15347682-5	2004	Evidence is also presented that the Cl(-)(i)-dependent regulatory pathway can be activated by a thermal stress but that it is no longer operational if NKCC1-expressing cells are pretreated with geldanamycin, an antibiotic that inhibits hsp90, albeit nonspecifically.	geldanamycin	194-206	heat shock protein 90 alpha family class A member 1	Homo sapiens	236-241
15533447-2	2004	To understand the mechanism of human Hsp90, we have carried out a detailed kinetic analysis of ATP binding, hydrolysis and product release.	Adenosine Triphosphate	95-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
15533447-7	2004	The thermodynamic linkage between client protein binding and nucleotide affinity revealed ATP bound Hsp90 has a higher affinity for client proteins than the ADP bound form.	Adenosine Triphosphate	90-93	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
15533447-7	2004	The thermodynamic linkage between client protein binding and nucleotide affinity revealed ATP bound Hsp90 has a higher affinity for client proteins than the ADP bound form.	Adenosine Diphosphate	157-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	100-105
15554686-9	2004	In addition, an analysis of the overall results of screening the library against the ATP binding site of two protein targets (HSP90 and CDK2) reveals different patterns of fragment binding, demonstrating that the approach can find selective compounds that discriminate between related binding sites.	Adenosine Triphosphate	85-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15632312-6	2004	The polyclonal antibody raised against a peptide, Met(315)-Glu(328), of human Grp94, which corresponded to the conserved region of hHsp90, cross-reacted with hHsp90, but not with other Hsp90-family members.	Glutamic Acid	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
15632312-6	2004	The polyclonal antibody raised against a peptide, Met(315)-Glu(328), of human Grp94, which corresponded to the conserved region of hHsp90, cross-reacted with hHsp90, but not with other Hsp90-family members.	Glutamic Acid	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	131-137
15632312-6	2004	The polyclonal antibody raised against a peptide, Met(315)-Glu(328), of human Grp94, which corresponded to the conserved region of hHsp90, cross-reacted with hHsp90, but not with other Hsp90-family members.	Glutamic Acid	59-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-164
15572859-0	2004	A drastic reduction in the basal level of heat-shock protein 90 in the brain of goldfish (Carassius auratus) after administration of geldanamycin.	geldanamycin	133-145	heat shock protein 90 alpha family class A member 1	Homo sapiens	42-63
15688614-1	2004	Benzoquinoid ansamycins can downregulate molecules which are chaperoned by heat shock protein (Hsp90), including numerous tyrosine kinases, steroid receptors, and cell cycle regulatory kinases.	benzoquinoid ansamycins	0-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
15292259-2	2004	Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone.	Adenosine Triphosphate	32-35	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15572859-1	2004	Geldanamycin (GA), a specific inhibitor of the chaperoning function of heat-shock protein 90 (Hsp90), has been shown to mimic heat shock (HS) in inducing expression of Hsp90, Hsp72 and other Hsps in unstressed mammalian cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-92
15572859-1	2004	Geldanamycin (GA), a specific inhibitor of the chaperoning function of heat-shock protein 90 (Hsp90), has been shown to mimic heat shock (HS) in inducing expression of Hsp90, Hsp72 and other Hsps in unstressed mammalian cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15572859-1	2004	Geldanamycin (GA), a specific inhibitor of the chaperoning function of heat-shock protein 90 (Hsp90), has been shown to mimic heat shock (HS) in inducing expression of Hsp90, Hsp72 and other Hsps in unstressed mammalian cells.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
15572859-1	2004	Geldanamycin (GA), a specific inhibitor of the chaperoning function of heat-shock protein 90 (Hsp90), has been shown to mimic heat shock (HS) in inducing expression of Hsp90, Hsp72 and other Hsps in unstressed mammalian cells.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	71-92
15572859-1	2004	Geldanamycin (GA), a specific inhibitor of the chaperoning function of heat-shock protein 90 (Hsp90), has been shown to mimic heat shock (HS) in inducing expression of Hsp90, Hsp72 and other Hsps in unstressed mammalian cells.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15572859-1	2004	Geldanamycin (GA), a specific inhibitor of the chaperoning function of heat-shock protein 90 (Hsp90), has been shown to mimic heat shock (HS) in inducing expression of Hsp90, Hsp72 and other Hsps in unstressed mammalian cells.	geldanamycin	14-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	168-173
15572859-2	2004	In the present study, intra-cerebral treatment of goldfish with GA (at a dose of 0.1 microg/g-body weight) diminished basal Hsp90 level to a 30-40% level in the brain, without affecting the basal Hsp72 level, as assayed 28-48 h after treatment.	geldanamycin	64-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	124-129
15569429-2	2004	METHODS: Heat shock protein 90-peptide complex (HSP90-PC) was isolated and purified by liquid chromatography after precipitation by 50% - 70% (NH4) 2SO4 saturation from 10 specimens of renal carcinoma resected from 10 patients aged 40 - 60 during operation.	Ammonium Sulfate	142-152	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
15388159-1	2004	Geldanamycin interferes with the action of heat shock protein 90 (Hsp90) by binding to the N-terminal ATP binding site and inhibiting an essential ATPase activity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-64
15388159-1	2004	Geldanamycin interferes with the action of heat shock protein 90 (Hsp90) by binding to the N-terminal ATP binding site and inhibiting an essential ATPase activity.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
