Evidence map›Paper›PMID 35196165›Full record

ReviewAmerican journal of physiology. Cell physiology2022

Is heparan sulfate a target for inhibition of RNA virus infection?

Jiaxin Ling, Jinlin Li, Asifa Khan, Åke Lundkvist, Jin-Ping Li

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Cell physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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  8. Article
  9. Pathogens that infect mammalian cells via sulfonated glycosaminoglycans.Frontiers in cellular and infection microbiology · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Article
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  16. 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

5 authors at 1 institution in 1 country.

Jiaxin LingDepartment of Medical Biochemistry and Microbiology, The Biomedical Center, University of Uppsala, Uppsala, Sweden.
Jinlin LiDepartment of Medical Biochemistry and Microbiology, The Biomedical Center, University of Uppsala, Uppsala, Sweden.ORCID 0000-0002-8998-9278
Asifa KhanDepartment of Medical Biochemistry and Microbiology, The Biomedical Center, University of Uppsala, Uppsala, Sweden.
Åke LundkvistDepartment of Medical Biochemistry and Microbiology, The Biomedical Center, University of Uppsala, Uppsala, Sweden.
Jin-Ping LiDepartment of Medical Biochemistry and Microbiology, The Biomedical Center, University of Uppsala, Uppsala, Sweden.
Uppsala University · SE

Funding

European Union Agency for Network and Information Security (ENISA) 874735 (VEO)Swedish Cancer Foundation CAN211417PjVetenskapsrådet (VR) 2020-05759; 2021-01094
6 · The paper itself

Abstract

Heparan sulfate (HS) is a linear polysaccharide attached to a core protein, forming heparan sulfate proteoglycans (HSPGs) that are ubiquitously expressed on the surface of almost all mammalian cells and the extracellular matrix. HS orchestrates the binding of various signal molecules to their receptors, thus regulating many biological processes, including homeostasis, metabolism, and various pathological processes. Due to its wide distribution and negatively charged properties, HS is exploited by many viruses as a cofactor to attach to host cells. Therefore, inhibition of the interaction between virus and HS is proposed as a promising approach to mitigate viral infection, including SARS-CoV-2. In this review, we summarize the interaction manners of HS with viruses with focus on significant pathogenic RNA viruses, including alphaviruses, flaviviruses, and coronaviruses. We also provide an overview of the challenges we may face when using HS mimetics as antivirals for clinical treatment. More studies are needed to provide a further understanding of the interplay between HS and viruses both in vitro and in vivo, which will favor the development of specific antiviral inhibitors.

Indexed as

COVID-19AnimalsHeparan SulfateHeparan Sulfate ProteoglycansMammalsProteinsSARS-CoV-2Heparan SulfateHeparan Sulfate ProteoglycansProteinsalphaviruscoronavirusflavivirusheparan sulfateSARS-CoV-2virus

Identifiers

PMID35196165
PMCPMC8977144
OpenAlexW4213440192

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.