Evidence map›Paper›PMID 36614009›Full record

ArticleInternational journal of molecular sciences2022

Investigation of the Fuzzy Complex between RSV Nucleoprotein and Phosphoprotein to Optimize an Inhibition Assay by Fluorescence Polarization.

Silva Khodjoyan, Deborha Morissette, Fortune Hontonnou, Luis Checa Ruano, Charles-Adrien Richard, Olivier Sperandio, Jean-François Eléouët, Marie Galloux, Philippe Durand, Stéphanie Deville-Foillard and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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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

11 authors at 2 institutions in 1 country.

Silva KhodjoyanInstitut de Chimie des Substances Naturelles, CNRS, Université Paris Saclay, F-91190 Gif-sur-Yvette, France.
Deborha MorissetteInstitut de Chimie des Substances Naturelles, CNRS, Université Paris Saclay, F-91190 Gif-sur-Yvette, France.
Fortune HontonnouVirologie et Immunologie Moléculaires, INRAE, Université Paris-Saclay, F-78350 Jouy-en-Josas, France.
Luis Checa RuanoStructural Bioinformatics Unit, Department of Structural Biology and Chemistry, Institut Pasteur, Université de Paris, CNRS UMR3528, F-75015 Paris, France.ORCID 0000-0001-6437-5379
Charles-Adrien RichardVirologie et Immunologie Moléculaires, INRAE, Université Paris-Saclay, F-78350 Jouy-en-Josas, France.
Olivier SperandioStructural Bioinformatics Unit, Department of Structural Biology and Chemistry, Institut Pasteur, Université de Paris, CNRS UMR3528, F-75015 Paris, France.
Jean-François EléouëtVirologie et Immunologie Moléculaires, INRAE, Université Paris-Saclay, F-78350 Jouy-en-Josas, France.
Marie GallouxVirologie et Immunologie Moléculaires, INRAE, Université Paris-Saclay, F-78350 Jouy-en-Josas, France.ORCID 0000-0001-7477-8489
Philippe DurandInstitut de Chimie des Substances Naturelles, CNRS, Université Paris Saclay, F-91190 Gif-sur-Yvette, France.
Stéphanie Deville-FoillardInstitut de Chimie des Substances Naturelles, CNRS, Université Paris Saclay, F-91190 Gif-sur-Yvette, France.
Christina SizunInstitut de Chimie des Substances Naturelles, CNRS, Université Paris Saclay, F-91190 Gif-sur-Yvette, France.ORCID 0000-0002-5760-2614
Centre National de la Recherche Scientifique · FRUniversité Paris-Saclay · FR

Funding

Agence Nationale de la Recherche ANR-19-CE18-0012-01LabEx LERMIT PepRSV
6 · The paper itself

Abstract

The interaction between Respiratory Syncytial Virus phosphoprotein P and nucleoprotein N is essential for the formation of the holo RSV polymerase that carries out replication. In vitro screening of antivirals targeting the N-P protein interaction requires a molecular interaction model, ideally consisting of a complex between N protein and a short peptide corresponding to the C-terminal tail of the P protein. However, the flexibility of C-terminal P peptides as well as their phosphorylation status play a role in binding and may bias the outcome of an inhibition assay. We therefore investigated binding affinities and dynamics of this interaction by testing two N protein constructs and P peptides of different lengths and composition, using nuclear magnetic resonance and fluorescence polarization (FP). We show that, although the last C-terminal Phe

Indexed as

NucleoproteinsRespiratory Syncytial Virus, HumanFluorescence PolarizationPeptidesPhosphoproteinsNucleoproteinsPeptidesPhosphoproteinsB-cyano BODIPYsfluorescence anisotropyfuzzy complexnuclear magnetic resonancenucleoproteinphosphoproteinPPI inhibitionprotein–protein interactionreplication complexrespiratory syncytial virus

Identifiers

PMID36614009
PMCPMC9820559
OpenAlexW4313328583

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.