Evidence map›Paper›PMID 34804050›Full record

ReviewFrontiers in immunology2021

Peptidylarginine Deiminase 2 in Host Immunity: Current Insights and Perspectives.

Zhenyu Wu, Patrick Li, Yuzi Tian, Wenlu Ouyang, Jessie Wai-Yan Ho, Hasan B Alam, Yongqing Li

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Citrullination in tumor immunity and therapy.The Journal of clinical investigation · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Protein citrullination: inhibition, identification and insertion.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  14. Small molecule activates citrullination through targeting PAD2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  15. Article
  16. Article
  17. Regulating Neutrophil PAD4/NOX-Dependent Cerebrovasular Thromboinflammation.International journal of biological sciences · 2023
    Article
  18. Review
  19. 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

7 authors at 4 institutions in 2 countries.

Zhenyu WuDepartment of Surgery, University of Michigan Hospital, Ann Arbor, MI, United States.
Patrick LiDepartment of Surgery, University of Michigan Hospital, Ann Arbor, MI, United States.
Yuzi TianDepartment of Surgery, University of Michigan Hospital, Ann Arbor, MI, United States.
Wenlu OuyangDepartment of Surgery, University of Michigan Hospital, Ann Arbor, MI, United States.
Jessie Wai-Yan HoDepartment of Surgery, Feinberg School of Medicine, Northwestern University, Chicago, IL, United States.
Hasan B AlamDepartment of Surgery, Feinberg School of Medicine, Northwestern University, Chicago, IL, United States.
Yongqing LiDepartment of Surgery, University of Michigan Hospital, Ann Arbor, MI, United States.
University of Michigan–Ann Arbor · USNorthwestern University · USNYU Langone Health · USXiangya Hospital Central South University · CN

Funding

PAD2 and CitH3 in Pathogenesis of Sepsis-induced ALIR01HL155116 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ALAM, HASAN B, LI, YONGQING · 2021 to 2024
$2.1M
Novel Cilia Trafficking MechanismsR01DK084725 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARGOLIS, BENJAMIN L · 2009 to 2010
$702k
NHLBI NIH HHS R01 HL155116NIDDK NIH HHS R01 DK084725
6 · The paper itself

Abstract

Peptidylarginine deiminases (PADs) are a group of enzymes that catalyze post-translational modifications of proteins by converting arginine residues into citrullines. Among the five members of the PAD family, PAD2 and PAD4 are the most frequently studied because of their abundant expression in immune cells. An increasing number of studies have identified PAD2 as an essential factor in the pathogenesis of many diseases. The successes of preclinical research targeting PAD2 highlights the therapeutic potential of PAD2 inhibition, particularly in sepsis and autoimmune diseases. However, the underlying mechanisms by which PAD2 mediates host immunity remain largely unknown. In this review, we will discuss the role of PAD2 in different types of cell death signaling pathways and the related immune disorders contrasted with functions of PAD4, providing novel therapeutic strategies for PAD2-associated pathology.

Indexed as

AnimalsHumansImmune System DiseasesInfectionsLeukocytesMacrophagesNeoplasmsProtein-Arginine Deiminase Type 2Protein-Arginine Deiminase Type 2autoimmune diseasesNETosisPAD2pyroptosissepsis

Identifiers

PMID34804050
PMCPMC8599989
OpenAlexW3213273764

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.