Evidence map›Paper›PMID 31776280›Full record

ReviewJournal of virology2020

Breaking the Convention: Sialoglycan Variants, Coreceptors, and Alternative Receptors for Influenza A Virus Entry.

Umut Karakus, Marie O Pohl, Silke Stertz

Open access · greenAbstract readReview
In one paragraph

Review in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 64 citations in OpenAlex.

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  17. H3N2 influenza A virus gradually adapts to human-type receptor binding and entry specificity after the start of the 1968 pandemic.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

3 authors at 1 institution in 1 country.

Umut Karakus *Institute of Medical Virology, University of Zurich, Zurich, Switzerland.
Marie O Pohl *Institute of Medical Virology, University of Zurich, Zurich, Switzerland.
Silke StertzInstitute of Medical Virology, University of Zurich, Zurich, Switzerland stertz.silke@virology.uzh.ch.
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influenza A virus (IAV) envelope protein hemagglutinin binds α2,6- or α2,3-linked sialic acid as a host cell receptor. Bat IAV subtypes H17N10 and H18N11 form an exception to this rule and do not bind sialic acid but enter cells via major histocompatibility complex (MHC) class II. Here, we review current knowledge on IAV receptors with a focus on sialoglycan variants, protein coreceptors, and alternative receptors that impact IAV attachment and internalization beyond the well-described sialic acid binding.

Indexed as

AnimalsChiropteraHEK293 CellsHemagglutinin Glycoproteins, Influenza VirusHistocompatibility Antigens Class IIHumansInfluenza A virusN-Acetylneuraminic AcidNeuraminidaseReceptors, VirusVirus AttachmentVirus InternalizationHemagglutinin Glycoproteins, Influenza VirusHistocompatibility Antigens Class IIN-Acetylneuraminic AcidNeuraminidaseReceptors, Virusinfluenza virusreceptorviral entry

Identifiers

PMID31776280
PMCPMC6997770
OpenAlexW2990192582

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.