15388159-1	2004	Geldanamycin interferes with the action of heat shock protein 90 (Hsp90) by binding to the N-terminal ATP binding site and inhibiting an essential ATPase activity.	Adenosine Triphosphate	102-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-64
15388159-1	2004	Geldanamycin interferes with the action of heat shock protein 90 (Hsp90) by binding to the N-terminal ATP binding site and inhibiting an essential ATPase activity.	Adenosine Triphosphate	102-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
15388159-2	2004	In a program directed toward finding potent, water soluble inhibitors of Hsp90, we prepared a library of over sixty 17-alkylamino-17-demethoxygeldanamycin analogs, and compared their affinity for Hsp90, ability to inhibit growth of SKBr3 mammalian cells, and in selected cases, water solubility.	Water	45-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
15569429-4	2004	The molecular weight and the identity of the purified HSP90-PC were confirmed by SDS-PAGE and Western blotting.	Sodium Dodecyl Sulfate	81-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	54-59
15471498-1	2004	Noviose is a key synthon for the construction of novobiocin, a clinically useful antitumor agent that has been shown to inhibit both type II topoisomerases and Hsp90.	noviose	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
15302866-4	2004	Inhibition of hsp90 function with 17-allylamino-17-demothoxygeldanamycin (17-AAG) reduces RET/PTC1 protein levels.	17-allylamino-17-demothoxygeldanamycin	34-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
15475321-2	2004	Many Hsp90 inhibitors function by binding to the N-terminal ATP pocket, but the chaperone has many other vulnerable points.	Adenosine Triphosphate	60-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	5-10
15471498-1	2004	Noviose is a key synthon for the construction of novobiocin, a clinically useful antitumor agent that has been shown to inhibit both type II topoisomerases and Hsp90.	Novobiocin	49-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	160-165
15284248-4	2004	We have found that the level of p53 is elevated with the decline of Hsp90 in UV-irradiated cells and that malfunction of Hsp90, as inhibited by geldanamycin, enhances the p53-involved UV irradiation-induced apoptosis.	geldanamycin	144-156	heat shock protein 90 alpha family class A member 1	Homo sapiens	121-126
15320777-7	2004	Urocortin-mediated cardioprotection involves several mechanisms, including increased expression of Kir6.1 K(ATP) channels and HSP90, although other as yet poorly understood mechanisms have also been implicated.	Urocortins	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15802049-6	2004	This may be due to a variety of factors, including chaperone activity, as steady-state luciferase levels were reduced by geldanamycin, an Hsp90 inhibitor.	geldanamycin	121-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
15358562-3	2004	Inhibition of Hsp90 with geldanamycin amplified Akt phosphorylation induced by insulin-like growth factor-1 (IGF-1) or insulin, indicating that Hsp90 normally buffers these signals.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	14-19
15378690-5	2004	In particular, the basal levels of HSC71 and HSP60 were increased in A431/Pt cells as compared to A431 cells, and cisplatin exposure resulted in up-regulation of HSP60 and HSP90 only in A431 cells.	Cisplatin	114-123	heat shock protein 90 alpha family class A member 1	Homo sapiens	172-177
15258137-3	2004	Two parameters were assayed: the ability and extent to which the constructs bound to Hsp90 and Cdc37, and the ability of the constructs to trigger salt-resistant high affinity complexes with Hsp90 and Cdc37 independent of the presence of molybdate.	Salts	147-151	heat shock protein 90 alpha family class A member 1	Homo sapiens	191-196
15364548-11	2004	Furthermore, the addition of the hsp90 inhibitors geldanamycin, herbimycin, and radicicol had no effect on the turnover of CYP2E1, differentiating the degradation of CYP2E1 from other substrates for proteasome-dependent degradation.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
15364548-11	2004	Furthermore, the addition of the hsp90 inhibitors geldanamycin, herbimycin, and radicicol had no effect on the turnover of CYP2E1, differentiating the degradation of CYP2E1 from other substrates for proteasome-dependent degradation.	monorden	80-89	heat shock protein 90 alpha family class A member 1	Homo sapiens	33-38
15247219-1	2004	Exposure of endothelial cells to vascular endothelial growth factor (VEGF) induced tyrosine phosphorylation of focal adhesion kinase (FAK) on site Tyr(407), an effect that required the association of VEGF receptor 2 (VEGFR2) with HSP90.	Tyrosine	83-91	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-235
15247219-1	2004	Exposure of endothelial cells to vascular endothelial growth factor (VEGF) induced tyrosine phosphorylation of focal adhesion kinase (FAK) on site Tyr(407), an effect that required the association of VEGF receptor 2 (VEGFR2) with HSP90.	Tyrosine	147-150	heat shock protein 90 alpha family class A member 1	Homo sapiens	230-235
15247219-2	2004	The association of VEGFR2 with HSP90 involved the last 130 amino acids of VEGFR2 and was blocked by geldanamycin, a specific inhibitor of HSP90.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	31-36
15247219-2	2004	The association of VEGFR2 with HSP90 involved the last 130 amino acids of VEGFR2 and was blocked by geldanamycin, a specific inhibitor of HSP90.	geldanamycin	100-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	138-143
15247219-9	2004	Our findings underscore for the first time the key role played by the VEGFR2-HSP90-RhoA-ROCK-FAK/Tyr(407) pathway in transducing the VEGF signal that leads to the assembly of focal adhesions and endothelial cell migration.	Tyrosine	97-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
15358562-3	2004	Inhibition of Hsp90 with geldanamycin amplified Akt phosphorylation induced by insulin-like growth factor-1 (IGF-1) or insulin, indicating that Hsp90 normally buffers these signals.	geldanamycin	25-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	144-149
