Evidence map›Paper›PMID 32351895›Full record

ReviewFrontiers in oncology2020

Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?

Camille Albrecht, Aline Appert-Collin, Dominique Bagnard, Sébastien Blaise, Béatrice Romier-Crouzet, Roman G Efremov, Hervé Sartelet, Laurent Duca, Pascal Maurice, Amar Bennasroune

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in oncology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  11. SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights.International journal of molecular sciences · 2022
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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

10 authors at 5 institutions in 2 countries.

Camille AlbrechtUniversité de Reims Champagne-Ardenne, Reims, France.
Aline Appert-CollinUniversité de Reims Champagne-Ardenne, Reims, France.
Dominique BagnardUniversité de Strasbourg, Strasbourg, France.
Sébastien BlaiseUniversité de Reims Champagne-Ardenne, Reims, France.
Béatrice Romier-CrouzetUniversité de Reims Champagne-Ardenne, Reims, France.
Roman G EfremovM. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Hervé SarteletUniversité de Reims Champagne-Ardenne, Reims, France.
Laurent DucaUniversité de Reims Champagne-Ardenne, Reims, France.
Pascal MauriceUniversité de Reims Champagne-Ardenne, Reims, France.
Amar BennasrouneUniversité de Reims Champagne-Ardenne, Reims, France.
Matrice Extracellulaire et Dynamique Cellulaire MEDyCCentre National de la Recherche Scientifique · FRBiopathologie de la myéline, neuroprotection et stratégies thérapeutiquesNational Research University Higher School of Economics · RUUniversité de Reims Champagne-Ardenne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular functions are regulated by extracellular signals such as hormones, neurotransmitters, matrix ligands, and other chemical or physical stimuli. Ligand binding on its transmembrane receptor induced cell signaling and the recruitment of several interacting partners to the plasma membrane. Nowadays, it is well-established that the transmembrane domain is not only an anchor of these receptors to the membrane, but it also plays a key role in receptor dimerization and activation. Indeed, interactions between transmembrane helices are associated with specific biological activity of the proteins as cell migration, proliferation, or differentiation. Overexpression or constitutive dimerization (due notably to mutations) of these transmembrane receptors are involved in several physiopathological contexts as cancers. The transmembrane domain of tyrosine kinase receptors as ErbB family proteins (implicated in several cancers as HER2 in breast cancer) or other receptors as Neuropilins has been described these last years as a target to inhibit their dimerization/activation using several strategies. In this review, we will focus on the strategy which consists in using peptides to disturb in a specific manner the interactions between transmembrane domains and the signaling pathways (induced by ligand binding) of these receptors involved in cancer. This approach can be extended to inhibit other transmembrane protein dimerization as neuraminidase-1 (the catalytic subunit of elastin receptor complex), Discoidin Domain Receptor 1 (a tyrosine kinase receptor activated by type I collagen) or G-protein coupled receptors (GPCRs) which are involved in cancer processes.

Indexed as

cancerspeptide delivery strategyprotein-protein interactiontransmembrane peptidestransmembrane protein dimerization inhibition

Identifiers

PMID32351895
PMCPMC7174899
OpenAlexW3017350708

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.