ReviewCell stress & chaperones2003
Cdc37 goes beyond Hsp90 and kinases.
Review in Cell stress & chaperones, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
54 citing papers in PubMed, 123 citations in OpenAlex.
- Molecular mechanism of PINK1 regulation by the Hsp90 machinery.Nature communications · 2025Article
- Prodrug-inspired adenosine triphosphate-activatable celastrol-Fe(III) chelate for cancer therapy.Science advances · 2024Article
- Predictive value of CDC37 gene expression for targeted therapy in metastatic colorectal cancer.European journal of cancer (Oxford, England : 1990) · 2024Article
- Detecting Posttranslational Modifications of Hsp90 Isoforms.Methods in molecular biology (Clifton, N.J.) · 2023Article
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Mechanism of Rapid Nuclear Factor-E2-Related Factor 2 (Nrf2) Activation via Membrane-Associated Estrogen Receptors: Roles of NADPH Oxidase 1, Neutral Sphingomyelinase 2 and Epidermal Growth Factor Receptor (EGFR).Antioxidants (Basel, Switzerland) · 2019Review
- Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases.Frontiers in neuroscience · 2019Review
- Global Dynamics of Yeast Hsp90 Middle and C-Terminal Dimer Studied by Advanced Sampling Simulations.Frontiers in molecular biosciences · 2019Article
- DNA methylation in blood as a mediator of the association of mid-childhood body mass index with cardio-metabolic risk score in early adolescence.Epigenetics · 2018Article
- Detecting Posttranslational Modifications of Hsp90.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Article
- Reactivation of ERK and Akt confers resistance of mutant BRAF colon cancer cells to the HSP90 inhibitor AUY922.Oncotarget · 2016Article
- The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.Scientific reports · 2016Article
- Hsp90 regulates autophagy and plays a role in cancer therapy.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Review
- A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.Scientific reports · 2015Article
- 5-Azacytidine-induced protein 2 (AZI2) regulates bone mass by fine-tuning osteoclast survival.The Journal of biological chemistry · 2015Article
- A visual review of the interactome of LRRK2: Using deep-curated molecular interaction data to represent biology.Proteomics · 2015Review
- Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins.Oncogene · 2015Article
- Cdc37 as a co-chaperone to Hsp90.Sub-cellular biochemistry · 2015Review
- Cdc37 engages in stable, S14A mutation-reinforced association with the most atypical member of the yeast kinome, Cdk-activating kinase (Cak1).Cell stress & chaperones · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cdc37 is a relatively poorly conserved and yet essential molecular chaperone. It has long been thought to function primarily as an accessory factor for Hsp90, notably directing Hsp90 to kinases as substrates. More recent discoveries challenge this simplistic view. Cdc37 client proteins other than kinases have now been found, and Cdc37 displays a variety of Hsp90-independent activities both in vitro and in vivo. It can function as a molecular chaperone by itself, interact with other Hsp90 cochaperones in the absence of Hsp90, and even support yeast growth and protein folding without its Hsp90-binding domain. Thus, for many substrates, there may be many alternative chaperone pathways involving Cdc37, Hsp90, or both.
Indexed as
Identifiers
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.