15144235-5	2004	The binding of HSP90 to ACK2 is blocked upon treatment with geldanamycin, an HSP90-specific ATPase inhibitor, and is required for the in vivo kinase activity of ACK2 and its association with Cdc42.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-20
15144235-5	2004	The binding of HSP90 to ACK2 is blocked upon treatment with geldanamycin, an HSP90-specific ATPase inhibitor, and is required for the in vivo kinase activity of ACK2 and its association with Cdc42.	geldanamycin	60-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
15301726-4	2004	One Hsp90 inhibitor, 17-allylamio-17- desmethoxygeldanamycin (17-AAG), is currently in clinical trial.	17-allylamio-17- desmethoxygeldanamycin	21-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15265741-1	2004	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone required for the stability and function of a number of client proteins, many of which are involved in cancer development.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-21
15265741-1	2004	Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone required for the stability and function of a number of client proteins, many of which are involved in cancer development.	Adenosine Triphosphate	36-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	23-28
15265741-2	2004	The natural products geldanamycin (GM) and radicicol (RD) are known inhibitors of Hsp90, and their derivatives are being developed for the treatment of various cancers.	geldanamycin	21-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
15265741-2	2004	The natural products geldanamycin (GM) and radicicol (RD) are known inhibitors of Hsp90, and their derivatives are being developed for the treatment of various cancers.	geldanamycin	35-37	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
15265741-2	2004	The natural products geldanamycin (GM) and radicicol (RD) are known inhibitors of Hsp90, and their derivatives are being developed for the treatment of various cancers.	monorden	43-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	82-87
15265741-3	2004	To identify novel Hsp90 inhibitors, a highly robust time-resolved fluorescence resonance energy transfer (TR-FRET)-based HTS assay that measures the binding of biotinylated geldanamycin (biotin-GM) to the His-tagged human Hsp90 N-terminal ATP-binding domain (Hsp90N) was developed.	geldanamycin	173-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
15265741-3	2004	To identify novel Hsp90 inhibitors, a highly robust time-resolved fluorescence resonance energy transfer (TR-FRET)-based HTS assay that measures the binding of biotinylated geldanamycin (biotin-GM) to the His-tagged human Hsp90 N-terminal ATP-binding domain (Hsp90N) was developed.	geldanamycin	173-185	heat shock protein 90 alpha family class A member 1	Homo sapiens	222-229
15265741-3	2004	To identify novel Hsp90 inhibitors, a highly robust time-resolved fluorescence resonance energy transfer (TR-FRET)-based HTS assay that measures the binding of biotinylated geldanamycin (biotin-GM) to the His-tagged human Hsp90 N-terminal ATP-binding domain (Hsp90N) was developed.	biotin-gm	187-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
15265741-3	2004	To identify novel Hsp90 inhibitors, a highly robust time-resolved fluorescence resonance energy transfer (TR-FRET)-based HTS assay that measures the binding of biotinylated geldanamycin (biotin-GM) to the His-tagged human Hsp90 N-terminal ATP-binding domain (Hsp90N) was developed.	biotin-gm	187-196	heat shock protein 90 alpha family class A member 1	Homo sapiens	222-229
15265741-3	2004	To identify novel Hsp90 inhibitors, a highly robust time-resolved fluorescence resonance energy transfer (TR-FRET)-based HTS assay that measures the binding of biotinylated geldanamycin (biotin-GM) to the His-tagged human Hsp90 N-terminal ATP-binding domain (Hsp90N) was developed.	Histidine	205-208	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	4,4-difluoro-4-bora-3a,4a-diaza-s-indacene	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-136
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	Adenosine Diphosphate	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-114
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	4,4-difluoro-4-bora-3a,4a-diaza-s-indacene	56-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	Adenosine Triphosphate	22-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-114
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-136
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	geldanamycin	72-84	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	geldanamycin	86-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-136
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	GM-BODIPY	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	GM-BODIPY	79-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-114
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	geldanamycin	86-88	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	geldanamycin	138-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-136
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	geldanamycin	138-140	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	Adenosine Triphosphate	180-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-136
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	Adenosine Triphosphate	180-183	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	Adenosine Diphosphate	184-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-136
15296636-3	2004	The assay is based on the competition of fluorescently (BODIPY) labeled geldanamycin (GM) for binding to purified recombinant Hsp90alpha (GM is a natural product that binds to the ATP/ADP pocket in the amino terminal of Hsp90).	Adenosine Diphosphate	184-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	126-131
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	geldanamycin	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-114
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	PU24FCl	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	PU24FCl	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	104-114
15296636-7	2004	GM, PU24FCl, ADP, and ATP, all known to bind to the Hsp90 pocket, compete with GM-BODIPY for binding to Hsp90alpha with EC(50)s in agreement with reported values.	Adenosine Diphosphate	13-16	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-57
