Evidence map›Paper›PMID 34934478›Full record

ArticleComputational and structural biotechnology journal2022

The fatty acid site is coupled to functional motifs in the SARS-CoV-2 spike protein and modulates spike allosteric behaviour.

A Sofia F Oliveira, Deborah K Shoemark, Amaurys Avila Ibarra, Andrew D Davidson, Imre Berger, Christiane Schaffitzel, Adrian J Mulholland

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. #COVIDisAirborne: AI-enabled multiscale computational microscopy of delta SARS-CoV-2 in a respiratory aerosol.The international journal of high performance computing applications · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Multifaceted membrane binding head of the SARS-CoV-2 spike protein.Current research in structural biology · 2022
    Article
  16. Article
  17. 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

7 authors at 1 institution in 1 country.

A Sofia F OliveiraCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, UK.
Deborah K ShoemarkBrisSynBio, Life Sciences Building, Tyndall Avenue, Bristol BS8 1TQ, UK.
Amaurys Avila IbarraResearch Software Engineering, Advanced Computing Research Centre, University of Bristol, Bristol BS1 5QD, UK.
Andrew D DavidsonSchool of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Imre BergerBrisSynBio, Life Sciences Building, Tyndall Avenue, Bristol BS8 1TQ, UK.
Christiane SchaffitzelBrisSynBio, Life Sciences Building, Tyndall Avenue, Bristol BS8 1TQ, UK.
Adrian J MulhollandCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, UK.
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Medical Research Council MR/V027506/1Wellcome Trust
6 · The paper itself

Abstract

The SARS-CoV-2 spike protein is the first contact point between the SARS-CoV-2 virus and host cells and mediates membrane fusion. Recently, a fatty acid binding site was identified in the spike (Toelzer

Indexed as

ACE2, angiotensin-converting 2 enzymeCD, connector domainCH, central helixFA, fatty acidFP, fusion peptideFPPR, fusion-peptide proximal regionHR1, heptad repeat 1LA, Linoleic acidMD, Molecular dynamicsMERS, middle east respiratory syndromeNTD, N-terminal domainRBD, receptor binding domainRBM, receptor-binding motifRMB, receptor binding motifSARS-CoV-2, severe acute respiratory syndrome 2SARS, severe acute respiratory syndrome

Identifiers

PMID34934478
PMCPMC8670790
OpenAlexW4226088324

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.