Evidence map›Paper›PMID 31952341›Full record

ReviewInternational journal of molecular sciences2020

Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases.

Marie-Claire Méchin, Hidenari Takahara, Michel Simon

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.5field-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

40 citing papers in PubMed, 59 citations in OpenAlex.

  1. Trial
  2. Review
  3. Unveiling nuclear localization signals in human arginine deiminase proteins.Protein science : a publication of the Protein Society · 2026
    Article
  4. Immune functions of the esophagus.The Journal of allergy and clinical immunology · 2026
    Review
  5. Article
  6. The oesophagus as an immune organ.Nature reviews. Gastroenterology & hepatology · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Small molecule activates citrullination through targeting PAD2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  14. Deimination in epidermal barrier and hair formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  15. Characterizing citrullination by mass spectrometry-based proteomics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  16. Transcriptomic analysis of PADI4 target genes during multi-lineage differentiation of embryonic stem cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  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

3 authors at 2 institutions in 2 countries.

Marie-Claire MéchinUDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Paul Sabatier, Université de Toulouse Midi-Pyrénées, U1056, Toulouse 31059, France.
Hidenari TakaharaUniversity of Ibaraki, School of Agriculture, Ibaraki 300-0393, Japan.
Michel SimonUDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Paul Sabatier, Université de Toulouse Midi-Pyrénées, U1056, Toulouse 31059, France.
Université Toulouse III - Paul Sabatier · FRIbaraki University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deimination, also known as citrullination, corresponds to the conversion of the amino acid arginine, within a peptide sequence, into the non-standard amino acid citrulline. This post-translational modification is catalyzed by a family of calcium-dependent enzymes called peptidylarginine deiminases (PADs). Deimination is implicated in a growing number of physiological processes (innate and adaptive immunity, gene regulation, embryonic development, etc.) and concerns several human diseases (rheumatoid arthritis, neurodegenerative diseases, female infertility, cancer, etc.). Here, we update the involvement of PADs in both the homeostasis of skin and skin diseases. We particularly focus on keratinocyte differentiation and the epidermal barrier function, and on hair follicles. Indeed, alteration of PAD activity in the hair shaft is responsible for two hair disorders, the uncombable hair syndrome and a particular form of inflammatory scarring alopecia, mainly affecting women of African ancestry.

Indexed as

Gene Expression RegulationProtein Processing, Post-TranslationalCitrullinationHomeostasisHumansIsoenzymesKeratinocytesProtein-Arginine DeiminasesSkinSkin DiseasesSkin Physiological PhenomenaIsoenzymesProtein-Arginine Deiminasesalopeciacitrullinationdifferentiationepidermishairkeratinocytepeptidylarginine deiminaseposttranslational modification

Identifiers

PMID31952341
PMCPMC7014782
OpenAlexW2999527302

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.