15168026-8	2004	Recent findings with 17-AAG indicate that tumor cells utilize Hsp90 quite differently from normal cells, explaining the selectivity of the drug and suggesting a central role of Hsp90 in malignant progression.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-67
15168026-8	2004	Recent findings with 17-AAG indicate that tumor cells utilize Hsp90 quite differently from normal cells, explaining the selectivity of the drug and suggesting a central role of Hsp90 in malignant progression.	tanespimycin	21-27	heat shock protein 90 alpha family class A member 1	Homo sapiens	177-182
15145929-2	2004	However, the laboratory that discovered pifithrin recently reported that the compound also inhibits heat shock and glucocorticoid receptor (GR) signaling, and they suggested that PFTalpha targets a factor common to all three signal transduction pathways, such as the hsp90/hsp70-based chaperone machinery (Komarova, E. A., Neznanov, N., Komarov, P. G., Chernov, M. V., Wang, K., and Gudkov, A. V. (2003) J. Biol.	pifithrin	40-49	heat shock protein 90 alpha family class A member 1	Homo sapiens	267-272
15145929-2	2004	However, the laboratory that discovered pifithrin recently reported that the compound also inhibits heat shock and glucocorticoid receptor (GR) signaling, and they suggested that PFTalpha targets a factor common to all three signal transduction pathways, such as the hsp90/hsp70-based chaperone machinery (Komarova, E. A., Neznanov, N., Komarov, P. G., Chernov, M. V., Wang, K., and Gudkov, A. V. (2003) J. Biol.	pifithrin	179-187	heat shock protein 90 alpha family class A member 1	Homo sapiens	267-272
15239664-0	2004	Synthesis and biological evaluation of a new class of geldanamycin derivatives as potent inhibitors of Hsp90.	geldanamycin	54-66	heat shock protein 90 alpha family class A member 1	Homo sapiens	103-108
15239664-2	2004	Inhibition of the ATPase activity of Hsp90 by natural products (e.g., 17-allylaminogeldanamycin or radicicol) leads to the ubiquitination of oncogenic client proteins such as Her-2, Raf-1, and p-Akt followed by their proteasomal degradation.	tanespimycin	70-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
15239664-2	2004	Inhibition of the ATPase activity of Hsp90 by natural products (e.g., 17-allylaminogeldanamycin or radicicol) leads to the ubiquitination of oncogenic client proteins such as Her-2, Raf-1, and p-Akt followed by their proteasomal degradation.	monorden	99-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
15239664-6	2004	In addition, we confirmed the selectivity of geldanamycin analogues for Hsp90 derived from tumor cells using a novel cell lysate binding assay.	geldanamycin	45-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
15269157-12	2004	CONCLUSIONS: We show that the Hsp90 targeting agents 17-DMAG and 17-AAG inhibit angiogenesis.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	30-35
15223329-2	2004	In carrying out these functions Hsp90 hydrolyses ATP as it cycles between ADP- and ATP-bound forms, and this ATPase activity is regulated by the transient association with a variety of co-chaperones.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
15223329-2	2004	In carrying out these functions Hsp90 hydrolyses ATP as it cycles between ADP- and ATP-bound forms, and this ATPase activity is regulated by the transient association with a variety of co-chaperones.	Adenosine Diphosphate	74-77	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
15223329-2	2004	In carrying out these functions Hsp90 hydrolyses ATP as it cycles between ADP- and ATP-bound forms, and this ATPase activity is regulated by the transient association with a variety of co-chaperones.	Adenosine Triphosphate	83-86	heat shock protein 90 alpha family class A member 1	Homo sapiens	32-37
15236592-2	2004	Hsp90 function is intimately linked to intrinsic ATP binding and hydrolysis activities, the latter of which is under the regulatory control of accessory factors.	Adenosine Triphosphate	49-52	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15271357-0	2004	Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin.	geldanamycin	121-133	heat shock protein 90 alpha family class A member 1	Homo sapiens	62-83
15077173-3	2004	Inhibition by the Hsp90 ATPase inhibitors, geldanamycin (GA) and radicicol (RC), revealed that Hsp90 controls IKKs at two levels, inducibility of enzymatic activity and biogenesis, which can be discriminated by short- and long-time GA incubation, respectively.	geldanamycin	43-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
15077173-3	2004	Inhibition by the Hsp90 ATPase inhibitors, geldanamycin (GA) and radicicol (RC), revealed that Hsp90 controls IKKs at two levels, inducibility of enzymatic activity and biogenesis, which can be discriminated by short- and long-time GA incubation, respectively.	geldanamycin	43-55	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
15077173-3	2004	Inhibition by the Hsp90 ATPase inhibitors, geldanamycin (GA) and radicicol (RC), revealed that Hsp90 controls IKKs at two levels, inducibility of enzymatic activity and biogenesis, which can be discriminated by short- and long-time GA incubation, respectively.	geldanamycin	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
15077173-3	2004	Inhibition by the Hsp90 ATPase inhibitors, geldanamycin (GA) and radicicol (RC), revealed that Hsp90 controls IKKs at two levels, inducibility of enzymatic activity and biogenesis, which can be discriminated by short- and long-time GA incubation, respectively.	geldanamycin	57-59	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
15077173-3	2004	Inhibition by the Hsp90 ATPase inhibitors, geldanamycin (GA) and radicicol (RC), revealed that Hsp90 controls IKKs at two levels, inducibility of enzymatic activity and biogenesis, which can be discriminated by short- and long-time GA incubation, respectively.	monorden	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	18-23
