ArticleAnalytical biochemistry2009
A dual-acceptor time-resolved Föster resonance energy transfer assay for simultaneous determination of thyroid hormone regulation of corepressor and coactivator binding to the thyroid hormone receptor: Mimicking the cellular context of thyroid hormone action.
Article in Analytical biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 23 citations in OpenAlex.
- Competitive Ligand-Induced Recruitment of Coactivators to Specific PPARα/δ/γ Ligand-Binding Domains Revealed by Dual-Emission FRET and X-Ray Diffraction of Cocrystals.Antioxidants (Basel, Switzerland) · 2025Article
- Evaluation of molecular glue-induced neomorphic protein-protein interaction with a cell lysate-based time-resolved fluorescence resonance energy transfer assay.ASPET discovery · 2025Article
- A multiplexed time-resolved fluorescence resonance energy transfer ultrahigh-throughput screening assay for targeting the SMAD4-SMAD3-DNA complex.Journal of molecular cell biology · 2024Article
- Rational design of a sensitivity-enhanced tracer for discovering efficient APC-Asef inhibitors.Nature communications · 2022Article
- Using TR-FRET to Investigate Protein-Protein Interactions: A Case Study of PXR-Coregulator Interaction.Advances in protein chemistry and structural biology · 2018Review
- Design of pathway preferential estrogens that provide beneficial metabolic and vascular effects without stimulating reproductive tissues.Science signaling · 2016Article
- Multicolored, Tb³⁺-Based Antibody-Free Detection of Multiple Tyrosine Kinase Activities.Analytical chemistry · 2015Article
- Cloning and identification of a novel thyroid hormone receptor β isoform expressed in the pituitary gland.Molecular and cellular biochemistry · 2014Article
- Mechanisms enforcing the estrogen receptor β selectivity of botanical estrogens.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Monitoring a coordinated exchange process in a four-component biological interaction system: development of a time-resolved terbium-based one-donor/three-acceptor multicolor FRET system.Journal of the American Chemical Society · 2010Article
- Minireview: Not picking pockets: nuclear receptor alternate-site modulators (NRAMs).Molecular endocrinology (Baltimore, Md.) · 2010Review
- Identification of pregnane X receptor ligands using time-resolved fluorescence resonance energy transfer and quantitative high-throughput screening.Assay and drug development technologies · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Previously, we reported the development of two in vitro time-resolved Föster resonance energy transfer (tr-FRET)-based assays for evaluating the potency and efficacy of different ligands of thyroid hormone receptor (TR) for regulating the recruitment of coregulators. We could measure independently, in separate assays, both the recruitment of SRC3 (steroid receptor coactivator 3, a transcriptional coactivator) and the dissociation of NCoR (nuclear receptor corepressor, a transcriptional corepressor) from a TR*retinoid X receptor (RXR) heterodimer bound to a DR+4 thyroid hormone response element (TRE). Here, by using the distinct emission peaks of Tb(3+), the donor fluorophore used to label the TRE-bound TR*RXR heterodimers, and selecting two distinct acceptor fluorophores, fluorescein and cyanine 5, to label of NCoR and SRC3, respectively, we have integrated our previous two assay formats into a single assay. Thus, we can measure the potency of TR ligands simultaneously for NCoR dissociation and SRC3 recruitment activities in a system that mimics many features of the cellular context of TR action. The performance of this dual assay was tested with a known, highly potent physiological TR ligand, triiodothyronine (T(3)), and with a synthetic TR antagonist, NH-3. Measured potencies and efficacies of these two TR ligands from this dual assay are highly comparable to those obtained from the two independent assays. Thus, this dual-acceptor tr-FRET assay further simplifies the measurement of ligand-modulated TR-coregulator interactions and should improve the overall efficiency of the screening process of TR drug discovery programs.
Indexed as
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.