Evidence map›Paper›PMID 22489184›Full record

ArticleInternational journal of molecular sciences2012

The effect of osmolytes on protein fibrillation.

Francesca Macchi, Maike Eisenkolb, Hans Kiefer, Daniel E Otzen

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.2field-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

26 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022
    Review
  10. Taurine Stabilizing Effect on Lysozyme.Life (Basel, Switzerland) · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The biofilm adhesion protein Aap fromThe Journal of biological chemistry · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization.Iranian journal of pharmaceutical research : IJPR · 2019
    Review
  20. 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

4 authors at 2 institutions in 2 countries.

Francesca MacchiiNANO, Center for Insoluble Protein Structures (inSPIN), Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
Maike EisenkolbHochschule Biberach, Pharmaceutical Biotechnology, Hubertus-Liebrecht-Str. 35, D-88400 Biberach, Germany.
Hans KieferHochschule Biberach, Pharmaceutical Biotechnology, Hubertus-Liebrecht-Str. 35, D-88400 Biberach, Germany.
Daniel E OtzeniNANO, Center for Insoluble Protein Structures (inSPIN), Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
Aarhus University · DKUniversity of Applied Sciences Biberach · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Osmolytes are small molecules that are exploited by cells as a protective system against stress conditions. They favour compact protein states which makes them stabilize globular proteins in vitro and promote folding. Conversely, this preference for compact states promotes aggregation of unstructured proteins. Here we combine a brief review of the effect of osmolytes on protein fibrillation with a report of the effect of osmolytes on the unstructured peptide hormone glucagon. Our results show that osmolytes either accelerate the fibrillation kinetics or leave them unaffected, with the exception of the osmolyte taurine. Furthermore, the osmolytes that affected the shape of the fibrillation time profile led to fibrils with different structure as revealed by CD. The structural changes induced by Pro, Ser and choline-O-sulfate could be due to specific osmolytes binding to the peptides, stabilizing an otherwise labile fibrillation intermediate.

Indexed as

Amino AcidsCircular DichroismGlucagonMethylaminesOsmotic PressureProtein AggregatesProtein ConformationProtein FoldingStress, PhysiologicalSugar AlcoholsAmino AcidsGlucagonMethylaminesProtein AggregatesSugar Alcoholsamyloidfibrillation mechanismglucagonpolymorphismtaurine

Identifiers

PMID22489184
PMCPMC3317744
OpenAlexW2139284540

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.