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ProteomicsTotal proteome analysis of WT vs TRAP1 KO in HCT-116 and HEK-293T cells grown on different carbon sources.
The molecular chaperone TRAP1, the mitochondrial isoform of cytosolic HSP90, remains poorly understood with respect to its pivotal role in the regulation of mitochondrial metabolism. To characterize the impact of TRAP1 in maintaining the cellular proteome under different energy sources we carried ou...
ORGANISM(S): Homo sapiens (Human) 
2020-01-16 | PXD015828 | Pride
Oxidative phosphorylation Trap1 Mitochondrion Hsp90 Molecular chaperone 
ProteomicsEffects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry
Complex conformational dynamics are essential for the chaperone function of heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization establishing ATPase competence. Biochemical data demonstrate that the intrinsic, but weak, ATP hydrolyzing activity of Hsp90 is markedly en...
ORGANISM(S): Homo sapiens (Human) 
2019-06-17 | PXD013476 | Pride
Cross-linking Aha1 Ptm Heat shock Phosphorylation Xl-ms Chaperone Hsp90 
UnknownMethods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.
Not available
S-EPMC6045531 | biostudies-literature
Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080713 | MassIVE
TranscriptomicsWee1 Inhibition sensitizes prostate cancer cells to Hsp90 inhibitor to activate the intrinsic apoptotic pathway
Heat shock protein 90 (Hsp90) is an essential evolutionarily conserved molecular chaperone in eukaryotes. Cancer cells rely on Hsp90 to chaperone activated oncoproteins, and its involvement in numerous signaling pathways makes it an attractive target for drug development. Surprisingly, however, the ...
ORGANISM(S): Homo sapiens 
2013-01-10 | E-GEOD-38972 | biostudies-arrayexpress
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