ArticleFuture oncology (London, England)2012
The double edge of the HSP90-CDC37 chaperone machinery: opposing determinants of kinase stability and activity.
Article in Future oncology (London, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 8 citations in OpenAlex.
- Knowledge-driven interpretable neural networks provide mechanistic insight.Genome research · 2026Article
- Nitration-induced ubiquitination and degradation control quality of ERK1.The Biochemical journal · 2019Article
- Up-Regulation of Cdc37 Contributes to Schwann Cell Proliferation and Migration After Sciatic Nerve Crush.Neurochemical research · 2018Article
- Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.The Journal of biological chemistry · 2015Article
- Cdc37 as a co-chaperone to Hsp90.Sub-cellular biochemistry · 2015Review
- LKB1 Tumor Suppressor: Therapeutic Opportunities Knock when LKB1 Is Inactivated.Genes & diseases · 2014Article
Corrections and comments
- Comment on
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The molecular chaperone HSP90, in concert with the co-chaperone CDC37, facilitates the maturation and modulates the activity of a variety of protein kinases. In this article, Gaude and colleagues described the dual activities of the HSP90-CDC37 chaperone machinery in maintaining the stability while inhibiting the activity of LKB1 kinase. LKB1 in complex with HSP90-CDC37 has a longer half-life but is incapable of autophosphorylation, and its kinase activity is increased upon HSP90 inhibition. Dissociation of HSP90 from LKB1 results in its interaction with HSP/HSC70. HSP/HSC70 recruits the ubiquitin ligase CHIP, which ubiquitinates LKB1, leading to its proteasome-mediated degradation. These data emphasize the versatile roles of molecular chaperones associated with LKB1 and warrant future studies to characterize the clinical relevance of these observations.
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.