Evidence map›Paper›PMID 33676233›Full record

ReviewCurrent opinion in chemical biology2021

Chemical biology of protein citrullination by the protein A arginine deiminases.

Santanu Mondal, Paul R Thompson

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.0field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Protein citrullination: inhibition, identification and insertion.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  16. Small molecule activates citrullination through targeting PAD2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  17. Development of LB244, an Irreversible STING Antagonist.Journal of the American Chemical Society · 2023
    Article
  18. Review
  19. Current insights into the role of citrullination in thrombosis.Current opinion in chemical biology · 2023
    Review
  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

2 authors at 1 institution in 1 country.

Santanu MondalDepartment of Biochemistry and Molecular Pharmacology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA; Program in Chemical Biology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA.
Paul R ThompsonDepartment of Biochemistry and Molecular Pharmacology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA; Program in Chemical Biology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA. Electronic address: Paul.Thompson@umassmed.edu.
UMass Memorial Health Care · US

Funding

Chemical probes to decipher PAD biologyR35GM118112 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Paul R Thompson · 2016 to 2026
$9.5M
NIGMS NIH HHS R35 GM118112
6 · The paper itself

Abstract

Citrullination is a post-translational modification (PTM) that converts peptidyl-arginine into peptidyl-citrulline; citrullination is catalyzed by the protein arginine deiminases (PADs). This PTM is associated with several physiological processes, including the epigenetic regulation of gene expression, neutrophil extracellular trap formation, and DNA-damage induced apoptosis. Notably, aberrant protein citrullination is relevant to several autoimmune and neurodegenerative diseases and certain forms of cancer. As such, the PADs are promising therapeutic targets. In this review, we discuss recent advances in the development of PAD inhibitors and activity-based probes, the development and use of citrulline-specific probes in chemoproteomic applications, and methods to site-specifically incorporate citrulline into proteins.

Indexed as

AnimalsArginineAutoimmune DiseasesCatalysisCitrullinationCitrullineEpigenesis, GeneticHumansNeoplasmsNeurodegenerative DiseasesProtein-Arginine DeiminasesProtein BindingProtein ConformationProtein Processing, Post-TranslationalProteinsArginineCitrullineProtein-Arginine DeiminasesProteinsActivity-based protein profilingAutocitrullinationCitrulline incorporationInhibitorPost-translational modificationsProtein arginine deiminase (PAD)

Identifiers

PMID33676233
PMCPMC8384633
OpenAlexW3133565544

What OpenQuestion holds

Textmetadata
LicenceTDM
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.