Evidence map›Paper›PMID 25468354›Full record

ArticleBiophysical journal2014

Association rates of membrane-coupled cell adhesion molecules.

Timo Bihr, Susanne Fenz, Erich Sackmann, Rudolf Merkel, Udo Seifert, Kheya Sengupta, Ana-Sunčana Smith

Open access · bronzeAbstract read
In one paragraph

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 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

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  6. Early T cell receptor signals globally modulate ligand:receptor affinities during antigen discrimination.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

7 authors at 5 institutions in 3 countries.

Timo BihrInstitut für Theoretische Physik and Cluster of Excellence Engineering of Advanced Materials, Friedrich-Alexander-Universität, Erlangen, Germany; II. Institut für Theoretische Physik, Universität Stuttgart, Stuttgart, Germany.
Susanne FenzInstitute of Complex Systems 7: Biomechanics Forschungszentrum Jülich, Jülich, Germany; Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Universität Würzburg, Würzburg, Germany.
Erich SackmannPhysics Department, Biophysics E22, Technische Universität München, München, Germany.
Rudolf MerkelInstitute of Complex Systems 7: Biomechanics Forschungszentrum Jülich, Jülich, Germany.
Udo SeifertII. Institut für Theoretische Physik, Universität Stuttgart, Stuttgart, Germany.
Kheya SenguptaAix-Marseille Université, CNRS, CINaM UMR 7325, Marseille, France.
Ana-Sunčana SmithInstitut für Theoretische Physik and Cluster of Excellence Engineering of Advanced Materials, Friedrich-Alexander-Universität, Erlangen, Germany; Institute Ruđer Bošković, Division of Physical Chemistry, Zagreb, Croatia. Electronic address: smith@physik.uni-erlangen.de.
Forschungszentrum Jülich · DEUniversity of Stuttgart · DECentre National de la Recherche Scientifique · FRFriedrich-Alexander-Universität Erlangen-Nürnberg · DETechnical University of Munich · DE

Funding

European Research Council 337283
6 · The paper itself

Abstract

Thus far, understanding how the confined cellular environment affects the lifetime of bonds, as well as the extraction of complexation rates, has been a major challenge in studies of cell adhesion. Based on a theoretical description of the growth curves of adhesion domains, we present a new (to our knowledge) method to measure the association rate k(on) of ligand-receptor pairs incorporated into lipid membranes. As a proof of principle, we apply this method to several systems. We find that the k(on) for the interaction of biotin with neutravidin is larger than that for integrin binding to RGD or sialyl Lewis(x) to E-selectin. Furthermore, we find k(on) to be enhanced by membrane fluctuations that increase the probability for encounters between the binders. The opposite effect on k(on) could be attributed to the presence of repulsive polymers that mimic the glycocalyx, which points to two potential mechanisms for controlling the speed of protein complexation during the cell recognition process.

Indexed as

AvidinBiotinCell Adhesion MoleculesCell MembraneKineticsMembrane ProteinsMicroscopyProtein BindingAvidinBiotinCell Adhesion MoleculesMembrane Proteins

Identifiers

PMID25468354
PMCPMC4255260
OpenAlexW2042225912

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.