15077173-3	2004	Inhibition by the Hsp90 ATPase inhibitors, geldanamycin (GA) and radicicol (RC), revealed that Hsp90 controls IKKs at two levels, inducibility of enzymatic activity and biogenesis, which can be discriminated by short- and long-time GA incubation, respectively.	monorden	65-74	heat shock protein 90 alpha family class A member 1	Homo sapiens	95-100
15040786-5	2004	In activated cells, cPGES phosphorylation occurred in parallel with increased cPGES enzymic activity and PGE2 production from exogenous and endogenous arachidonic acid, and these processes were facilitated by Hsp90 (heat-shock protein 90), a molecular chaperone that formed a tertiary complex with cPGES and CK-II.	Arachidonic Acid	151-167	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
15040786-8	2004	Moreover, the CK-II-Hsp90-mediated activation of cPGES was ameliorated by the p38 mitogen-activated protein kinase inhibitor SB20358 or by the anti-inflammatory glucocorticoid dexamethasone.	Ethyl 2-amino-5-Boc-6,7-dihydro-4H-thieno[3,2-c]pyridine-3-carboxylate	125-132	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15040786-8	2004	Moreover, the CK-II-Hsp90-mediated activation of cPGES was ameliorated by the p38 mitogen-activated protein kinase inhibitor SB20358 or by the anti-inflammatory glucocorticoid dexamethasone.	Dexamethasone	176-189	heat shock protein 90 alpha family class A member 1	Homo sapiens	20-25
15271357-1	2004	The affinity of geldanamycin (GA) for binding to heat shock protein 90 (HSP90) is 50- to 100-fold weaker than is the affinity of the structurally distinct natural product radicicol.	geldanamycin	30-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-70
15271357-1	2004	The affinity of geldanamycin (GA) for binding to heat shock protein 90 (HSP90) is 50- to 100-fold weaker than is the affinity of the structurally distinct natural product radicicol.	geldanamycin	30-32	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
15271357-4	2004	Thus, we propose that HSP90 catalyzes the isomerization of GA. We identify Ser113, a conserved residue outside the ATP binding pocket, as essential for the isomerization of GA.	Adenosine Triphosphate	115-118	heat shock protein 90 alpha family class A member 1	Homo sapiens	22-27
15271357-5	2004	In support of this model, we show that radicicol binds equally well to both wild-type HSP90 and the Ser113 mutant, whereas the binding of GA to the Ser113 mutant is decreased significantly from its binding to wild-type HSP90.	monorden	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	86-91
15271357-1	2004	The affinity of geldanamycin (GA) for binding to heat shock protein 90 (HSP90) is 50- to 100-fold weaker than is the affinity of the structurally distinct natural product radicicol.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	49-70
15271357-6	2004	Based on this finding, a mechanism of keto-enol tautomerization of GA catalyzed by HSP90 is proposed.	keto-enol	38-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
15271357-1	2004	The affinity of geldanamycin (GA) for binding to heat shock protein 90 (HSP90) is 50- to 100-fold weaker than is the affinity of the structurally distinct natural product radicicol.	geldanamycin	16-28	heat shock protein 90 alpha family class A member 1	Homo sapiens	72-77
15209518-0	2004	Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
15360086-0	2004	Radicicol potentiates heat-induced cell killing in a human oesophageal cancer cell line: the Hsp90 chaperone complex as a new molecular target for enhancement of thermosensitivity.	monorden	0-9	heat shock protein 90 alpha family class A member 1	Homo sapiens	93-98
15360086-1	2004	PURPOSE: To examine the ability of a heat shock protein 90 (Hsp90) chaperone complex inhibitor, radicicol, to modify thermal response and heat-induced cell killing, and to clarify the underlining mechanisms.	monorden	96-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-58
15360086-1	2004	PURPOSE: To examine the ability of a heat shock protein 90 (Hsp90) chaperone complex inhibitor, radicicol, to modify thermal response and heat-induced cell killing, and to clarify the underlining mechanisms.	monorden	96-105	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
15360086-6	2004	Heat alone activated Raf-1 and p42/p44 extracellular signal-regulated kinase (Erk), and heat in combination with radicicol inhibited the activation of Raf-1 and p42/p44 Erk through reduced binding of Raf-1 to Hsp90.	monorden	113-122	heat shock protein 90 alpha family class A member 1	Homo sapiens	209-214
15360086-8	2004	CONCLUSIONS: The Hsp90 chaperone complex inhibitor, radicicol, potentiated heat-induced cellular killing, and inhibition of p42/p44 Erk and Akt activation rather than modification of Hsp expression might be involved in enhancing cellular thermosensitivity.	monorden	52-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-22
15209518-8	2004	The recombinant C-terminal domain of Hsp90 adopted a proteolytic resistant conformation in the presence of novobiocin, indicating that alteration of Hsp90/cochaperone interactions was not the cause of the novobiocin-induced protease resistance within Hsp90"s C-terminal domain.	Novobiocin	107-117	heat shock protein 90 alpha family class A member 1	Homo sapiens	37-42
15209518-9	2004	The concentration dependence of this novobiocin-induced conformation change correlated with the dissociation of Hsp90 and Cdc37 from immature HRI and novobiocin-induced inhibition of Hsp90/Cdc37-dependent activation of HRI"s autokinase activity.	Novobiocin	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	112-117
15209518-9	2004	The concentration dependence of this novobiocin-induced conformation change correlated with the dissociation of Hsp90 and Cdc37 from immature HRI and novobiocin-induced inhibition of Hsp90/Cdc37-dependent activation of HRI"s autokinase activity.	Novobiocin	37-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
15209518-9	2004	The concentration dependence of this novobiocin-induced conformation change correlated with the dissociation of Hsp90 and Cdc37 from immature HRI and novobiocin-induced inhibition of Hsp90/Cdc37-dependent activation of HRI"s autokinase activity.	Novobiocin	150-160	heat shock protein 90 alpha family class A member 1	Homo sapiens	183-188
