Evidence map›Paper›PMID 19384417›Full record

ArticlePloS one2009

Molecular identification and expression analysis of filaggrin-2, a member of the S100 fused-type protein family.

Zhihong Wu, Britta Hansmann, Ulf Meyer-Hoffert, Regine Gläser, Jens-Michael Schröder

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 129 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Influence of Calcium Ions on the Membrane Binding of S100B Protein.Langmuir : the ACS journal of surfaces and colloids · 2025
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  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Relevance of Coding Variation inJID innovations : skin science from molecules to population health · 2023
    Article
  14. Review
  15. Genetic/Protein Association of Atopic Dermatitis and Tooth Agenesis.International journal of molecular sciences · 2023
    Review
  16. Article
  17. Article
  18. Anti-Frontiers in microbiology · 2023
    Review
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Zhihong WuDepartment of Dermatology, University Hospital of Schleswig-Holstein, Kiel, Germany.
Britta Hansmann
Ulf Meyer-Hoffert
Regine Gläser
Jens-Michael Schröder
University Hospital Schleswig-Holstein · DEUniversity of Lübeck · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genes of the S100 fused-type protein (SFTP) family are clustered within the epidermal differentiation complex and encode essential components that maintain epithelial homeostasis and barrier functions. Recent genetic studies have shown that mutations within the gene encoding the SFTP filaggrin cause ichthyosis vulgaris and are major predisposing factors for atopic dermatitis. As a vital component of healthy skin, filaggrin is also a precursor of natural moisturizing factors. Here we present the discovery of a member of this family, designated as filaggrin-2 (FLG2) that is expressed in human skin. The FLG2 gene encodes a histidine- and glutamine-rich protein of approximately 248 kDa, which shares common structural features with other SFTP members, in particular filaggrin. We found that FLG2 transcripts are present in skin, thymus, tonsils, stomach, testis and placenta. In cultured primary keratinocytes, FLG2 mRNA expression displayed almost the same kinetics as that of filaggrin following Ca(2+) stimulation, suggesting an important role in molecular regulation of epidermal terminal differentiation. We provide evidences that like filaggrin, FLG2 is initially expressed by upper granular cells, proteolytically processed and deposited in the stratum granulosum and stratum corneum (SC) layers of normal epidermis. Thus, FLG2 and filaggrin may have overlapping and perhaps synergistic roles in the formation of the epidermal barrier, protecting the skin from environmental insults and the escape of moisture by offering precursors of natural moisturizing factors.

Indexed as

Amino Acid SequenceCells, CulturedDermatitis, AtopicFilaggrin ProteinsHumansIntermediate Filament ProteinsMolecular Sequence DataMultigene FamilyPsoriasisRNA, MessengerS100 ProteinsSequence Homology, Amino AcidFilaggrin ProteinsFLG2 protein, humanFLG protein, humanIntermediate Filament ProteinsRNA, MessengerS100 Proteins

Identifiers

PMID19384417
PMCPMC2668185
OpenAlexW2080179721

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.