Evidence map›Paper›PMID 33615316›Full record

ArticleAdvanced nanobiomed research2021

Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy.

Yang Xin, Guido Grundmeier, Adrian Keller

Open access · goldAbstract read
In one paragraph

Article in Advanced nanobiomed research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 31% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Light-Induced Transformation of Virus-Like Particles on TiOACS applied materials & interfaces · 2024
    Article
  2. Article
  3. Adsorption of Ferritin at Nanofaceted AlInternational journal of molecular sciences · 2023
    Article
  4. Review
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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.

Yang XinTechnical and Macromolecular Chemistry Paderborn University Warburger Str. 100 Paderborn 33098 Germany.
Guido GrundmeierTechnical and Macromolecular Chemistry Paderborn University Warburger Str. 100 Paderborn 33098 Germany.ORCID 0000-0003-2550-4048
Adrian KellerTechnical and Macromolecular Chemistry Paderborn University Warburger Str. 100 Paderborn 33098 Germany.ORCID 0000-0001-7139-3110
Paderborn University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ongoing coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represents a serious threat to the health of millions of people. Respiratory viruses such as SARS-CoV-2 can be transmitted via airborne and fomite routes. The latter requires virion adsorption at abiotic surfaces and most likely involves the SARS-CoV-2 spike protein subunit 1 (S1), which is the outermost point of its envelope. Understanding S1 spike protein interaction with fomite surfaces thus represents an important milestone on the road to fighting the spread of COVID-19. Herein, high-speed atomic force microscopy (HS-AFM) is used to monitor the adsorption of the SARS-CoV-2 spike protein S1 at Al

Indexed as

Al2O3biointerfaceshigh-speed atomic force microscopySARS-CoV-2TiO2

Identifiers

PMID33615316
PMCPMC7883093
OpenAlexW4205959278

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.