Evidence map›Paper›PMID 29262365›Full record

ArticleBiophysical journal2017

Interfacial Properties of N

Anaïs Bénarouche, Johnny Habchi, Alain Cagna, Ofelia Maniti, Agnès Girard-Egrot, Jean-François Cavalier, Sonia Longhi, Frédéric Carrière

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. 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

8 authors at 4 institutions in 1 country.

Anaïs BénaroucheAix-Marseille University, CNRS, Enzymologie Interfaciale et Physiologie de la Lipolyse UMR 7282, Marseille, France; TECLIS Scientific, Tassin, France.
Johnny HabchiAix-Marseille University, CNRS, Architecture et Fonction des Macromolécules Biologiques (AFMB) UMR 7257, Marseille, France.
Alain CagnaTECLIS Scientific, Tassin, France.
Ofelia ManitiUniversité de Lyon, Université Claude Bernard Lyon 1, CNRS, INSA Lyon, CPE Lyon, UMR 5246 Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Equipe Génie Enzymatique, Membranes Biomimétiques et Assemblages Supramoléculaires (GEMBAS), Villeurbanne, France.
Agnès Girard-EgrotUniversité de Lyon, Université Claude Bernard Lyon 1, CNRS, INSA Lyon, CPE Lyon, UMR 5246 Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Equipe Génie Enzymatique, Membranes Biomimétiques et Assemblages Supramoléculaires (GEMBAS), Villeurbanne, France.
Jean-François CavalierAix-Marseille University, CNRS, Enzymologie Interfaciale et Physiologie de la Lipolyse UMR 7282, Marseille, France.
Sonia LonghiAix-Marseille University, CNRS, Architecture et Fonction des Macromolécules Biologiques (AFMB) UMR 7257, Marseille, France. Electronic address: sonia.longhi@afmb.univ-mrs.fr.
Frédéric CarrièreAix-Marseille University, CNRS, Enzymologie Interfaciale et Physiologie de la Lipolyse UMR 7282, Marseille, France. Electronic address: carriere@imm.cnrs.fr.
Aix-Marseille Université · FRCentre National de la Recherche Scientifique · FRInstitut de Chimie et Biochimie Moléculaires et Supramoléculaires · FRInstitut National des Sciences Appliquées de Lyon · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) lack stable secondary and tertiary structure under physiological conditions in the absence of their biological partners and thus exist as dynamic ensembles of interconverting conformers, often highly soluble in water. However, in some cases, IDPs such as the ones involved in neurodegenerative diseases can form protein aggregates and their aggregation process may be triggered by the interaction with membranes. Although the interfacial behavior of globular proteins has been extensively studied, experimental data on IDPs at the air/water (A/W) and water/lipid interfaces are scarce. We studied here the intrinsically disordered C-terminal domain of the Hendra virus nucleoprotein (N

Indexed as

AdsorptionAirIntrinsically Disordered ProteinsMuramidaseNucleocapsid ProteinsNucleoproteinsPhosphatidylcholinesProtein ConformationViral ProteinsWaterIntrinsically Disordered ProteinsMuramidaseNucleocapsid Proteinsnucleoprotein, Hendra virusNucleoproteinsPhosphatidylcholinesViral ProteinsWater

Identifiers

PMID29262365
PMCPMC5770565
OpenAlexW2780939308

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.