Evidence map›Paper›PMID 23305734›Full record

ReviewBlood2013

Mechanisms of fibrin polymerization and clinical implications.

John W Weisel, Rustem I Litvinov

Abstract readReview
In one paragraph

Review in Blood, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 219 papers.

0numbers the graph read from it
0cells of the map it votes in
219citing papers in PubMed
–field-weighted citation impact
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

219 citing papers in PubMed.

  1. Method Comparison of Three Automated D-Dimer Assays.Diagnostics (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Potential Role of Polyphenols in Platelet Aggregation and Blood Coagulation.Journal of cardiovascular development and disease · 2026
    Review
  12. Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen.Protein science : a publication of the Protein Society · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

159 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

2 authors.

John W WeiselDepartment of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. weisel@mail.med.upenn.edu
Rustem I Litvinov

Funding

STRUCTURAL STUDIES OF BLOOD CLOTTING PROTEINSR01HL030954 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 1985 to 2008
$3.0M
Structural origin of fibrin clot mechanical propertiesR01HL090774 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 2009 to 2012
$1.6M
Structural origin of fibrin clot mechanical propertiesR56HL090774 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 2014 to 2014
$408k
NHLBI NIH HHS HL030954NHLBI NIH HHS HL090774NHLBI NIH HHS R01 HL030954NHLBI NIH HHS R01 HL090774NHLBI NIH HHS R56 HL090774
6 · The paper itself

Abstract

Research on all stages of fibrin polymerization, using a variety of approaches including naturally occurring and recombinant variants of fibrinogen, x-ray crystallography, electron and light microscopy, and other biophysical approaches, has revealed aspects of the molecular mechanisms involved. The ordered sequence of fibrinopeptide release is essential for the knob-hole interactions that initiate oligomer formation and the subsequent formation of 2-stranded protofibrils. Calcium ions bound both strongly and weakly to fibrin(ogen) have been localized, and some aspects of their roles are beginning to be discovered. Much less is known about the mechanisms of the lateral aggregation of protofibrils and the subsequent branching to yield a 3-dimensional network, although the αC region and B:b knob-hole binding seem to enhance lateral aggregation. Much information now exists about variations in clot structure and properties because of genetic and acquired molecular variants, environmental factors, effects of various intravascular and extravascular cells, hydrodynamic flow, and some functional consequences. The mechanical and chemical stability of clots and thrombi are affected by both the structure of the fibrin network and cross-linking by plasma transglutaminase. There are important clinical consequences to all of these new findings that are relevant for the pathogenesis of diseases, prophylaxis, diagnosis, and treatment.

Indexed as

AnimalsBiopolymersBlood Coagulation DisordersFibrinHumansPolymerizationBiopolymersFibrin

Identifiers

PMID23305734
PMCPMC3591795

What OpenQuestion holds

Textmetadata
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.