Evidence map›Paper›PMID 35901239›Full record

ReviewPhysiological reviews2023

Protease-activated receptors in health and disease.

Chloe J Peach, Laura E Edgington-Mitchell, Nigel W Bunnett, Brian L Schmidt

Open access · greenAbstract readReview
In one paragraph

Review in Physiological reviews, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
13.0field-weighted citation impact, top 1% 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

74 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Effect of gut bacterial extracellular vesicles on angiogenic potential and vascular integrity: positive and negative aspects.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. MMP1 and PRSS23 induce PARCommunications biology · 2026
    Article
  13. Article
  14. Review
  15. mbioRxiv : the preprint server for biology · 2026
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Electrophysiological and Proteomic Evidence of Protease-Mediated Pro-nociceptive Signaling in Inflammatory Bowel Disease Patients.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article

14 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

4 authors at 3 institutions in 2 countries.

Chloe J PeachDepartment of Molecular Pathobiology, College of Dentistry, New York University, New York, New York.
Laura E Edgington-MitchellDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia.ORCID 0000-0002-6810-6149
Nigel W BunnettDepartment of Molecular Pathobiology, College of Dentistry, New York University, New York, New York.ORCID 0000-0003-3367-0644
Brian L SchmidtDepartment of Molecular Pathobiology, College of Dentistry, New York University, New York, New York.
New York University · USCenter for Clinical Research (United States) · USThe University of Melbourne · AU

Funding

Targeting Endosomal Receptors for Treatment of Chronic PainR01DE029951 · NIDCR · NEW YORK UNIVERSITY · PI BUNNETT, NIGEL W, SCHMIDT, BRIAN L · 2020 to 2024
$4.7M
Protease/PAR2/TRPV4 Axis and Oral Cancer PainR01DE026806 · NIDCR · NEW YORK UNIVERSITY · PI BUNNETT, NIGEL W, SCHMIDT, BRIAN L · 2018 to 2022
$3.9M
Endosomal Platforms for Signaling PainR01NS102722 · NINDS · NEW YORK UNIVERSITY · PI NIGEL W BUNNETT, Brian L Schmidt · 2017 to 2026
$3.4M
Trafficking-Dependent Signaling of Pain by Protease-Activated ReceptorsR01DK118971 · NIDDK · NEW YORK UNIVERSITY · PI BUNNETT, NIGEL W, SCHMIDT, BRIAN L · 2018 to 2021
$3.2M
NIDCR NIH HHS R01 DE026806NIDCR NIH HHS R01 DE029951NIDDK NIH HHS R01 DK118971NINDS NIH HHS R01 NS102722
6 · The paper itself

Abstract

Proteases are signaling molecules that specifically control cellular functions by cleaving protease-activated receptors (PARs). The four known PARs are members of the large family of G protein-coupled receptors. These transmembrane receptors control most physiological and pathological processes and are the target of a large proportion of therapeutic drugs. Signaling proteases include enzymes from the circulation; from immune, inflammatory epithelial, and cancer cells; as well as from commensal and pathogenic bacteria. Advances in our understanding of the structure and function of PARs provide insights into how diverse proteases activate these receptors to regulate physiological and pathological processes in most tissues and organ systems. The realization that proteases and PARs are key mediators of disease, coupled with advances in understanding the atomic level structure of PARs and their mechanisms of signaling in subcellular microdomains, has spurred the development of antagonists, some of which have advanced to the clinic. Herein we review the discovery, structure, and function of this receptor system, highlight the contribution of PARs to homeostatic control, and discuss the potential of PAR antagonists for the treatment of major diseases.

Indexed as

Receptors, Proteinase-ActivatedSignal TransductionHomeostasisHumansPeptide HydrolasesReceptors, G-Protein-CoupledPeptide HydrolasesReceptors, G-Protein-CoupledReceptors, Proteinase-Activatedantagonistsdiseasehomeostasisproteasesreceptors

Identifiers

PMID35901239
PMCPMC9662810
OpenAlexW4288434597

What Socratic holds

Textmetadata
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 Socratic graph.