Evidence map›Paper›PMID 20085718›Full record

ArticleBiophysical journal2010

Modeling multivalent ligand-receptor interactions with steric constraints on configurations of cell-surface receptor aggregates.

Michael I Monine, Richard G Posner, Paul B Savage, James R Faeder, William S Hlavacek

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.7field-weighted citation impact, top 7% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  5. A spatio-temporal model reveals self-limiting FcRoyal Society open science · 2018
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  7. Maximal aggregation of polynomial dynamical systems.Proceedings of the National Academy of Sciences of the United States of America · 2017
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 5 institutions in 1 country.

Michael I MonineTheoretical Biology and Biophysics Group, Theoretical Division and Center for Nonlinear Studies, Los Alamos National Laboratory, Los Alamos, New Mexico, USA.
Richard G Posner
Paul B Savage
James R Faeder
William S Hlavacek
Brigham Young University · USLos Alamos National Laboratory · USNorthern Arizona University · USUniversity of New Mexico · USUniversity of Pittsburgh · US

Funding

UNM TRAININGP50GM085273 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI EDWARDS, JEREMY S · 2009 to 2018
$26.1M
Validation of Amplified Genes in Pancreatic CancerP01CA109552 · NCI · TRANSLATIONAL GENOMICS RESEARCH INST · PI VON HOFF, DANIEL D · 2005 to 2009
$15.2M
COMPUTATIONAL TOOLS FOR RULE-BASED MODELING OF BIOCHEMICAL SYSTEMSR01GM076570 · NIGMS · UNIVERSITY OF NEW MEXICO · PI HLAVACEK, WILLIAM S · 2007 to 2009
$815k
Receptor Aggregation on the Cell SurfaceR01AI035997 · NIAID · TRANSLATIONAL GENOMICS RESEARCH INST · PI POSNER, RICHARD G · 2002 to 2006
$701k
RECEPTOR AGGREGATION ON THE CELL SURFACER29AI035997 · NIAID · NORTHERN ARIZONA UNIVERSITY · PI POSNER, RICHARD G · 1993 to 1997
–
NCI NIH HHS CA109552NCI NIH HHS P01 CA109552NIAID NIH HHS AI35997NIAID NIH HHS R01 AI035997NIAID NIH HHS R29 AI035997NIGMS NIH HHS GM076570NIGMS NIH HHS GM085273NIGMS NIH HHS P50 GM085273NIGMS NIH HHS R01 GM076570
6 · The paper itself

Abstract

We use flow cytometry to characterize equilibrium binding of a fluorophore-labeled trivalent model antigen to bivalent IgE-FcepsilonRI complexes on RBL cells. We find that flow cytometric measurements are consistent with an equilibrium model for ligand-receptor binding in which binding sites are assumed to be equivalent and ligand-induced receptor aggregates are assumed to be acyclic. However, this model predicts extensive receptor aggregation at antigen concentrations that yield strong cellular secretory responses, which is inconsistent with the expectation that large receptor aggregates should inhibit such responses. To investigate possible explanations for this discrepancy, we evaluate four rule-based models for interaction of a trivalent ligand with a bivalent cell-surface receptor that relax simplifying assumptions of the equilibrium model. These models are simulated using a rule-based kinetic Monte Carlo approach to investigate the kinetics of ligand-induced receptor aggregation and to study how the kinetics and equilibria of ligand-receptor interaction are affected by steric constraints on receptor aggregate configurations and by the formation of cyclic receptor aggregates. The results suggest that formation of linear chains of cyclic receptor dimers may be important for generating secretory signals. Steric effects that limit receptor aggregation and transient formation of small receptor aggregates may also be important.

Indexed as

Models, ChemicalAnimalsBinding SitesCell LineCell MembraneComputer SimulationImmunoglobulin ELigandsMast CellsMultiprotein ComplexesProtein BindingProtein Interaction MappingRatsReceptors, IgEImmunoglobulin ELigandsMultiprotein ComplexesReceptors, IgE

Identifiers

PMID20085718
PMCPMC2800967
OpenAlexW2170780924

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.