Evidence map›Paper›PMID 39237366›Full record

ArticleLife science alliance2024

Cell-Int: a cell-cell interaction assay to identify native membrane protein interactions.

Thibaud Aymoz-Bressot, Marie Canis, Florian Meurisse, Anne Wijkhuisen, Benoit Favier, Guillaume Mousseau, Anne Dupressoir, Thierry Heidmann, Agathe Bacquin

Abstract read
In one paragraph

Article in Life science alliance, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. The human endogenous retroviral envelope HEMO protein interacts with BACE2: Novel partnership acquired in the primate lineage.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
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.

Thibaud Aymoz-BressotCNRS UMR9196, Laboratory of Molecular Physiology and Pathology of Endogenous and Infectious Retroviruses, Gustave Roussy, Université Paris-Saclay, Villejuif, France.
Marie CanisCNRS UMR9196, Laboratory of Molecular Physiology and Pathology of Endogenous and Infectious Retroviruses, Gustave Roussy, Université Paris-Saclay, Villejuif, France.
Florian MeurisseUniversité Paris-Saclay, Inserm, CEA, Center for Immunology of Viral, Auto-immune, Hematological and Bacterial Diseases (IMVA-HB/IDMIT), Paris, France.
Anne WijkhuisenUniversité Paris-Saclay, CEA, INRAE, Médicaments et Technologies pour la Santé (MTS), Gif-sur-Yvette, France.ORCID 0009-0000-0738-0446
Benoit FavierUniversité Paris-Saclay, Inserm, CEA, Center for Immunology of Viral, Auto-immune, Hematological and Bacterial Diseases (IMVA-HB/IDMIT), Paris, France.ORCID 0000-0001-9191-6273
Guillaume MousseauVIROXIS, Gustave Roussy, Villejuif, France.
Anne DupressoirCNRS UMR9196, Laboratory of Molecular Physiology and Pathology of Endogenous and Infectious Retroviruses, Gustave Roussy, Université Paris-Saclay, Villejuif, France.
Thierry HeidmannCNRS UMR9196, Laboratory of Molecular Physiology and Pathology of Endogenous and Infectious Retroviruses, Gustave Roussy, Université Paris-Saclay, Villejuif, France.
Agathe BacquinVIROXIS, Gustave Roussy, Villejuif, France agathe.bacquin@gustaveroussy.fr.ORCID 0009-0000-1976-8747

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intercellular protein-protein interactions (PPIs) have pivotal roles in biological functions and diseases. Membrane proteins are therefore a major class of drug targets. However, studying such intercellular PPIs is challenging because of the properties of membrane proteins. Current methods commonly use purified or modified proteins that are not physiologically relevant and hence might mischaracterize interactions occurring in vivo. Here, we describe Cell-Int: a cell interaction assay for studying plasma membrane PPIs. The interaction signal is measured through conjugate formation between two populations of cells each expressing either a ligand or a receptor. In these settings, membrane proteins are in their native environment thus being physiologically relevant. Cell-Int has been applied to the study of diverse protein partners, and enables to investigate the inhibitory potential of blocking antibodies, as well as the retargeting of fusion proteins for therapeutic development. The assay was also validated for screening applications and could serve as a platform for identifying new protein interactors.

Indexed as

Cell CommunicationCell MembraneMembrane ProteinsProtein BindingProtein Interaction MappingAnimalsBiological AssayHEK293 CellsHumansMembrane Proteins

Identifiers

PMID39237366
PMCPMC11377309

What OpenQuestion holds

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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.