ArticleScientific reports2020
Computational analysis of androgen receptor (AR) variants to decipher the relationship between protein stability and related-diseases.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Clinical features and genetic analysis of androgen receptor gene variants in 30 prepubertal patients with androgen insensitivity syndrome.Asian journal of andrology · 2026Article
- Complete androgen insensitivity syndrome with cryptorchid sertoli cell tumor: a case report and literature review.Frontiers in medicine · 2026Article
- A Computational and In Vitro Appraisal of Ostarine to Target Androgen Receptor in Glioma C6 Cells.Cell biochemistry and biophysics · 2025Article
- Structural insights into SOD1: from in silico and molecular dynamics to experimental analyses of ALS-associated E49K and R115G mutants.Frontiers in molecular biosciences · 2025Article
- Identification of the Rare Ala871Glu Mutation in the Androgen Receptor Gene Leading to Complete Androgen Insensitivity Syndrome in an Adolescent Girl with Primary Amenorrhea.Children (Basel, Switzerland) · 2022Article
- Allosteric interactions prime androgen receptor dimerization and activation.Molecular cell · 2022Article
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although more than 1,000 androgen receptor (AR) mutations have been identified and these mutants are pathologically important, few theoretical studies have investigated the role of AR protein folding stability in disease and its relationship with the phenotype of the patients. Here, we extracted AR variant data from four databases: ARDB, HGMD, Cosmic, and 1,000 genome. 905 androgen insensitivity syndrome (AIS)-associated loss-of-function mutants and 168 prostate cancer-associated gain-of-function mutants in AR were found. We analyzed the effect of single-residue variation on the folding stability of AR by FoldX and guanidine hydrochloride denaturation experiment, and found that genetic disease-associated mutations tend to have a significantly greater effect on protein stability than gene polymorphisms. Moreover, AR mutants in complete androgen insensitivity syndrome (CAIS) tend to have a greater effect on protein stability than in partial androgen insensitive syndrome (PAIS). This study, by linking disease phenotypes to changes in AR stability, demonstrates the importance of protein stability in the pathogenesis of hereditary disease.
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