ArticleBiophysical journal2005
Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed.
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Four-color single-molecule imaging with engineered tags resolves the molecular architecture of signaling complexes in the plasma membrane.Cell reports methods · 2022Article
- Optimal ligand discrimination by asymmetric dimerization and turnover of interferon receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- In Cellulo Protein Semi-Synthesis from Endogenous and Exogenous Fragments Using the Ultra-Fast Split Gp41-1 Intein.Angewandte Chemie (International ed. in English) · 2020Article
- Self-assembly of robust gold nanoparticle monolayer architectures for quantitative protein interaction analysis by LSPR spectroscopy.Analytical and bioanalytical chemistry · 2020Article
- Critical assessment of relevant methods in the field of biosensors with direct optical detection based on fibers and waveguides using plasmonic, resonance, and interference effects.Analytical and bioanalytical chemistry · 2020Review
- Interferon Receptor Trafficking and Signaling: Journey to the Cross Roads.Frontiers in immunology · 2020Review
- Quantitative systems pharmacology of interferon alpha administration: A multi-scale approach.PloS one · 2019Article
- TLR3 Ligand PolyI:C Prevents Acute Pancreatitis Through the Interferon-β/Interferon-α/β Receptor Signaling Pathway in a Caerulein-Induced Pancreatitis Mouse Model.Frontiers in immunology · 2019Article
- Cytosolic GAPDH as a redox-dependent regulator of energy metabolism.BMC plant biology · 2018Article
- Multi-functional DNA nanostructures that puncture and remodel lipid membranes into hybrid materials.Nature communications · 2018Article
- Immunomodulatory and antitumor effects of type I interferons and their application in cancer therapy.Oncotarget · 2017Review
- Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments.Nature communications · 2017Article
- Receptor dimer stabilization by hierarchical plasma membrane microcompartments regulates cytokine signaling.Science advances · 2016Article
- Structural Insights into the Neutralization Properties of the Fully Human, Anti-interferon Monoclonal Antibody Sifalimumab.The Journal of biological chemistry · 2015Article
- Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling.The Journal of cell biology · 2015Article
- Live cell micropatterning reveals the dynamics of signaling complexes at the plasma membrane.The Journal of cell biology · 2014Article
- Mathematical modelling and computational study of two-dimensional and three-dimensional dynamics of receptor-ligand interactions in signalling response mechanisms.Journal of mathematical biology · 2014Article
- The Mon1-Ccz1 GEF activates the Rab7 GTPase Ypt7 via a longin-fold-Rab interface and association with PI3P-positive membranes.Journal of cell science · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe an experimental approach for studying ligand-receptor interactions in the plane of the membrane. The extracellular domains of the type I interferon receptor subunits ifnar1-EC and ifnar2-EC were tethered in an oriented fashion onto solid-supported, fluid lipid bilayers, thus mimicking membrane anchoring and lateral diffusion of the receptor. Ligand-induced receptor assembling was investigated by simultaneous total internal reflection fluorescence spectroscopy and reflectance interferometry (RIf). Based on a rigorous characterization of the interactions of fluorescence-labeled IFNalpha2 with each of the receptor subunits, the dynamics of the ternary complex formation on the fluid lipid bilayer was addressed in further detail making use of the features of the simultaneous detection. All these measurements supported the formation of a ternary complex in two steps, i.e., association of the ligand to ifnar2-EC and subsequent recruitment of ifnar1-EC on the surface of the membrane. Based on the ability to control and quantify the receptor surface concentrations, equilibrium, and rate constants of the interaction in the plane of the membrane were determined by monitoring ligand dissociation at different receptor surface concentrations. Using mutants of IFNalpha2 binding to ifnar2-EC with different association rate constants, the key role of the association rate constants for the assembling mechanism was demonstrated.
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.