ArticleJournal of proteome research2008
Intrinsic disorder in nuclear hormone receptors.
Article in Journal of proteome research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Transcriptomic and Bioinformatic Analyses Identifying a Central Mif-Cop9-Nf-kB Signaling Network in Innate Immunity Response ofInternational journal of molecular sciences · 2023Article
- Drugging the Undruggable: Targeting the N-Terminal Domain of Nuclear Hormone Receptors.Advances in experimental medicine and biology · 2022Article
- Circulating extracellular vesicles and rheumatoid arthritis: a proteomic analysis.Cellular and molecular life sciences : CMLS · 2021Review
- Transcriptomic Analyses Reveal 2 and 4 Family Members of Cytochromes P450 (CYP) Involved in LPS Inflammatory Response in Pharynx ofInternational journal of molecular sciences · 2021Article
- Networks of Networks: An Essay on Multi-Level Biological Organization.Frontiers in genetics · 2021Review
- Intrinsic Disorder in Tetratricopeptide Repeat Proteins.International journal of molecular sciences · 2020Article
- New technologies to analyse protein function: an intrinsic disorder perspective.F1000Research · 2020Review
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- Intrinsic Disorder of the BAF Complex: Roles in Chromatin Remodeling and Disease Development.International journal of molecular sciences · 2019Article
- Reciprocal Perspective for Improved Protein-Protein Interaction Prediction.Scientific reports · 2018Article
- Ensemble allosteric model: energetic frustration within the intrinsically disordered glucocorticoid receptor.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- The mechanism of enterohepatic circulation in the formation of gallstone disease.The Journal of membrane biology · 2014Review
- Research resource: EPSLiM: ensemble predictor for short linear motifs in nuclear hormone receptors.Molecular endocrinology (Baltimore, Md.) · 2014Article
- Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators.Frontiers in molecular biosciences · 2014Review
- Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.The Journal of biological chemistry · 2013Article
- Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Endocrine reviews · 2012Review
- Evolutionary history and functional characterization of the amphibian xenosensor CAR.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Roles of intrinsic disorder in protein-nucleic acid interactions.Molecular bioSystems · 2012Review
- Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors.The Journal of biological chemistry · 2011Review
- Evolution of promiscuous nuclear hormone receptors: LXR, FXR, VDR, PXR, and CAR.Molecular and cellular endocrinology · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Many proteins possess intrinsic disorder (ID) and lack a rigid three-dimensional structure in at least part of their sequence. ID has been hypothesized to influence protein-protein and protein-ligand interactions. We calculated ID for nearly 400 vertebrate and invertebrate members of the biomedically important nuclear hormone receptor (NHR) superfamily, including all 48 known human NHRs. The predictions correctly identified regions in 20 of the 23 NHRs suggested as disordered based on published X-ray and NMR structures. Of the four major NHR domains (N-terminal domain, DNA-binding domain, D-domain, and ligand-binding domain), we found ID to be highest in the D-domain, a region of NHRs critical in DNA recognition and heterodimerization, coactivator/corepressor interactions and protein-protein interactions. ID in the D-domain and LBD was significantly higher in "hub" human NHRs that have 10 or more downstream proteins in their interaction networks compared to "non-hub" NHRs that interact with fewer than 10 downstream proteins. ID in the D-domain and LBD was also higher in classic, ligand-activated NHRs than in orphan, ligand-independent NHRs in human. The correlation between ID in human and mouse NHRs was high. Less correlation was found for ID between mammalian and non-mammalian vertebrate NHRs. For some invertebrate species, particularly sea squirts ( Ciona), marked differences were observed in ID between invertebrate NHRs and their vertebrate orthologs. Our results indicate that variability of ID within NHRs, particularly in the D-domain and LBD, is likely an important evolutionary force in shaping protein-protein interactions and NHR function. This information enables further understanding of these therapeutic targets.
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