Evidence map›Paper›PMID 38297113›Full record

ArticleScientific reports2024

Internal fibrinolysis of fibrin clots is driven by pore expansion.

Rebecca A Risman, Bradley Paynter, Victoria Percoco, Mitali Shroff, Brittany E Bannish, Valerie Tutwiler

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

  1. A grading system of dynamic fibrinolysis resistance in sepsis associates with ICU outcomes.American journal of respiratory and critical care medicine · 2026
    Article
  2. Article
  3. Toward improved thrombolysis in ischemic stroke: targeting nonfibrin components.Research and practice in thrombosis and haemostasis · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Deconstructing fibrin(ogen) structure.Journal of thrombosis and haemostasis : JTH · 2025
    Review
  10. Protofibril packing density of individual fibers alters fibrinolysis.Research and practice in thrombosis and haemostasis · 2025
    Article
  11. Article
  12. Article
  13. Dependence of clot structure and fibrinolysis on apixaban and clotting activator.Research and practice in thrombosis and haemostasis · 2024
    Article
  14. Review
  15. Article
  16. 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

6 authors at 2 institutions in 1 country.

Rebecca A RismanDepartment of Biomedical Engineering, Rutgers University, 599 Taylor Road, Piscataway, NJ, 08854, USA.
Bradley PaynterDepartment of Mathematics and Statistics, University of Central Oklahoma, Edmond, USA.
Victoria PercocoDepartment of Biomedical Engineering, Rutgers University, 599 Taylor Road, Piscataway, NJ, 08854, USA.
Mitali ShroffDepartment of Cell Biology and Neuroscience, Rutgers University, Piscataway, USA.
Brittany E BannishDepartment of Mathematics and Statistics, University of Central Oklahoma, Edmond, USA.
Valerie TutwilerDepartment of Biomedical Engineering, Rutgers University, 599 Taylor Road, Piscataway, NJ, 08854, USA. valerie.tutwiler@rutgers.edu.
Rutgers, The State University of New Jersey · USUniversity of Central Oklahoma · US

Funding

Rutgers Biotechnology Training ProgramT32GM135141 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ANN M. STOCK, Martin L Yarmush · 2020 to 2026
$3.5M
Systematic multidisciplinary approach to study traumatic bleeding as a complex structural and biomechanical problemR00HL148646 · NHLBI · RUTGERS, THE STATE UNIV OF N.J. · PI TUTWILER, VALERIE · 2020 to 2022
$747k
NHLBI NIH HHS R00 HL148646NIGMS NIH HHS T32 GM135141NIH HHS R00HL148646-01NIH HHS T32 GM135141
6 · The paper itself

Abstract

Blood clots, which are composed of blood cells and a stabilizing mesh of fibrin fibers, are critical in cessation of bleeding following injury. However, their action is transient and after performing their physiological function they must be resolved through a process known as fibrinolysis. Internal fibrinolysis is the degradation of fibrin by the endogenous or innate presence of lytic enzymes in the bloodstream; under healthy conditions, this process regulates hemostasis and prevents bleeding or clotting. Fibrin-bound tissue plasminogen activator (tPA) converts nearby plasminogen into active plasmin, which is bound to the fibrin network, breaking it down into fibrin degradation products and releasing the entrapped blood cells. It is poorly understood how changes in the fibrin structure and lytic protein ratios influence the biochemical regulation and behavior of internal fibrinolysis. We used turbidity kinetic tracking and microscopy paired with mathematical modeling to study fibrin structure and lytic protein ratios that restrict internal fibrinolysis. Analysis of simulations and experiments indicate that fibrinolysis is driven by pore expansion of the fibrin network. We show that this effect is strongly influenced by the ratio of fibrin:tPAwhen compared to absolute tPA concentration. Thus, it is essential to consider relative protein concentrations when studying internal fibrinolysis both experimentally and in the clinic. An improved understanding of effective internal lysis can aid in development of better therapeutics for the treatment of bleeding and thrombosis.

Indexed as

FibrinolysisThrombosisBlood CoagulationFibrinHumansTissue Plasminogen ActivatorFibrinTissue Plasminogen Activator

Identifiers

PMID38297113
PMCPMC10830469
OpenAlexW4392786793

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.