Evidence map›Paper›PMID 25818946›Full record

ArticleActa biomaterialia2015

Relevance of glycosylation of S-layer proteins for cell surface properties.

Bernhard Schuster, Uwe B Sleytr

Open access · hybridAbstract read
In one paragraph

Article in Acta biomaterialia, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Engineering Microbial Particles for Next-Generation Biomedical Platforms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Cyanobacterium-Biotechnology reports (Amsterdam, Netherlands) · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The dental plaque biofilm matrix.Periodontology 2000 · 2021
    Review
  11. Review
  12. Review
  13. Article
  14. Electrochemical Biosensors Based on S-Layer Proteins.Sensors (Basel, Switzerland) · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. The S-Layer Protein of the Anammox BacteriumFrontiers in microbiology · 2016
    Article
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 1 institution in 1 country.

Bernhard SchusterInstitute for Synthetic Bioarchitectures, Department of NanoBiotechnology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 11, 1190 Vienna, Austria. Electronic address: bernhard.schuster@boku.ac.at.
Uwe B SleytrInstitute for Biophysics, Department of NanoBiotechnology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 11, 1190 Vienna, Austria. Electronic address: uwe.sleytr@boku.ac.at.
BOKU University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elucidating the building principles and intrinsic features modulating certain water-associated processes (e.g., surface roughness in the nanometer scale, surface hydration and accompanied antifouling property, etc.) of surface structures from (micro)organisms is nowadays a highly challenging task in fields like microbiology, biomimetic engineering and (bio)material sciences. Here, we show for the first time the recrystallization of the wild-type S-layer glycoprotein wtSgsE from Geobacillus stearothermophilus NRS 2004/3a and its recombinantly produced non-glycosylated form, rSgsE, on gold sensor surfaces. Whereas the proteinaceous lattice of the S-layer proteins is forming a rigid layer on the sensor surface, the glycan chains are developing an overall soft, highly dissipative film. Interestingly, to the wtSgsE lattice almost twice the amount of water is bound and/or coupled in comparison with the non-glycosylated rSgsE with the preferred region being the extending glycan residues. The present results are discussed in terms of the effect of the glycan residues on the recrystallization, the adjoining hydration layer, and the nanoscale roughness and fluidic behavior. The latter features may turn out to be one of the most general ones among bacterial and archaeal S-layer lattices.

Indexed as

Membrane FluidityMembranes, ArtificialAdsorptionCell MembraneGlycosylationGoldMaterials TestingMembrane GlycoproteinsGoldMembrane GlycoproteinsMembranes, ArtificialS-layer proteinsBiomimeticsGeneral features of S-layersGlycansHydration layerS-layer (glyco)proteins

Identifiers

PMID25818946
PMCPMC4414373
OpenAlexW2094428443

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.