Evidence map›Paper›PMID 25386620›Full record

ReviewTheScientificWorldJournal2014

Functional stability of plasminogen activator inhibitor-1.

Songul Yasar Yildiz, Pinar Kuru, Ebru Toksoy Oner, Mehmet Agirbasli

Open access · goldAbstract readReview
In one paragraph

Review in TheScientificWorldJournal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.7field-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

38 citing papers in PubMed, 102 citations in OpenAlex.

  1. Plasminogen Activator Inhibitor-1 is Internalized by Endothelial Cells via A Pinocytosis-Like Mechanism and Evades Degradation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Article
  3. Article
  4. Reversing PAI-1 deficiency in blood using mRNA lipid nanoparticles.Molecular therapy. Methods & clinical development · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Changes of new coagulation markers in healthy pregnant women and establishment of reference intervals in Changsha.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Unbiased proteomics identifies plasminogen activator inhibitor-1 as a negative regulator of endothelial nitric oxide synthase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Songul Yasar YildizDepartment of Bioengineering, Marmara University, 34722 Istanbul, Turkey.ORCID 0000-0001-8875-3637
Pinar KuruDepartment of Cardiology, Faculty of Medicine, Marmara University, Selimiye M. Tibbiye C. No. 38, Haydarpasa, 34668 Istanbul, Turkey.
Ebru Toksoy OnerDepartment of Bioengineering, Marmara University, 34722 Istanbul, Turkey.
Mehmet AgirbasliDepartment of Cardiology, Faculty of Medicine, Marmara University, Selimiye M. Tibbiye C. No. 38, Haydarpasa, 34668 Istanbul, Turkey.
Marmara University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasminogen activator inhibitor-1 (PAI-1) is the main inhibitor of plasminogen activators, such as tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA), and a major regulator of the fibrinolytic system. PAI-1 plays a pivotal role in acute thrombotic events such as deep vein thrombosis (DVT) and myocardial infarction (MI). The biological effects of PAI-1 extend far beyond thrombosis including its critical role in fibrotic disorders, atherosclerosis, renal and pulmonary fibrosis, type-2 diabetes, and cancer. The conversion of PAI-1 from the active to the latent conformation appears to be unique among serpins in that it occurs spontaneously at a relatively rapid rate. Latency transition is believed to represent a regulatory mechanism, reducing the risk of thrombosis from a prolonged antifibrinolytic action of PAI-1. Thus, relying solely on plasma concentrations of PAI-1 without assessing its function may be misleading in interpreting the role of PAI-1 in many complex diseases. Environmental conditions, interaction with other proteins, mutations, and glycosylation are the main factors that have a significant impact on the stability of the PAI-1 structure. This review provides an overview on the current knowledge on PAI-1 especially importance of PAI-1 level and stability and highlights the potential use of PAI-1 inhibitors for treating cardiovascular disease.

Indexed as

HumansKidneyMyocardial InfarctionPlasminogen Activator Inhibitor 1Protein StabilityTissue Plasminogen ActivatorUrokinase-Type Plasminogen ActivatorVenous ThrombosisPlasminogen Activator Inhibitor 1SERPINE1 protein, humanTissue Plasminogen ActivatorUrokinase-Type Plasminogen Activator

Identifiers

PMID25386620
PMCPMC4214104
OpenAlexW2166590594

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.