Evidence map›Paper›PMID 33392200›Full record

ArticleFrontiers in cell and developmental biology2020

Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation.

Camille Albrecht, Andrey S Kuznetsov, Aline Appert-Collin, Zineb Dhaideh, Maïté Callewaert, Yaroslav V Bershatsky, Anatoly S Urban, Eduard V Bocharov, Dominique Bagnard, Stéphanie Baud and 8 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

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  10. Antiviral Peptides as Anti-Influenza Agents.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

18 authors at 7 institutions in 2 countries.

Camille AlbrechtUniversité de Reims Champagne-Ardenne, Reims, France.
Andrey S KuznetsovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Aline Appert-CollinUniversité de Reims Champagne-Ardenne, Reims, France.
Zineb DhaidehUniversité de Reims Champagne-Ardenne, Reims, France.
Maïté CallewaertUniversité de Reims Champagne-Ardenne, Reims, France.
Yaroslav V BershatskyShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Anatoly S UrbanShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Eduard V BocharovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Dominique BagnardUniversité de Strasbourg, Strasbourg, France.
Stéphanie BaudUniversité de Reims Champagne-Ardenne, Reims, France.
Sébastien BlaiseUniversité de Reims Champagne-Ardenne, Reims, France.
Béatrice Romier-CrouzetUniversité de Reims Champagne-Ardenne, Reims, France.
Roman G EfremovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Manuel DauchezUniversité de Reims Champagne-Ardenne, Reims, France.
Laurent DucaUniversité de Reims Champagne-Ardenne, Reims, France.
Marc GueroultUniversité de Reims Champagne-Ardenne, Reims, France.
Pascal MauriceUniversité de Reims Champagne-Ardenne, Reims, France.
Amar BennasrouneUniversité de Reims Champagne-Ardenne, Reims, France.
Université de Reims Champagne-Ardenne · FRCentre National de la Recherche Scientifique · FRMoscow Institute of Physics and Technology · RUInserm · FRInstitute of Bioorganic Chemistry · RUMatrice Extracellulaire et Dynamique Cellulaire MEDyCNational Research University Higher School of Economics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialidases, or neuraminidases, are involved in several human disorders such as neurodegenerative, infectious and cardiovascular diseases, and cancers. Accumulative data have shown that inhibition of neuraminidases, such as NEU1 sialidase, may be a promising pharmacological target, and selective inhibitors of NEU1 are therefore needed to better understand the biological functions of this sialidase. In the present study, we designed interfering peptides (IntPep) that target a transmembrane dimerization interface previously identified in human NEU1 that controls its membrane dimerization and sialidase activity. Two complementary strategies were used to deliver the IntPep into cells, either flanked to a TAT sequence or non-tagged for solubilization in detergent micelles. Combined with molecular dynamics simulations and heteronuclear nuclear magnetic resonance (NMR) studies in membrane-mimicking environments, our results show that these IntPep are able to interact with the dimerization interface of human NEU1, to disrupt membrane NEU1 dimerization and to strongly decrease its sialidase activity at the plasma membrane. In conclusion, we report here new selective inhibitors of human NEU1 of strong interest to elucidate the biological functions of this sialidase.

Indexed as

interfering peptidesmembrane protein dimerizationneuraminidase-1sialidase activitytransmembrane domain

Identifiers

PMID33392200
PMCPMC7772355
OpenAlexW3110661703

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.