ReviewTH open : companion journal to thrombosis and haemostasis2025
A Contemporary Review of Plasminogen Activator Inhibitor Type 1: Structure, Function, Genetic Architecture, and Intracellular/Extracellular Roles.
Review in TH open : companion journal to thrombosis and haemostasis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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.
Who cites it
5 citing papers in PubMed.
- SERPINE1/PAI-1 in Skeletal Degeneration: A Proposed Context-Dependent Framework for Bone Remodeling Regulation.Calcified tissue international · 2026Review
- A Novel Signaling Driven by the Stem Cell Marker ALDH1A3 Promotes Glioblastoma Cell Mobility.Cells · 2026Article
- Aptamer-mediated modulation of PAI-1 function reveals a novel mechanism for restoring fibrinolytic balance.NAR molecular medicine · 2026Article
- Plasminogen activator inhibitor-1 as an oncologic target: biology, therapeutic inhibitors, and clinical translation.Frontiers in oncology · 2026Review
- The expanding landscape of adipokines: emerging roles of PAI-1 and vaspin in cardiometabolic diseases.Frontiers in endocrinology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasminogen activator inhibitor type 1 (PAI-1) is the key regulator of the fibrinolytic system, thereby acting as a potent mediator in thrombosis. Plasminogen activators such as PAI-1 mediate the conversion of the inactive zymogen plasminogen to plasmin, an active serine protease. As a member of the serpin superfamily, the highly conserved structure of PAI-1 is critical for its regulatory function. This review elucidates PAI-1 structure, function, and genetic architecture, and then discusses intracellular and extracellular functions that have broad implications for proliferative signaling and cell death, angiogenesis, cellular transit, and emerging roles in cancer biology. By understanding the complex and elaborate mechanism of PAI-1 in the fibrinolytic system and as a biomarker, PAI-1 may have broad implications across many disease states not related to its historical roles in fibrinolysis and thrombosis.
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Registered trials
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.