Evidence map›Paper›PMID 32721790›Full record

ReviewBiophysical chemistry2020

Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.

Hirak Chakraborty, Surajit Bhattacharjya

Open access · greenAbstract readReview
In one paragraph

Review in Biophysical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. SARS-CoV-2 FP1 Destabilizes Lipid Membranes and Facilitates Pore Formation.International journal of molecular sciences · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Multifaceted role of natural sources for COVID-19 pandemic as marine drugs.Environmental science and pollution research international · 2022
    Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Virus-Mediated Cell-Cell Fusion.International journal of molecular sciences · 2020
    Review
  17. Article
  18. 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

2 authors at 2 institutions in 2 countries.

Hirak ChakrabortySchool of Chemistry, Sambalpur University, Jyoti Vihar, Burla, Odisha 768 019, India; Centre of Excellence in Natural Products and Therapeutics, Sambalpur University, Jyoti Vihar, Burla, Odisha 768 019, India. Electronic address: hirak@suniv.ac.in.
Surajit BhattacharjyaSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore. Electronic address: surajit@ntu.edu.sg.
Nanyang Technological University · SGSambalpur University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emerging and re-emerging viral diseases are continuous threats to the wellbeing of human life. Previous outbreaks of Severe Acute Respiratory Syndrome (SARS) and Middle East Respiratory Syndrome (MERS had evidenced potential threats of coronaviruses in human health. The recent pandemic due to SARS-CoV-2 is overwhelming and has been going beyond control. Vaccines and antiviral drugs are ungently required to mitigate the pandemic. Therefore, it is important to comprehend the mechanistic details of viral infection process. The fusion between host cell and virus being the first step of infection, understanding the fusion mechanism could provide crucial information to intervene the infection process. Interestingly, all enveloped viruses contain fusion protein on their envelope that acts as fusion machine. For coronaviruses, the spike or S glycoprotein mediates successful infection through receptor binding and cell fusion. The cell fusion process requires merging of virus and host cell membranes, and that is essentially performed by the S2 domain of the S glycoprotein. In this review, we have discussed cell fusion mechanism of SARS-CoV-1 from available atomic resolution structures and membrane binding of fusion peptides. We have further discussed about the cell fusion of SARS-CoV-2 in the context of present pandemic situation.

Indexed as

Virus InternalizationBetacoronavirusHumansMembrane FusionProtein DomainsProtein Structure, SecondarySARS-CoV-2Severe acute respiratory syndrome-related coronavirusViral Fusion ProteinsViral Fusion ProteinsCell fusionCOVID-19Fusion peptideFusion proteinSARS-CoV-1SARS-CoV-2

Identifiers

PMID32721790
PMCPMC7375304
OpenAlexW3044652454

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.