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GenomicsHeat-shock protein 90 globally targets paused promoters and regulates environment-induced gene expression
In this study we provide evidence that Hsp90 binds chromatin at specific sites close to several TSS in Drosophila S2 cell line. In addition of finding a preference for stalled promoter regions of annotated genes, we uncover many intergenic Hsp90 binding sites coinciding with non-annotated transcript...
ORGANISM(S): Drosophila melanogaster 
2012-05-14 | E-GEOD-31226 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of Arabidopsis thaliana with reduced HSP90 levels
The molecular chaperone HSP90 aids the maturation of a diverse but select set of metastable protein clients, many of which are key to a variety of signal transduction pathways. HSP90 function has been best investigated in animal and fungal systems, where inhibition of the chaperone has exceptionall...
ORGANISM(S): Arabidopsis thaliana 
2008-06-15 | E-GEOD-7796 | biostudies-arrayexpress
TranscriptomicsRadicicol treatment of Drosophila cells
Drosophila S2 cells were treated with Heat-shock protein 90 (Hsp90) inhibitor radicicol for 15min, 30min and 1h. Poly(A) RNA was isolated and sequenced. Kinetics of transcriptional response to Hsp90 inhibition
ORGANISM(S): Drosophila melanogaster 
2012-05-14 | E-GEOD-35812 | biostudies-arrayexpress
ProteomicsHDX-MS data on bRaf, bRaf/Cdc37 and bRaf/Cdc37/Hsp90 protein complexes
HDX-MS data on bRaf, bRaf/Cdc37 and bRaf/Cdc37/Hsp90 protein complexes
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-01-04 | MSV000088635 | MassIVE
ProteomicsThe Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions
Molecular chaperones govern proteome health to support cell homeostasis. An essential eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology approach we characterized the features driving the Hsp90 physical interactome.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-08-10 | PXD040875 | Pride
Hsp90 Interactome Crosslinking Bpa 
ProteomicsGlobal proteome changes of normal NIH 3T3 versus Ras-transformed NIH cells treated with 3 different Hsp90 inhibitors (geldanamycin, PU-H71 and pochoxime A)
Heat shock protein 90 (Hsp90) is a major hub in the protein network that maintains cellular homeostasis and function. The qualitative and quantitative changes and rewiring of this protein network in tumor cells make them vastly dependent on Hsp90, and as a consequence its inhibition creates a profou...
ORGANISM(S): Mus Musculus (mouse) 
2019-02-11 | PXD009055 | JPOST Repository
ProteomicsHSP90 promotes Burkitt lymphoma cell survival by maintaining tonic B cell receptor signaling
Burkitt’s lymphoma (BL) is an aggressive B-cell neoplasm that is currently treated by intensive chemotherapy in combination with anti-CD20 antibodies. Because of their toxicity, current treatment regimens are often not suitable for elderly patients or for patients in developing countries where BL is...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080781 | MassIVE
TranscriptomicsPho85, Pcl1, and Hms1 Signaling Governs Candida albicans Morphogenesis Induced by Elevated Temperature or Hsp90 Compromise [ChIP-chip]
The capacity to sense and transduce temperature signals pervades all aspects of biology, and temperature exerts powerful control over the development and virulence of diverse pathogens. In the leading fungal pathogen of humans, Candida albicans, temperature has a profound impact on morphogenesis, a ...
ORGANISM(S): Candida albicans 
2012-03-20 | E-GEOD-34938 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of Arabidopsis plants after heat shock or treatment with HSP90 inhibitors (geldanamycin and radicicol)
Effect of heat shock or HSP90 inhibitors (geldanamycin and radicicol) on wild type Arabidopsis thaliana.
ORGANISM(S): Arabidopsis thaliana 
2007-06-01 | E-ATMX-12 | biostudies-arrayexpress
ProteomicsCharacterizations of HSP90-interacting complex in renal cells using tandem affinity purification and its potential role in kidney stone formation
Heat shock protein 90 (HSP90) is a highly abundant molecular chaperone that interacts with many other intracellular proteins to regulate various cellular processes. However, compositions of the HSP90-interacting complex remain underinvestigated. This study thus aimed to characterize such complex in ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-12-17 | MSV000083252 | MassIVE
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