Evidence map›Paper›PMID 23436906›Full record

ArticleMolecular & cellular proteomics : MCP2013

Parallel visualization of multiple protein complexes in individual cells in tumor tissue.

Karl-Johan Leuchowius, Carl-Magnus Clausson, Karin Grannas, Yücel Erbilgin, Johan Botling, Agata Zieba, Ulf Landegren, Ola Söderberg

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 60 citations in OpenAlex.

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  9. Proximity Ligation Assay as a Tool for Antibody Validation in Human Tissues.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2020
    Article
  10. SYNPLA, a method to identify synapses displaying plasticity after learning.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  19. Let There Be Light!Proteomes · 2016
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Karl-Johan LeuchowiusDepartment of Immunology, Genetics and Pathology, Science for Life Laboratory, Rudbeck Laboratory, University of Uppsala, Uppsala, Sweden. leuchowius@wehi.edu.au
Carl-Magnus Clausson
Karin Grannas
Yücel Erbilgin
Johan Botling
Agata Zieba
Ulf Landegren
Ola Söderberg
Science for Life Laboratory · SEIstanbul University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular functions are regulated and executed by complex protein interaction networks. Accordingly, it is essential to understand the interplay between proteins in determining the activity status of signaling cascades. New methods are therefore required to provide information on different protein interaction events at the single cell level in heterogeneous cell populations such as in tissue sections. Here, we describe a multiplex proximity ligation assay for simultaneous visualization of multiple protein complexes in situ. The assay is an enhancement of the original proximity ligation assay, and it is based on using proximity probes labeled with unique tag sequences that can be used to read out which probes, from a pool of probes, have bound a certain protein complex. Using this approach, it is possible to gain information on the constituents of different protein complexes, the subcellular location of the complexes, and how the balance between different complex constituents can change between normal and malignant cells, for example. As a proof of concept, we used the assay to simultaneously visualize multiple protein complexes involving EGFR, HER2, and HER3 homo- and heterodimers on a single-cell level in breast cancer tissue sections. The ability to study several protein complex formations concurrently at single cell resolution could be of great potential for a systems understanding, paving the way for improved disease diagnostics and possibilities for drug development.

Indexed as

Gene Expression Regulation, NeoplasticAnimalsBiopsyBreast NeoplasmsEndothelial CellsErb-b2 Receptor Tyrosine KinasesErbB ReceptorsFemaleHumansImmunoconjugatesMolecular ImagingMolecular ProbesProtein BindingProtein Interaction MappingProtein MultimerizationReceptor, ErbB-3EGFR protein, humanERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesERBB3 protein, humanErbB ReceptorsImmunoconjugatesMolecular ProbesReceptor, ErbB-3

Identifiers

PMID23436906
PMCPMC3675814
OpenAlexW2024551273

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.