15209518-10	2004	The data suggest that binding of novobiocin to the C-terminal nucleotide binding site of Hsp90 induces a change in Hsp90"s conformation leading to the dissociation of bound kinase.	Novobiocin	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	89-94
15209518-10	2004	The data suggest that binding of novobiocin to the C-terminal nucleotide binding site of Hsp90 induces a change in Hsp90"s conformation leading to the dissociation of bound kinase.	Novobiocin	33-43	heat shock protein 90 alpha family class A member 1	Homo sapiens	115-120
15209518-0	2004	Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	63-68
15209518-11	2004	The unique structure and properties of novobocin-bound Hsp90 suggest that it may represent the "client-release" conformation of the Hsp90 machine.	novobocin	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
15209518-11	2004	The unique structure and properties of novobocin-bound Hsp90 suggest that it may represent the "client-release" conformation of the Hsp90 machine.	novobocin	39-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	132-137
15209518-2	2004	Hsp90 function is modulated through its interactions with cochaperones and the binding and hydrolysis of ATP.	Adenosine Triphosphate	105-108	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15209518-3	2004	Recently, novobiocin has been shown to bind to a second nucleotide binding site located within the C-terminal domain of Hsp90.	Novobiocin	10-20	heat shock protein 90 alpha family class A member 1	Homo sapiens	120-125
15212536-0	2004	New efficient synthesis of resorcinylic macrolides via ynolides: establishment of cycloproparadicicol as synthetically feasible preclinical anticancer agent based on Hsp90 as the target.	resorcinylic macrolides	27-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
15209518-4	2004	In this report, we have examined the effect of novobiocin on Hsp90 function in reticulocyte lysate.	Novobiocin	47-57	heat shock protein 90 alpha family class A member 1	Homo sapiens	61-66
15212536-0	2004	New efficient synthesis of resorcinylic macrolides via ynolides: establishment of cycloproparadicicol as synthetically feasible preclinical anticancer agent based on Hsp90 as the target.	cycloproparadicicol	82-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	166-171
15209518-6	2004	Novobiocin induced the dissociation of Hsp90 and Cdc37 from immature HRI, while the Hsp90 cochaperones p23, FKBP52, and protein phosphatase 5 remained associated with immature HRI.	Novobiocin	0-10	heat shock protein 90 alpha family class A member 1	Homo sapiens	39-44
15212536-1	2004	A program currently ongoing in our laboratory envisions natural macrolide radicicol-based inhibitors targeting the molecular chaperone Hsp90.	Macrolides	64-73	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
15209518-7	2004	Proteolytic fingerprinting of Hsp90 indicated that novobiocin had a distinct effect on the conformation of Hsp90, and molybdate lowered the concentration of novobiocin required to alter Hsp90"s conformation by 10-fold.	Novobiocin	51-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
15212536-1	2004	A program currently ongoing in our laboratory envisions natural macrolide radicicol-based inhibitors targeting the molecular chaperone Hsp90.	monorden	74-83	heat shock protein 90 alpha family class A member 1	Homo sapiens	135-140
15209518-7	2004	Proteolytic fingerprinting of Hsp90 indicated that novobiocin had a distinct effect on the conformation of Hsp90, and molybdate lowered the concentration of novobiocin required to alter Hsp90"s conformation by 10-fold.	Novobiocin	51-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	107-112
15147973-8	2004	An immunoprecipitation assay indicated that BpA dissociated heat shock protein 90 (Hsp90) from HIF-1alpha and destabilized HIF-1alpha protein.	bisphenol A	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-81
15202892-2	2004	Hsp90 is essential to the survival of cancer cells and is inhibited by members of the ansamycin family of antibiotics.	Rifabutin	86-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	0-5
15202892-3	2004	In particular, the quinone-containing antibiotics geldanamycin (GDA) and herbimycin A inhibit Hsp90 function in vitro at low micromolar concentrations via interaction with an ATP binding domain.	quinone	19-26	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15202892-3	2004	In particular, the quinone-containing antibiotics geldanamycin (GDA) and herbimycin A inhibit Hsp90 function in vitro at low micromolar concentrations via interaction with an ATP binding domain.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15202892-3	2004	In particular, the quinone-containing antibiotics geldanamycin (GDA) and herbimycin A inhibit Hsp90 function in vitro at low micromolar concentrations via interaction with an ATP binding domain.	geldanamycin	64-67	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15202892-3	2004	In particular, the quinone-containing antibiotics geldanamycin (GDA) and herbimycin A inhibit Hsp90 function in vitro at low micromolar concentrations via interaction with an ATP binding domain.	herbimycin	73-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15202892-3	2004	In particular, the quinone-containing antibiotics geldanamycin (GDA) and herbimycin A inhibit Hsp90 function in vitro at low micromolar concentrations via interaction with an ATP binding domain.	Adenosine Triphosphate	175-178	heat shock protein 90 alpha family class A member 1	Homo sapiens	94-99
15202892-4	2004	Many proteins bind ATP, and the discovery of selective Hsp90 inhibitors requires the identification of other proteins that bind GDA and may cause undesired effects.	Adenosine Triphosphate	19-22	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
15202892-4	2004	Many proteins bind ATP, and the discovery of selective Hsp90 inhibitors requires the identification of other proteins that bind GDA and may cause undesired effects.	geldanamycin	128-131	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
15202892-7	2004	Preliminary studies indicate several proteins other than Hsp90 are isolated with biotinylated GDA.	geldanamycin	94-97	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
