ReviewSub-cellular biochemistry2015
Cdc37 as a co-chaperone to Hsp90.
Review in Sub-cellular biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 56 citations in OpenAlex.
- HSP90 and the cancer transcriptome: a comprehensive review of inhibitors and mechanistic insights.International journal of clinical oncology · 2025Review
- The possibilities and challenges associated with selective targetingTransactions of the Royal Society of South Africa. Royal Society of South Africa · 2025Article
- Discovery of new Hsp90-Cdc37 protein-protein interaction inhibitors:RSC advances · 2024Article
- HSP70 Is a Critical Regulator of HSP90 Inhibitor's Effectiveness in Preventing HCl-Induced Chronic Lung Injury and Pulmonary Fibrosis.International journal of molecular sciences · 2024Article
- Review
- Oscillation of Autophagy Induction under Cellular Stress and What Lies behind It, a Systems Biology Study.International journal of molecular sciences · 2023Article
- Multiple Targeting of HSP Isoforms to Challenge Isoform Specificity and Compensatory Expression.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Rational design, synthesis and structural characterization of peptides and peptidomimetics to target Hsp90/Cdc37 interaction for treating hepatocellular carcinoma.Computational and structural biotechnology journal · 2023Article
- The Chaperone System in Breast Cancer: Roles and Therapeutic Prospects of the Molecular Chaperones Hsp27, Hsp60, Hsp70, and Hsp90.International journal of molecular sciences · 2022Review
- (20S) Ginsenoside Rh2 Exerts Its Anti-Tumor Effect by Disrupting the HSP90A-Cdc37 System in Human Liver Cancer Cells.International journal of molecular sciences · 2021Article
- Triple knockdown of CDC37, HSP90-alpha and HSP90-beta diminishes extracellular vesicles-driven malignancy events and macrophage M2 polarization in oral cancer.Journal of extracellular vesicles · 2020Article
- Article
- A Long Non-coding RNA Lnc712 Regulates Breast Cancer Cell Proliferation.International journal of biological sciences · 2020Article
- Roles of Extracellular HSPs as Biomarkers in Immune Surveillance and Immune Evasion.International journal of molecular sciences · 2019Review
- MZF1 and SCAND1 Reciprocally RegulateCancers · 2019Article
- It's not magic - Hsp90 and its effects on genetic and epigenetic variation.Seminars in cell & developmental biology · 2019Review
- Hsp90 Interacts with the Bacterial Effector NleH1.Pathogens (Basel, Switzerland) · 2018Article
- Cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the CDK9 activation loop promotes P-TEFb assembly with Tat and proviral HIV reactivation.The Journal of biological chemistry · 2018Article
- Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.Journal of hematology & oncology · 2018Review
- Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. The Hsp90/Cdc37complex controls the folding of a large proportion of protein kinases and thus stands at the hub of a multitude of intracellular signaling networks. Its effects thus reach beyond the housekeeping pathways of protein folding into regulation of a wide range of cellular processes. Due to its influence in cell growth pathways Cdc37 has attracted much attention as a potential intermediate in carcinogenesis. Cdc37 is an attractive potential target in cancer due to: (1) it may be expressed to high level in some types of cancer and (2) Cdc37 controls multiple signaling pathways. This indicates a potential for: (1) selectivity due to its elevated expression and (2) robustness as the co-chaperone may control multiple growth signaling pathways and thus be less prone to evolution of resistance than other oncoproteins. Cdc37 may also be involved in other aspects of pathophysiology. Protein aggregation disorders have been linked to molecular chaperones and to age related declines in molecular chaperones and co-chaperones. Cdc37 appears to be a potential agent in longevity due to its links to protein folding and autophagy and it will be informative to study the role of Cdc37 maintenance/decline in aging organisms.
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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.