Evidence map›Paper›PMID 39536819›Full record

ReviewJournal of thrombosis and haemostasis : JTH2025

Deconstructing fibrin(ogen) structure.

Rebecca A Risman, Mehmet Sen, Valerie Tutwiler, Nathan E Hudson

Abstract readReview
In one paragraph

Review in Journal of thrombosis and haemostasis : JTH, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Toward improved thrombolysis in ischemic stroke: targeting nonfibrin components.Research and practice in thrombosis and haemostasis · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Homocysteinylation of Fibrinogen: A Post-Translational Link to Thrombosis.International journal of molecular sciences · 2025
    Review
  11. Review
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.

Rebecca A RismanDepartment of Biomedical Engineering, Rutgers University, New Brunswick, New Jersey, USA. Electronic address: https://twitter.com/rebecca_risman.
Mehmet SenDepartment of Biology and Biochemistry, University of Houston, Houston, Texas, USA.
Valerie TutwilerDepartment of Biomedical Engineering, Rutgers University, New Brunswick, New Jersey, USA. Electronic address: https://twitter.com/vatutwiler.
Nathan E HudsonDepartment of Physics, East Carolina University, Greenville, North Carolina, USA. Electronic address: hudsonn16@ecu.edu.

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
MIRA R35: Fibrin(ogen) in regulating health and diseaseR35GM155242 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI Valerie Tutwiler · 2024 to 2026
$1.2M
Identifying the function of the Fibrin(ogen) alpha-C connector regionR15HL148842 · NHLBI · EAST CAROLINA UNIVERSITY · PI HUDSON, NATHAN · 2019 to 2024
$893k
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
Identifying structural differences between fibrinogen and fibrin to provide novel therapeutic targetsR15HL150666 · NHLBI · EAST CAROLINA UNIVERSITY · PI OFFENBACHER, ADAM · 2020 to 2020
$441k
NHLBI NIH HHS R00 HL148646NHLBI NIH HHS R15 HL148842NHLBI NIH HHS R15 HL150666NIGMS NIH HHS R35 GM155242NIGMS NIH HHS T32 GM135141
6 · The paper itself

Abstract

Fibrinogen and its insoluble degradation product fibrin are pivotal plasma proteins that play important roles in blood coagulation, wound healing, and immune responses. This review highlights research from the last 24 months connecting our progressing view of fibrin(ogen)'s structure, and in particular its conformational flexibility and posttranslational modifications, to its (patho)physiologic roles, molecular interactions, mechanical properties, use as a biomaterial, and potential as a therapeutic target. Recent work suggests that fibrinogen structure is highly dynamic, sampling multiple conformations, which may explain its myriad physiologic functions and the presence of cryptic binding sites. Investigations into fibrin clot structure elucidated the impact of posttranslational modifications, therapeutic interventions, and pathologic conditions on fibrin network morphology, offering insights into thrombus formation and embolization. Studies exploring the mechanical properties of fibrin reveal its response to blood flow and platelet-driven contraction, offering implications for clot stability and embolization risk. Moreover, advancements in tissue engineering leverage fibrin's biocompatibility and customizable properties for diverse applications, from wound healing to tissue regeneration and biomaterial interactions. These findings underscore the structural origins of fibrin(ogen)'s multifaceted roles and its potential as a target for therapeutic interventions.

Indexed as

Blood CoagulationFibrinFibrinogenAnimalsHumansProtein ConformationProtein Processing, Post-TranslationalStructure-Activity RelationshipThrombosisTissue EngineeringWound HealingFibrinFibrinogenblood clotfibrinfibrinogenmechanicstissue engineering

Identifiers

PMID39536819
PMCPMC11786978

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.