Evidence map›Paper›PMID 24519400›Full record

ArticleHistochemistry and cell biology2014

Quantitative single-molecule localization microscopy combined with rule-based modeling reveals ligand-induced TNF-R1 reorganization toward higher-order oligomers.

Franziska Fricke, Sebastian Malkusch, Gaby Wangorsch, Johannes F Greiner, Barbara Kaltschmidt, Christian Kaltschmidt, Darius Widera, Thomas Dandekar, Mike Heilemann

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Article in Histochemistry and cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

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  20. Super-Resolution Imaging of Plasma Membrane Proteins with Click Chemistry.Frontiers in cell and developmental biology · 2016
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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

9 authors.

Franziska FrickeInstitute for Physical and Theoretical Chemistry, Johann-Wolfgang-Goethe-University Frankfurt, Frankfurt am Main, Germany.
Sebastian Malkusch
Gaby Wangorsch
Johannes F Greiner
Barbara Kaltschmidt
Christian Kaltschmidt
Darius Widera
Thomas Dandekar
Mike Heilemann

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report on the assembly of tumor necrosis factor receptor 1 (TNF-R1) prior to ligand activation and its ligand-induced reorganization at the cell membrane. We apply single-molecule localization microscopy to obtain quantitative information on receptor cluster sizes and copy numbers. Our data suggest a dimeric pre-assembly of TNF-R1, as well as receptor reorganization toward higher oligomeric states with stable populations comprising three to six TNF-R1. Our experimental results directly serve as input parameters for computational modeling of the ligand-receptor interaction. Simulations corroborate the experimental finding of higher-order oligomeric states. This work is a first demonstration how quantitative, super-resolution and advanced microscopy can be used for systems biology approaches at the single-molecule and single-cell level.

Indexed as

Models, MolecularCell MembraneHeLa CellsHumansLigandsMicroscopy, FluorescenceMolecular ImagingProtein MultimerizationReceptors, Tumor Necrosis Factor, Type IRecombinant ProteinsTumor Necrosis Factor-alphaLigandsReceptors, Tumor Necrosis Factor, Type IRecombinant ProteinsTumor Necrosis Factor-alpha

Identifiers

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Registered trials

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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.