ArticleThe Journal of biological chemistry2010
Facilitating Akt clearance via manipulation of Hsp70 activity and levels.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 85 citations in OpenAlex.
- Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026Review
- Streptozotocin and L-Buthionine-Sulfoximine Decrease Neuron Membrane Lipid Packing and Alter Insulin Signaling.Neurotoxicity research · 2025Article
- Pifithrin-µ Induces Stress Granule Formation, Regulates Cell Survival, and Rewires Cellular Signaling.Cells · 2024Article
- Akt Is Controlled by Bag5 through a Monoubiquitination to Polyubiquitination Switch.International journal of molecular sciences · 2023Article
- Clinical implications of heat shock protein 70 in oral carcinogenesis and prediction of progression and recurrence in oral squamous cell carcinoma patients: a retrospective clinicopathological study.European journal of medical research · 2023Article
- Natural Products Targeting Hsp90 for a Concurrent Strategy in Glioblastoma and Neurodegeneration.Metabolites · 2022Review
- Cytoplasmic proteotoxicity regulates HRI-dependent phosphorylation of eIF2α via the Hsp70-Bag3 module.iScience · 2022Article
- The HSP-RTK-Akt axis mediates acquired resistance to Ganetespib in HER2-positive breast cancer.Cell death & disease · 2021Article
- The role and therapeutic potential of Hsp90, Hsp70, and smaller heat shock proteins in peripheral and central neuropathies.Medicinal research reviews · 2021Review
- Targeting Follistatin like 1 ameliorates liver fibrosis induced by carbon tetrachloride through TGF-β1-miR29a in mice.Cell communication and signaling : CCS · 2020Article
- HSP70 Multi-Functionality in Cancer.Cells · 2020Review
- Inhibitors and chemical probes for molecular chaperone networks.The Journal of biological chemistry · 2019Review
- Discovery of new chromen-4-one derivatives as telomerase inhibitors through regulating expression of dyskerin.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Mild heat induces a distinct "eustress" response in Chinese Hamster Ovary cells but does not induce heat shock protein synthesis.Scientific reports · 2017Article
- TRIM32-Cytoplasmic-Body Formation Is an ATP-Consuming Process Stimulated by HSP70 in Cells.PloS one · 2017Article
- Article
- Targeting the Diabetic Chaperome to Improve Peripheral Neuropathy.Current diabetes reports · 2016Review
- The human HSP70 family of chaperones: where do we stand?Cell stress & chaperones · 2016Review
- Hsp70 in cancer: back to the future.Oncogene · 2015Review
- An RNA aptamer specific to Hsp70-ATP conformation inhibits its ATPase activity independent of Hsp40.Nucleic acid therapeutics · 2015Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
Abstract
Members of the 70-kDa heat shock family can control and manipulate a host of oncogenic client proteins. This role of Hsp70 in both the folding and degradation of these client proteins makes it a potential drug target for certain forms of cancer. The phenothiazine family of compounds, as well as the flavonoid myricetin, was recently shown to inhibit Hsp70-ATPase activity, whereas members of the dihydropyrimidine family stimulated ATPase function. Akt, a major survival kinase, was found to be under the regulation of Hsp70, and when the ATPase activity of Hsp70 was increased or decreased by these compounds, Akt levels were also increased or decreased. Also, increasing Hsp70 levels concurrent with inhibition of its ATPase function synergistically reduced Akt levels to a greater extent than either manipulation alone, providing new insights about client fate decisions. Akt reductions mediated by Hsp70 inhibitors were prevented when Hsp70 expression was silenced with small interfering RNA. Inhibiting Hsp70 ATPase function produced cytotoxic events only in breast cancer cell lines where Akt dysfunction was previously shown, suggesting therapeutic specificity depending on the Hsp70 client profile. Thus, increasing Hsp70 levels combined with inhibiting its ATPase function may serve to dramatically reduce Akt levels and facilitate cell death in certain types of cancer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.