15147973-8	2004	An immunoprecipitation assay indicated that BpA dissociated heat shock protein 90 (Hsp90) from HIF-1alpha and destabilized HIF-1alpha protein.	bisphenol A	44-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	83-88
15174023-4	2004	Moreover, Hsp90 inhibitor geldanamycin destroyed the wild-type GCH level, and heat shock increased the synthesis of GCH protein.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15217611-0	2004	Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms.	purine	36-42	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
15217612-2	2004	Here we present PU24FCl, a representative of the first class of designed Hsp90 inhibitors.	PU24FCl	16-23	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
15217612-3	2004	By specifically and potently inhibiting tumor Hsp90, PU24FCl exhibits wide-ranging anti-cancer activities that occur at similar doses in all tested tumor types.	PU24FCl	53-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	46-51
15217612-6	2004	In concordance with its higher affinity for tumor Hsp90, in vivo PU24FCl accumulates in tumors while being rapidly cleared from normal tissue.	PU24FCl	65-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	50-55
15181088-0	2004	17-Allylamino-17-demethoxygeldanamycin activity against thyroid cancer cell lines correlates with heat shock protein 90 levels.	tanespimycin	0-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	98-119
15181088-3	2004	The goal of this study was to determine whether thyroid cancer cells are sensitive to the cytotoxic effects of 17-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90 inhibitor in clinical trials, and to determine predictors of this response.	tanespimycin	111-149	heat shock protein 90 alpha family class A member 1	Homo sapiens	163-168
15181088-7	2004	Western blot demonstrated that the NPA cells that were most resistant to 17AAG-induced cytotoxicity had the lowest levels of Hsp90 and were the only cells with persistent levels of Akt protein.	tanespimycin	73-78	heat shock protein 90 alpha family class A member 1	Homo sapiens	125-130
15133471-2	2004	17-allylaminogeldanamycin (17-AAG) is the first Hsp90 inhibitor to be tested in a clinical trial.	tanespimycin	0-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
15133471-2	2004	17-allylaminogeldanamycin (17-AAG) is the first Hsp90 inhibitor to be tested in a clinical trial.	tanespimycin	27-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
15133471-4	2004	We have developed a method for imaging the inhibition of Hsp90 by 17-AAG.	tanespimycin	66-72	heat shock protein 90 alpha family class A member 1	Homo sapiens	57-62
15177193-3	2004	The Hsp90 inhibitor 17-allylaminogeldanamycin (17-AAG) is presently in clinical trials.	tanespimycin	20-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
15004035-7	2004	By using a temperature-sensitive mutant of p53 where cytoplasmic-nuclear movement occurs by shift to permissive temperature, we show that p53 movement is impeded when p53 binding to hsp90 is inhibited by the hsp90 inhibitor radicicol.	monorden	224-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	182-187
15152036-7	2004	Using the hsp90-specific inhibitors radicicol and geldanamycin, we show that hsp90 is required for the constitutive trafficking of AMPA receptors into synapses during their continuous cycling between synaptic and nonsynaptic sites.	monorden	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15152036-7	2004	Using the hsp90-specific inhibitors radicicol and geldanamycin, we show that hsp90 is required for the constitutive trafficking of AMPA receptors into synapses during their continuous cycling between synaptic and nonsynaptic sites.	monorden	36-45	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
15152036-7	2004	Using the hsp90-specific inhibitors radicicol and geldanamycin, we show that hsp90 is required for the constitutive trafficking of AMPA receptors into synapses during their continuous cycling between synaptic and nonsynaptic sites.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15152036-7	2004	Using the hsp90-specific inhibitors radicicol and geldanamycin, we show that hsp90 is required for the constitutive trafficking of AMPA receptors into synapses during their continuous cycling between synaptic and nonsynaptic sites.	geldanamycin	50-62	heat shock protein 90 alpha family class A member 1	Homo sapiens	77-82
15004035-7	2004	By using a temperature-sensitive mutant of p53 where cytoplasmic-nuclear movement occurs by shift to permissive temperature, we show that p53 movement is impeded when p53 binding to hsp90 is inhibited by the hsp90 inhibitor radicicol.	monorden	224-233	heat shock protein 90 alpha family class A member 1	Homo sapiens	208-213
14761955-3	2004	Using NMR spectroscopy, we show that only the CS domain of human Sgt1 physically interacts with HSP90.	Cesium	46-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	96-101
15001580-9	2004	Upon treatment of MCF-7 cells with geldanamycin, an ansamycin antibiotic that inhibits Hsp90 function, MLK3 levels decrease dramatically.	geldanamycin	35-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
15001580-9	2004	Upon treatment of MCF-7 cells with geldanamycin, an ansamycin antibiotic that inhibits Hsp90 function, MLK3 levels decrease dramatically.	Rifabutin	52-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92
15126367-2	2004	Targeting hsp90 by the ansamycins geldanamycin and 17-allyl-amino-demethoxygeldanamycin (17-AAG) promotes degradation of several proteins through the ubiquitin-proteasome pathway, including oncogenic Raf, v-Src, erbB2, and BCR-ABL.	Lactams, Macrocyclic	23-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15126367-2	2004	Targeting hsp90 by the ansamycins geldanamycin and 17-allyl-amino-demethoxygeldanamycin (17-AAG) promotes degradation of several proteins through the ubiquitin-proteasome pathway, including oncogenic Raf, v-Src, erbB2, and BCR-ABL.	geldanamycin	34-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
15126367-2	2004	Targeting hsp90 by the ansamycins geldanamycin and 17-allyl-amino-demethoxygeldanamycin (17-AAG) promotes degradation of several proteins through the ubiquitin-proteasome pathway, including oncogenic Raf, v-Src, erbB2, and BCR-ABL.	17-allyl-amino-demethoxygeldanamycin	51-87	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
