ArticleThe Journal of biological chemistry2016
Binding Studies of TNF Receptor Superfamily (TNFRSF) Receptors on Intact Cells.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers, 1 of them a synthesis that pooled it.
What it found
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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
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.
- Alterations in bone fracture healing associated with TNFRSF signaling pathways.Frontiers in pharmacology · 2022Pooled it
- A simple and broadly applicable nanobody-based approach to generate potent TNFR agonists.Cell death & disease · 2026Article
- Network of interactions between the tumor necrosis factor superfamily members and small S100 proteins.PloS one · 2026Article
- Article
- Role of endosomal RANKL-LGR4 signaling during osteoclast differentiation.Journal of molecular medicine (Berlin, Germany) · 2025Article
- CD163, a novel receptor for TNF, was revealedHeliyon · 2025Article
- Tumor necrosis factor receptor 2 in allergen tolerance: a perspective view.Frontiers in immunology · 2025Review
- Genetically engineered IgG1 and nanobody oligomers acquire strong intrinsic CD40 agonism.Bioengineered · 2024Article
- Regulation of temporal cytokine production by co-stimulation receptors in TCR-T cells is lost in CAR-T cells.Immunotherapy advances · 2024Article
- The crosstalk between neuropilin-1 and tumor necrosis factor-α in endothelial cells.Frontiers in cell and developmental biology · 2024Article
- How does the same ligand activate signaling of different receptors in TNFR superfamily: a computational study.Journal of cell communication and signaling · 2023Article
- Bistability regulates TNFR2-mediated survival and death of T-regulatory cells.Journal of biological physics · 2023Article
- Basic characterization of antibodies targeting receptors of the tumor necrosis factor receptor superfamily.Frontiers in immunology · 2023Article
- T-cell trans-synaptic vesicles are distinct and carry greater effector content than constitutive extracellular vesicles.Nature communications · 2022Article
- Visceral adiposity, inflammation, and hippocampal function in obesity.Neuropharmacology · 2022Review
- Controlled Modular Multivalent Presentation of the CD40 Ligand on P22 Virus-like Particles Leads to Tunable Amplification of CD40 Signaling.ACS applied bio materials · 2021Article
- Anti-Fn14 Antibody-Conjugated Nanoparticles Display Membrane TWEAK-Like Agonism.Pharmaceutics · 2021Article
- A multiscale study on the mechanisms of spatial organization in ligand-receptor interactions on cell surfaces.Computational and structural biotechnology journal · 2021Article
- A Systematic Test of Receptor Binding Kinetics for Ligands in Tumor Necrosis Factor Superfamily by Computational Simulations.International journal of molecular sciences · 2020Article
- Receptor Oligomerization and Its Relevance for Signaling by Receptors of the Tumor Necrosis Factor Receptor Superfamily.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ligands of the tumor necrosis factor superfamily (TNFSF) interact with members of the TNF receptor superfamily (TNFRSF). TNFSF ligand-TNFRSF receptor interactions have been intensively evaluated by many groups. The affinities of TNFSF ligand-TNFRSF receptor interactions are highly dependent on the oligomerization state of the receptor, and cellular factors (e.g. actin cytoskeleton and lipid rafts) influence the assembly of ligand-receptor complexes, too. Binding studies on TNFSF ligand-TNFRSF receptor interactions were typically performed using cell-free assays with recombinant fusion proteins that contain varying numbers of TNFRSF ectodomains. It is therefore not surprising that affinities determined for an individual TNFSF ligand-TNFRSF interaction differ sometimes by several orders of magnitude and often do not reflect the ligand activity observed in cellular assays. To overcome the intrinsic limitations of cell-free binding studies and usage of recombinant receptor domains, we performed comprehensive binding studies with Gaussia princeps luciferase TNFSF ligand fusion proteins for cell-bound TNFRSF members on intact cells at 37 °C. The affinities of the TNFSF ligand G. princeps luciferase-fusion proteins ranged between 0.01 and 19 nm and offer the currently most comprehensive and best suited panel of affinities for in silico studies of ligand-receptor systems of the TNF family.
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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.