Evidence map›Paper›PMID 30072441›Full record

ArticleJournal of cell science2018

ProLIF - quantitative integrin protein-protein interactions and synergistic membrane effects on proteoliposomes.

Nicola De Franceschi, Mitro Miihkinen, Hellyeh Hamidi, Jonna Alanko, Anja Mai, Laura Picas, Camilo Guzmán, Daniel Lévy, Peter Mattjus, Benjamin T Goult and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. A membrane protein display platform for receptor interactome discovery.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  2. Review
  3. Article
  4. Integrins as biomechanical sensors of the microenvironment.Nature reviews. Molecular cell biology · 2019
    Review
  5. Review
  6. 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

12 authors at 4 institutions in 3 countries.

Nicola De FranceschiTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Mitro MiihkinenTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Hellyeh HamidiTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Jonna AlankoTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Anja MaiTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Laura PicasInstitut Curie, PSL Research University, UMR 168, Centre de Recherche, 75248 Paris, France.
Camilo GuzmánTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Daniel LévyInstitut Curie, PSL Research University, UMR 168, Centre de Recherche, 75248 Paris, France.
Peter MattjusBiochemistry, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.
Benjamin T GoultSchool of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Bruno GoudInstitut Curie, PSL Research University, UMR 168, Centre de Recherche, 75248 Paris, France.
Johanna IvaskaTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20520 Turku, Finland Johanna.ivaska@utu.fi.ORCID 0000-0002-6295-6556
Åbo Akademi University · FIUniversité Paris Sciences et Lettres · FRCentre National de la Recherche Scientifique · FRUniversity of Kent · GB

Funding

European Research Council 615258
6 · The paper itself

Abstract

Integrin transmembrane receptors control a wide range of biological interactions by triggering the assembly of large multiprotein complexes at their cytoplasmic interface. Diverse methods have been used to investigate interactions between integrins and intracellular proteins, and predominantly include peptide-based pulldowns and biochemical immuno-isolations from detergent-solubilised cell lysates. However, quantitative methods to probe integrin-protein interactions in a more biologically relevant context where the integrin is embedded within a lipid bilayer have been lacking. Here, we describe 'protein-liposome interactions by flow cytometry' (denoted ProLIF), a technique to reconstitute recombinant integrin transmembrane domains (TMDs) and cytoplasmic tail (CT) fragments in liposomes as individual subunits or as αβ heterodimers and, via flow cytometry, allow rapid and quantitative measurement of protein interactions with these membrane-embedded integrins. Importantly, the assay can analyse binding of fluorescent proteins directly from cell lysates without further purification steps. Moreover, the effect of membrane composition, such as PI(4,5)P

Indexed as

Cell AdhesionCell MembraneCytoplasmDimerizationFlow CytometryHumansIntegrinsLiposomesProtein BindingProteolipidsIntegrinsLiposomesProteolipidsproteoliposomesIntegrinsLiposomesProtein–lipid interactionsProtein–protein interactions

Identifiers

PMID30072441
PMCPMC6398480
OpenAlexW2885878706

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.