ReviewThe Biochemical journal2016
Mechanisms of Hsp90 regulation.
Review in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 170 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
170 citing papers in PubMed, 308 citations in OpenAlex.
- Proteasome inhibitors rescue hypomyelination in iPSC based model of HIKESHI-associated leukodystrophy.Journal of translational medicine · 2026Article
- Dual Epigenetic and Chaperone Inhibition Disrupts Hypoxia Signaling and Tumor Progression in 3-D Models of Triple-Negative Breast Cancer.Research square · 2026Article
- Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Article
- Embracing diversity: Post-translational modifications, the chaperone code, and the emergence of new chaperone entities.Cell stress & chaperones · 2026Review
- Article
- HSP Inhibitor Sensitize Resistant MCF-7 Cells to Doxorubicin through Suppressing HSP90AB4P Pseudogene and HSPB1 Expression.Anti-cancer agents in medicinal chemistry · 2026Article
- Identification of Potential Dual HDAC6 and HSP90 Inhibitors for the Treatment of Cancer using Molecular Docking, Molecular Dynamics and MM/PBSA Studies: A ComprehensiveMedicinal chemistry (Shariqah (United Arab Emirates)) · 2026Article
- Small-molecule inhibitor of C‑terminal HSP90 dimerization modulates autophagy and functions synergistically with mTOR inhibition to kill cisplatin-resistant cancer cells.Cell death & disease · 2025Article
- Effects of defatted black soldier fly larvae meal on growth, nutrient digestibility, hepatopancreas biochemistry, intestinal microbiota, and phosphorus discharge of giant freshwater prawn (Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2025Article
- Molecular mechanism of PINK1 regulation by the Hsp90 machinery.Nature communications · 2025Article
- Exogenous application of γ-aminobutyric acid alleviates temperature stress in mungbean (Vigna radiata) and its wild non-progenitor (Vigna glabrescens) by regulating heat shock protein genes.BMC plant biology · 2025Article
- Short-term impacts of embryonic thermal manipulation in mule duck, a kinetic study: new tools for metabolic programming.BMC genomics · 2025Article
- Hsp90 and associates shaping parasite biology.mSphere · 2025Review
- Small Extracellular Vesicles Derived from NF2-Associated Schwannoma Cells Modulate Tumor Progression and Immunity via HSP90.Current oncology (Toronto, Ont.) · 2025Article
- The Hsp90β Isoform: An Attractive Target for Drug Development.Medicinal research reviews · 2025Review
- Quail development inVeterinary and animal science · 2025Article
- Nitration-driven structural changes in Hsp90 linked to gain of pathological functions.The Biochemical journal · 2025Article
- Glucose-regulated protein 94 (Grp94/gp96) in viral pathogenesis: Insights into its role and therapeutic potentials.European journal of medicinal chemistry · 2025Review
- Role of HSP90 in Type 2 Diabetes Mellitus and Its Association with Liver Diseases.Molecular biotechnology · 2025Review
110 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its activity. Perhaps the most important regulator is heat shock factor 1 (HSF1), which is primarily responsible for upregulating Hsp90 by binding heat shock elements (HSEs) within Hsp90 promoters. HSF1 is itself subject to a variety of regulatory processes and can directly respond to stress. HSF1 also interacts with a variety of transcriptional factors that help integrate biological signals, which in turn regulate Hsp90 appropriately. Because of the diverse clientele of Hsp90 a whole variety of co-chaperones also regulate its activity and some are directly responsible for delivery of client protein. Consequently, co-chaperones themselves, like Hsp90, are also subject to regulatory mechanisms such as post translational modification. This review, looks at the many different levels by which Hsp90 activity is ultimately regulated.
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What OpenQuestion holds
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.