ArticlePloS one2013
Structural insights into the folding defects of oncogenic pVHL lead to correction of its function in vitro.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer.Molecular oncology · 2026Review
- [A Family case of von Hippel-Lindau syndrome].Problemy endokrinologii · 2025Article
- Review
- Review
- Review
- Arginine refolds, stabilizes, and restores function of mutant pVHL proteins in animal model of the VHL cancer syndrome.Oncogene · 2019Article
- Clinical and molecular characteristics of unicentric mediastinal Castleman disease.Journal of thoracic disease · 2018Article
- Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations.Open biology · 2018Review
- Total proteome turbidity assay for tracking global protein aggregation in the natural cellular environment.Journal of biological methods · 2017Article
- Computational and experimental characterization of dVHL establish a Drosophila model of VHL syndrome.PloS one · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Loss of function mutations in the von Hippel-Lindau (pVHL) tumor suppressor protein are tumorigenic. In silico analysis of the structure and folding of WT pVHL identified in its core an aromatic tetrahedron, essential for stabilizing the protein. The mutations disrupt the aromatic tetrahedron, leading to misfolding of pVHL. Using biophysical methods we confirmed the in silico predictions, demonstrating that mutant pVHL proteins have lower stability than the WT, distort the core domain and as a result reduce the ability of the protein to bind its target HIF-1α. Using bacterial pVHL-EGFP based assay we screened for osmolytes capable of restoring folding of mutant pVHL. Among them, Arginine was the most effective and was verified by in vitro assays as a potent re-folder of pVHL. This resulted in functional restoration of the mutant proteins to the level of the WT.
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Registered trials
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