ArticleStructure (London, England : 1993)2011
Mechanism of fibrin(ogen) forced unfolding.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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.
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.
Who cites it
57 citing papers in PubMed, 139 citations in OpenAlex.
- Insights into fibrinogen mechanics under cyclic high-strain loading.Biophysical journal · 2026Article
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Loading causes molecular damage in fibrin fibers.Soft matter · 2025Article
- Review
- A novel pathogenic variant in the fibrinogen gamma chain gene p.Glu275Lys causes congenital hypofibrinogenemia.Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis · 2025Article
- Biomaterials in Postoperative Adhesion Barriers and Uterine Tissue Engineering.Gels (Basel, Switzerland) · 2025Review
- Structural Mechanisms of Forced Unfolding of Double-Stranded Fibrin Oligomers.The journal of physical chemistry. B · 2025Article
- Rupture mechanics of blood clot fibrin fibers: A coarse-grained model study.Journal of the mechanics and physics of solids · 2025Article
- Fibrinogen αC-region acts as a functional safety latch: Implications for a fibrin biomechanical behaviour model.Acta biomaterialia · 2024Article
- Hyperelasticity of blood clots: Bridging the gap between microscopic and continuum scales.Journal of the mechanics and physics of solids · 2024Article
- Mechanical fatigue testing in silico: Dynamic evolution of material properties of nanoscale biological particles.Acta biomaterialia · 2023Article
- Multiscale mechanical characterization and computational modeling of fibrin gels.Acta biomaterialia · 2023Article
- Fibrin protofibril packing and clot stability are enhanced by extended knob-hole interactions and catch-slip bonds.Blood advances · 2022Article
- Exploring the Effect of Mechanical Anisotropy of Protein Structures in the Unfoldase Mechanism of AAA+ Molecular Machines.Nanomaterials (Basel, Switzerland) · 2022Article
- Review
- Engineered Molecular Therapeutics Targeting Fibrin and the Coagulation System: a Biophysical Perspective.Biophysical reviews · 2022Review
- Microscale structural changes of individual fibrin fibers during fibrinolysis.Acta biomaterialia · 2022Article
- Strength, deformability and toughness of uncrosslinked fibrin fibers from theoretical reconstruction of stress-strain curves.Acta biomaterialia · 2021Article
- Development of a mesoscopic framework spanning nanoscale protofibril dynamics to macro-scale fibrin clot formation.Journal of the Royal Society, Interface · 2021Article
- Physical forces regulating hemostasis and thrombosis: Vessels, cells, and molecules in illustrated review.Research and practice in thrombosis and haemostasis · 2021Review
Corrections and comments
- Commented on by
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Fibrinogen, upon enzymatic conversion to monomeric fibrin, provides the building blocks for fibrin polymer, the scaffold of blood clots and thrombi. Little has been known about the force-induced unfolding of fibrin(ogen), even though it is the foundation for the mechanical and rheological properties of fibrin, which are essential for hemostasis. We determined mechanisms and mapped the free energy landscape of the elongation of fibrin(ogen) monomers and oligomers through combined experimental and theoretical studies of the nanomechanical properties of fibrin(ogen), using atomic force microscopy-based single-molecule unfolding and simulations in the experimentally relevant timescale. We have found that mechanical unraveling of fibrin(ogen) is determined by the combined molecular transitions that couple stepwise unfolding of the γ chain nodules and reversible extension-contraction of the α-helical coiled-coil connectors. These findings provide important characteristics of the fibrin(ogen) nanomechanics necessary to understand the molecular origins of fibrin viscoelasticity at the fiber and whole clot levels.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.