Evidence map›Paper›PMID 22489132›Full record

ReviewInternational journal of molecular sciences2012

Pro-inflammatory S100A8 and S100A9 proteins: self-assembly into multifunctional native and amyloid complexes.

Thomas Vogl, Anna L Gharibyan, Ludmilla A Morozova-Roche

Open access · goldAbstract readReview
In one paragraph

Review 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 118 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed, 4 pooled it
4.8field-weighted citation impact, top 4% 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

118 citing papers in PubMed, 4 syntheses or guidelines pooled it, 206 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Calprotectin (S100A8/S100A9): a key protein between inflammation and cancer.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2018
    Pooled it
  4. Pooled it
  5. Diagnostic Value of Synovial Fluid Biomarkers for Periprosthetic Joint Infection: A Prospective, Double-blind Trial.Medical science monitor : international medical journal of experimental and clinical research · 2023
    Trial
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Virtual Probing on the Influence of CaCell biochemistry and biophysics · 2025
    Article
  20. Article

58 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Thomas VoglInstitute of Immunology, University of Muenster, Röntgenstr. 21, 48149 Muenster, Germany.
Anna L GharibyanDepartment of Medical Biochemistry and Biophysics, Umea University, SE-901 87 Umea, Sweden.
Ludmilla A Morozova-RocheDepartment of Medical Biochemistry and Biophysics, Umea University, SE-901 87 Umea, Sweden.
Umeå University · SEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S100A8 and S100A9 are EF-hand Ca(2+) binding proteins belonging to the S100 family. They are abundant in cytosol of phagocytes and play critical roles in numerous cellular processes such as motility and danger signaling by interacting and modulating the activity of target proteins. S100A8 and S100A9 expression levels increased in many types of cancer, neurodegenerative disorders, inflammatory and autoimmune diseases and they are implicated in the numerous disease pathologies. The Ca(2+) and Zn(2+)-binding properties of S100A8/A9 have a pivotal influence on their conformation and oligomerization state, including self-assembly into homo- and heterodimers, tetramers and larger oligomers. Here we review how the unique chemical and conformational properties of individual proteins and their structural plasticity at the quaternary level account for S100A8/A9 functional diversity. Additional functional diversification occurs via non-covalent assembly into oligomeric and fibrillar amyloid complexes discovered in the aging prostate and reproduced in vitro. This process is also regulated by Ca(2+)and Zn(2+)-binding and effectively competes with the formation of the native complexes. High intrinsic amyloid-forming capacity of S100A8/A9 proteins may lead to their amyloid depositions in numerous ailments characterized by their elevated expression patterns and have additional pathological significance requiring further thorough investigation.

Indexed as

AmyloidAnimalsCalgranulin ACalgranulin BHumansInflammation MediatorsMultiprotein ComplexesProtein MultimerizationAmyloidCalgranulin ACalgranulin BInflammation MediatorsMultiprotein Complexesamyloidcalcium-bindingcalprotectincancerinflammationS100A8S100A9S100 proteinsself-assembly

Identifiers

PMID22489132
PMCPMC3317694
OpenAlexW2017656054

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.