ArticleScientific reports2017
Site-specific phosphorylation regulates the structure and function of an intrinsically disordered domain of the glucocorticoid receptor.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Biomolecular Pathways Linking Preoperative Chronic Stress to Postoperative Cardiovascular Dysfunction in Noncardiac Surgery.Biomolecules · 2026Review
- Bovine α-herpesvirus 1 replication and immediate early transcription unit 1 promoter are jointly stimulated by glucocorticoid receptor and DNA-dependent ATPases.The Journal of general virology · 2026Article
- Glucocorticoid-Induced Proteome and Phosphoproteome Changes in Breast Cancer Cell Lines.Journal of proteome research · 2026Article
- Phosphorylation-Regulated Conformational Diversity and Topological Dynamics of an Intrinsically Disordered Nuclear Receptor.The journal of physical chemistry. B · 2025Article
- High dose methylprednisolone mediates YAP/TAZ-TEAD in vocal fold fibroblasts with macrophages.Scientific reports · 2025Article
- Impaired glucocorticoid receptor function attenuates herpes simplex virus 1 production during explant-induced reactivation from latency in female mice.Journal of virology · 2023Article
- Dose-Dependent Glucocorticoid Regulation of Transcription Factors in Vocal Fold Fibroblasts and Macrophages.The Laryngoscope · 2023Article
- Review
- Loss of glucocorticoid receptor phosphorylation contributes to cognitive and neurocentric damages of the amyloid-β pathway.Acta neuropathologica communications · 2022Article
- Crosstalk between p38 MAPK and GR Signaling.International journal of molecular sciences · 2022Review
- Intrinsically disordered proteins play diverse roles in cell signaling.Cell communication and signaling : CCS · 2022Review
- Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Experience and activity-dependent control of glucocorticoid receptors during the stress response in large-scale brain networks.Stress (Amsterdam, Netherlands) · 2021Article
- 90 YEARS OF PROGESTERONE: Steroid receptors as MAPK signaling sensors in breast cancer: let the fates decide.Journal of molecular endocrinology · 2020Review
- Emerging role of glucocorticoid receptor in castration resistant prostate cancer: A potential therapeutic target.Journal of Cancer · 2020Review
- Improved Glucocorticoid Receptor Ligands: Fantastic Beasts, but How to Find Them?Frontiers in endocrinology · 2020Review
- Functional Characterization of Glucocorticoid Receptor Variants Is Required to Avoid Misinterpretation of NGS Data.Journal of the Endocrine Society · 2019Article
- Role of Phosphorylation in the Modulation of the Glucocorticoid Receptor's Intrinsically Disordered Domain.Biomolecules · 2019Review
- A General Introduction to Glucocorticoid Biology.Frontiers in immunology · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered (ID) regions of the transcription factor proteins have much larger frequency of phosphorylation sites than ordered regions, suggesting an important role in their regulatory capacity. Consistent with this phenomenon, most of the functionally known phosphorylation sites in the steroid receptor family of transcription factors are located in the ID N-terminal domain that contains a powerful activation function (AF1) region. In this study, we determined the structural and functional consequences of functionally known phosphorylation residues (Ser203, 211, and 226) located in the human glucocorticoid receptor's (GR's) ID AF1 domain. We report the relative importance of each phosphorylation site in inducing a functionally active ordered conformation in GR's ID AF1 domain. Our data demonstrate a mechanism through which ID domain of the steroid receptors and other similar transcription factors may adopt a functionally active conformation under physiological conditions.
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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.