Evidence map›Paper›PMID 37885881›Full record

ReviewFrontiers in immunology2023

Structural insights into the biological functions of the long pentraxin PTX3.

Anna Margherita Massimino, Filippo Emanuele Colella, Barbara Bottazzi, Antonio Inforzato

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2023. 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
3.9field-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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Analysis of MSX1, RYK, NFκB p65, and CCL4 Proteins andInternational journal of molecular sciences · 2025
    Article
  9. Article
  10. Review
  11. Review
  12. Pentraxin 3 as a Prognostic Biomarker in Aneurysmal Subarachnoid Hemorrhage.Medical science monitor : international medical journal of experimental and clinical research · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Anna Margherita MassiminoDepartment of Biomedical Sciences, Humanitas University, Pieve Emanuele, Italy.
Filippo Emanuele ColellaDepartment of Biomedical Sciences, Humanitas University, Pieve Emanuele, Italy.
Barbara BottazziLaboratory of Cellular and Humoral Innate Immunity, IRCCS Humanitas Research Hospital, Rozzano, Italy.
Antonio InforzatoDepartment of Biomedical Sciences, Humanitas University, Pieve Emanuele, Italy.
Humanitas University · ITIRCCS Humanitas Research Hospital · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Soluble pattern recognition molecules (PRMs) are a heterogenous group of proteins that recognize pathogen- and danger-associated molecular patterns (PAMPs and DAMPs, respectively), and cooperate with cell-borne receptors in the orchestration of innate and adaptive immune responses to pathogenic insults and tissue damage. Amongst soluble PRMs, pentraxins are a family of highly conserved proteins with distinctive structural features. Originally identified in the early 1990s as an early inflammatory gene, PTX3 is the prototype of long pentraxins. Unlike the short pentraxin C reactive protein (CRP), whose expression is mostly confined to the liver, PTX3 is made by several immune and non-immune cells at sites of infection and inflammation, where it intercepts fundamental aspects of infection immunity, inflammation, and tissue remodeling. Of note, PTX3 cross talks to components of the complement system to control cancer-related inflammation and disposal of pathogens. Also, it is an essential component of inflammatory extracellular matrices (ECMs) through crosslinking of hyaluronic acid and turn-over of provisional fibrin networks that assemble at sites of tissue injury. This functional diversity is mediated by unique structural characteristics whose fine details have been unveiled only recently. Here, we revisit the structure/function relationships of this long pentraxin in light of the most recent advances in its structural biology, with a focus on the interplay with complement and the emerging roles as a component of the ECM. Differences to and similarities with the short pentraxins are highlighted and discussed.

Indexed as

C-Reactive ProteinImmunity, InnateSerum Amyloid P-ComponentComplement System ProteinsHumansInflammationPentraxinsComplement System ProteinsC-Reactive ProteinPentraxinsSerum Amyloid P-Componentcomplementextracellular matrixpattern recognition molecules (PRM)pentraxinsPTX3structure

Identifiers

PMID37885881
PMCPMC10598717
OpenAlexW4387454458

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.