ArticleBiophysical journal2014
Open and closed conformations of the isolated transmembrane domain of death receptor 5 support a new model of activation.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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Who cites it
13 citing papers in PubMed.
- Article
- Multiplexed Dark FRET Biosensors: An accessible live-cell platform for target- and cell-specific monitoring of protein-protein interactions in 2D and 3D model systems.Research square · 2025Article
- Nimesulide, a COX-2 inhibitor, sensitizes pancreatic cancer cells to TRAIL-induced apoptosis by promoting DR5 clustering †.Cancer biology & therapy · 2023Article
- Noncompetitive Allosteric Antagonism of Death Receptor 5 by a Synthetic Affibody Ligand.Biochemistry · 2020Article
- Conformational states of TNFR1 as a molecular switch for receptor function.Protein science : a publication of the Protein Society · 2020Article
- Human immunoglobulin G hinge regulates agonistic anti-CD40 immunostimulatory and antitumour activities through biophysical flexibility.Nature communications · 2019Article
- Noncompetitive inhibitors of TNFR1 probe conformational activation states.Science signaling · 2019Article
- Molecular Mode of Action of TRAIL Receptor Agonists-Common Principles and Their Translational Exploitation.Cancers · 2019Review
- An Innovative High-Throughput Screening Approach for Discovery of Small Molecules That Inhibit TNF Receptors.SLAS discovery : advancing life sciences R & D · 2017Article
- Piecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.Biochimica et biophysica acta. Biomembranes · 2017Review
- Death Receptor 5 Activation Is Energetically Coupled to Opening of the Transmembrane Domain Dimer.Biophysical journal · 2017Article
- High-Throughput Spectral and Lifetime-Based FRET Screening in Living Cells to Identify Small-Molecule Effectors of SERCA.SLAS discovery : advancing life sciences R & D · 2017Article
- Death Receptor 5 Networks Require Membrane Cholesterol for Proper Structure and Function.Journal of molecular biology · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
It has long been presumed that activation of the apoptosis-initiating Death Receptor 5, as well as other structurally homologous members of the TNF-receptor superfamily, relies on ligand-stabilized trimerization of noninteracting receptor monomers. We and others have proposed an alternate model in which the TNF-receptor dimer-sitting at the vertices of a large supramolecular receptor network of ligand-bound receptor trimers-undergoes a closed-to-open transition, propagated through a scissorslike conformational change in a tightly bundled transmembrane (TM) domain dimer. Here we have combined electron paramagnetic resonance spectroscopy and potential-of-mean force calculations on the isolated TM domain of the long isoform of DR5. The experiments and calculations both independently validate that the opening transition is intrinsic to the physical character of the TM domain dimer, with a significant energy barrier separating the open and closed states.
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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.