Evidence map›Paper›PMID 23541171›Full record

ReviewTrends in cardiovascular medicine2013

Protein disulfide isomerase as an antithrombotic target.

Robert Flaumenhaft

Abstract readReview
In one paragraph

Review in Trends in cardiovascular medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Assays of Thiol Isomerase Activity.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Rutin-Loaded Silver Nanoparticles With Antithrombotic Function.Frontiers in bioengineering and biotechnology · 2020
    Article
  14. Article
  15. Protein disulfide isomerase enhances tissue factor-dependent thrombin generation.Biochemical and biophysical research communications · 2018
    Article
  16. Article
  17. Review
  18. Discovery of a Novel ERp57 Inhibitor as Antiplatelet Agent from DanshenEvidence-based complementary and alternative medicine : eCAM · 2018
    Article
  19. Advances in vascular thiol isomerase function.Current opinion in hematology · 2017
    Review
  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

1 author at 1 institution in 1 country.

Robert FlaumenhaftDivision of Hemostasis and Thrombosis, Department of Medicine, BIDMC, Harvard Medical School, Boston, MA, USA. Electronic address: rflaumen@bidmc.harvard.edu.
Beth Israel Deaconess Medical Center · US

Funding

Translational Research Skills DevelopmentU54HL112302 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI FURIE, BRUCE · 2012 to 2016
$11.1M
Thrombus Formation In VivoP01HL087203 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI FURIE, BRUCE · 2008 to 2012
$8.8M
Vascular Thiol Isomerases in ThrombosisR01HL136394 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI ITALIANO, JOSEPH E, ZWICKER, JEFFREY · 2017 to 2020
$3.3M
Identification of small molecule inhibitors of protein disulfide isomeraseR03DA032476 · NIDA · BETH ISRAEL DEACONESS MEDICAL CENTER · PI FLAUMENHAFT, ROBERT C · 2011 to 2012
$87k
NHLBI NIH HHS HL87203NHLBI NIH HHS P01 HL087203NHLBI NIH HHS U54 HL112302NHLBI NIH HHS U54HL112302NIDA NIH HHS DA032476NIDA NIH HHS R03 DA032476
6 · The paper itself

Abstract

Protein disulfide isomerase (PDI) is a ubiquitously expressed oxidoreductase required for proper protein folding. It is highly concentrated in the endoplasmic reticulum, but can also be released into the extracellular environment. Several in vivo thrombosis models have demonstrated that vascular PDI secreted by platelets and endothelial cells is essential for normal thrombus formation. Inhibition of extracellular PDI thus represents a potential strategy for antithrombotic therapy. Yet this approach requires the discovery of well-tolerated PDI inhibitors. A recent high-throughput screening identified the commonly ingested flavonoid, quercetin-3-rutinoside, as an inhibitor of PDI. Quercetin-3-rutinoside blocked thrombus formation at concentrations that are commonly ingested as nutritional supplements. The observation that a compound with Generally Recognized As Safe status inhibits PDI and blocks thrombosis in animal models forms a rationale for clinical trials evaluating PDI inhibitors as a new class of antithrombotics.

Indexed as

Protein Disulfide-IsomerasesThrombosisAnimalsBlood PlateletsDrug DiscoveryEndoplasmic ReticulumEndothelial CellsFibrinolytic AgentsHumansModels, CardiovascularRutinFibrinolytic AgentsProtein Disulfide-IsomerasesRutin

Identifiers

PMID23541171
PMCPMC3701031
OpenAlexW1988133576

What OpenQuestion holds

Textmetadata
LicenceTDM
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.