Evidence map›Paper›PMID 34778199›Full record

ArticleFrontiers in chemistry2021

Characterization of Natural and Synthetic Sialoglycans Targeting the Hemagglutinin-Neuraminidase of Mumps Virus.

Rosa Ester Forgione, Cristina Di Carluccio, Francesco Milanesi, Marie Kubota, Ferran Fabregat Nieto, Antonio Molinaro, Takao Hashiguchi, Oscar Francesconi, Roberta Marchetti, Alba Silipo

Open access · goldAbstract read
In one paragraph

Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 81% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Rosa Ester ForgioneDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Naples, Italy.
Cristina Di CarluccioDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Naples, Italy.
Francesco MilanesiDepartment of Chemistry "Ugo Schiff" and INSTM, University of Florence Polo Scientifico e Tecnologico, Florence, Italy.
Marie KubotaDepartment of Virology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
Ferran Fabregat NietoDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Naples, Italy.
Antonio MolinaroDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Naples, Italy.
Takao HashiguchiLaboratory of Medical Virology, Department of Virus Research, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Oscar FrancesconiDepartment of Chemistry "Ugo Schiff" and INSTM, University of Florence Polo Scientifico e Tecnologico, Florence, Italy.
Roberta MarchettiDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Naples, Italy.
Alba SilipoDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Naples, Italy.
University of Naples Federico II · ITKyoto University · JPKyushu University · JPNational Interuniversity Consortium of Materials Science and Technology · ITUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inhibition of surface viral glycoproteins offers great potential to hamper the attachment of viruses to the host cells surface and the spreading of viral infection. Mumps virus (MuV) is the etiological agent of the mumps infectious disease and causes a wide spectrum of mild to severe symptoms due to the inflammation of the salivary glands. Here we focus our attention on the hemagglutinin-neuraminidase (HN) isolated from MuV SBL-1 strain. We describe the molecular features of host sialoglycans recognition by HN protein by means of NMR, fluorescence assays and computational studies. Furthermore, we also describe the synthesis of a N-acetylneuraminic acid-derived thiotrisaccharide targeting the viral protein, and the corresponding 3D-complex. Our results provide the basis to improve the design and synthesis of potent viral hemagglutinin-neuraminidase inhibitors.

Indexed as

computational studiesinhibitorsmolecular recognitionmumpsNMR

Identifiers

PMID34778199
PMCPMC8578797
OpenAlexW3209063763

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.