Evidence map›Paper›PMID 20966169›Full record

ArticleBlood2011

The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies.

Colin Longstaff, Craig Thelwell, Stella C Williams, Marta M C G Silva, László Szabó, Krasimir Kolev

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 5% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 142 citations in OpenAlex.

  1. Guideline
  2. Trial
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  6. Article
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  8. Article
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  11. Review
  12. Protofibril packing density of individual fibers alters fibrinolysis.Research and practice in thrombosis and haemostasis · 2025
    Article
  13. Article
  14. Article
  15. Connecting impaired fibrinolysis and dyslipidemia.Research and practice in thrombosis and haemostasis · 2024
    Article
  16. Review
  17. Article
  18. Altered fibrinogen γ-chain cross-linking in mutant fibrinogen-γJournal of thrombosis and haemostasis : JTH · 2023
    Article
  19. Fibrinolysis: an illustrated review.Research and practice in thrombosis and haemostasis · 2023
    Review
  20. Article

7 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Colin LongstaffNational Institute for Biological Standards and Control, South Mimms, UK. colin.longstaff@nibsc.hpa.org.uk
Craig Thelwell
Stella C Williams
Marta M C G Silva
László Szabó
Krasimir Kolev
National Institute for Biological Standards and Control · GBHUN-REN Research Centre for Natural Sciences · HUSemmelweis University · HU

Funding

British Heart Foundation F5/06/021Wellcome Trust 083174
6 · The paper itself

Abstract

Regulation of tissue-type plasminogen activator (tPA) depends on fibrin binding and fibrin structure. tPA structure/function relationships were investigated in fibrin formed by high or low thrombin concentrations to produce a fine mesh and small pores, or thick fibers and coarse structure, respectively. Kinetics studies were performed to investigate plasminogen activation and fibrinolysis in the 2 types of fibrin, using wild-type tPA (F-G-K1-K2-P, F and K2 binding), K1K1-tPA (F-G-K1-K1-P, F binding), and delF-tPA (G-K1-K2-P, K2 binding). There was a trend of enzyme potency of tPA > K1K1-tPA > delF-tPA, highlighting the importance of the finger domain in regulating activity, but the differences were less apparent in fine fibrin. Fine fibrin was a better surface for plasminogen activation but more resistant to lysis. Scanning electron and confocal microscopy using orange fluorescent fibrin with green fluorescent protein-labeled tPA variants showed that tPA was strongly associated with agglomerates in coarse but not in fine fibrin. In later lytic stages, delF-tPA-green fluorescent protein diffused more rapidly through fibrin in contrast to full-length tPA, highlighting the importance of finger domain-agglomerate interactions. Thus, the regulation of fibrinolysis depends on the starting nature of fibrin fibers and complex dynamic interaction between tPA and fibrin structures that vary over time.

Indexed as

FibrinFibrinolysisHumansKineticsMicroscopy, ConfocalMicroscopy, Electron, ScanningPlasminogenProtein BindingThrombinTissue Plasminogen ActivatorFibrinPlasminogenThrombinTissue Plasminogen Activator

Identifiers

PMID20966169
PMCPMC3031486
OpenAlexW1970454941

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.