14999769-0	2004	Geldanamycin, an inhibitor of the chaperone activity of HSP90, induces MAPK-independent cell cycle arrest.	geldanamycin	0-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	56-61
14999769-2	2004	GA and related molecules act by inhibiting the chaperone function of the Hsp90 protein through competition for ATP binding.	Gallium	0-2	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
14999769-2	2004	GA and related molecules act by inhibiting the chaperone function of the Hsp90 protein through competition for ATP binding.	Adenosine Triphosphate	111-114	heat shock protein 90 alpha family class A member 1	Homo sapiens	73-78
15141013-1	2004	The ansamycin antibiotic, geldanamycin, targets the hsp 90 protein chaperone and promotes ubiquitin-dependent proteasomal degradation of its numerous client proteins.	Rifabutin	4-13	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-58
15141013-1	2004	The ansamycin antibiotic, geldanamycin, targets the hsp 90 protein chaperone and promotes ubiquitin-dependent proteasomal degradation of its numerous client proteins.	geldanamycin	26-38	heat shock protein 90 alpha family class A member 1	Homo sapiens	52-58
15141013-4	2004	We hypothesized that destabilization of hsp 90 client proteins with geldanamycin, while blocking their degradation with bortezomib, would promote the accumulation of aggregated, ubiquitinated, and potentially cytotoxic proteins.	geldanamycin	68-80	heat shock protein 90 alpha family class A member 1	Homo sapiens	40-46
15141013-9	2004	Individually, both geldanamycin and bortezomib induced hsp 90, hsp 70, and GRP78 stress proteins, but the drug combination superinduced these chaperones and caused them to become detergent insoluble.	geldanamycin	19-31	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-61
15141013-9	2004	Individually, both geldanamycin and bortezomib induced hsp 90, hsp 70, and GRP78 stress proteins, but the drug combination superinduced these chaperones and caused them to become detergent insoluble.	Bortezomib	36-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-61
15141013-12	2004	These observations support a mechanism whereby the geldanamycin plus bortezomib combination simultaneously disrupts hsp 90 and proteasome function, promotes the accumulation of aggregated, ubiquitinated proteins, and results in enhanced antitumor activity.	geldanamycin	51-63	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-122
15141013-12	2004	These observations support a mechanism whereby the geldanamycin plus bortezomib combination simultaneously disrupts hsp 90 and proteasome function, promotes the accumulation of aggregated, ubiquitinated proteins, and results in enhanced antitumor activity.	Bortezomib	69-79	heat shock protein 90 alpha family class A member 1	Homo sapiens	116-122
14754890-3	2004	The best predicted site was on the opposite face of the beta sheet from the pan-HSP90 radicicol-binding pocket, in close proximity to a deep hydrophobic pocket.	monorden	86-95	heat shock protein 90 alpha family class A member 1	Homo sapiens	80-85
14764593-0	2004	Aryl hydrocarbon nuclear translocator (ARNT) promotes oxygen-independent stabilization of hypoxia-inducible factor-1alpha by modulating an Hsp90-dependent regulatory pathway.	Oxygen	54-60	heat shock protein 90 alpha family class A member 1	Homo sapiens	139-144
14764593-4	2004	We demonstrated previously that pharmacologic inhibition of Hsp90 by geldanamycin (GA) impairs HIF transcription and promotes VHL (Von Hippel-Lindau)-independent degradation of the protein, thus implicating Hsp90 as an essential interacting partner for HIF.	geldanamycin	69-81	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
14764593-4	2004	We demonstrated previously that pharmacologic inhibition of Hsp90 by geldanamycin (GA) impairs HIF transcription and promotes VHL (Von Hippel-Lindau)-independent degradation of the protein, thus implicating Hsp90 as an essential interacting partner for HIF.	geldanamycin	83-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65
14764593-4	2004	We demonstrated previously that pharmacologic inhibition of Hsp90 by geldanamycin (GA) impairs HIF transcription and promotes VHL (Von Hippel-Lindau)-independent degradation of the protein, thus implicating Hsp90 as an essential interacting partner for HIF.	geldanamycin	83-85	heat shock protein 90 alpha family class A member 1	Homo sapiens	207-212
14761955-7	2004	Although ATP is absolutely required for p23 binding to HSP90, Sgt1 binds to HSP90 also in the absence of the non-hydrolyzable analog ATPgammaS.	Adenosine Triphosphate	9-12	heat shock protein 90 alpha family class A member 1	Homo sapiens	55-60
15013520-7	2004	The first-in-class Hsp90 inhibitor 17AAG has entered clinical trials with promising early results and a range of other agents is under investigation and preclinical development.	tanespimycin	35-40	heat shock protein 90 alpha family class A member 1	Homo sapiens	19-24
14744870-10	2004	The hsp90 inhibitor, geldanamycin, similarly blocked transcriptional activity of both functionally distinct receptors.	geldanamycin	21-33	heat shock protein 90 alpha family class A member 1	Homo sapiens	4-9
19749232-1	2009	Synthesis of benzoquinone ansa-adenosines, which are rationally designed as Hsp90 inhibitors by extracting and fusing a natural substrate, ATP, and a natural product, geldanamycin, was described.	benzoquinone ansa-adenosines	13-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
19749232-1	2009	Synthesis of benzoquinone ansa-adenosines, which are rationally designed as Hsp90 inhibitors by extracting and fusing a natural substrate, ATP, and a natural product, geldanamycin, was described.	Adenosine Triphosphate	139-142	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
19749232-1	2009	Synthesis of benzoquinone ansa-adenosines, which are rationally designed as Hsp90 inhibitors by extracting and fusing a natural substrate, ATP, and a natural product, geldanamycin, was described.	geldanamycin	167-179	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81