ReviewCell biochemistry and biophysics2007
A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers.
Review in Cell biochemistry and biophysics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
What it found
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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.
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Who cites it
98 citing papers in PubMed.
- Biomimetic Fibrin Matrix Modulates Early Human Follicular Growth Dynamics in a Bioengineered Artificial Ovary Derived from Cryopreserved Tissue: In Vitro Morphometric Assessment.International journal of molecular sciences · 2026Article
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Elastic analysis bridges structure and dynamics of an AAA+ molecular motor.PLoS computational biology · 2025Article
- Revisiting the biophysical aspects of extracellular-matrix-mimicking hydrogels: what cells seeBiomaterials science · 2025Review
- Construction and Bioengineering of Human Bioprosthetic Ovaries from Cryopreserved Ovarian Tissue.International journal of molecular sciences · 2025Review
- Structural Mechanisms of Forced Unfolding of Double-Stranded Fibrin Oligomers.The journal of physical chemistry. B · 2025Article
- Advances in Fibrin-Based Bioprinting for Skin Tissue Regeneration: Exploring Design, and Innovative Approaches.Biomedical materials & devices (New York, N.Y.) · 2025Article
- Comprehensive analysis of scRNA-seq and bulk RNA-seq reveals the non-cardiomyocytes heterogeneity and novel cell populations in dilated cardiomyopathy.Journal of translational medicine · 2025Article
- Molecular and functional MRI enables detection of cardiac fibrosis and evaluation of treatment response afterTheranostics · 2025Article
- 3D-Printed Polymeric Biomaterials for Health Applications.Advanced healthcare materials · 2025Review
- Rupture mechanics of blood clots: Influence of fibrin network structure on the rupture resistance.Acta biomaterialia · 2024Article
- Matrix Architecture and Mechanics Regulate Myofibril Organization, Costamere Assembly, and Contractility in Engineered Myocardial Microtissues.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Fibrinogen αC-region acts as a functional safety latch: Implications for a fibrin biomechanical behaviour model.Acta biomaterialia · 2024Article
- Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.ACS nano · 2024Article
- Characterization of Atlantic Forest Tucum (Plants (Basel, Switzerland) · 2024Article
- Structure, Properties and Degradation of Self-Assembled Fibrinogen Nanofiber Scaffolds.ACS applied bio materials · 2024Article
- Article
- Clots reveal anomalous elastic behavior of fiber networks.Science advances · 2024Article
- Soft ferroelectret ultrasound receiver for targeted peripheral neuromodulation.Nature communications · 2023Article
- Biomechanics, Energetics, and Structural Basis of Rupture of Fibrin Networks.Advanced healthcare materials · 2023Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
In the past few years a great deal of progress has been made in studying the mechanical and structural properties of biological protein fibers. Here, we compare and review the stiffness (Young's modulus, E) and breaking strain (also called rupture strain or extensibility, epsilon(max)) of numerous biological protein fibers in light of the recently reported mechanical properties of fibrin fibers. Emphasis is also placed on the structural features and molecular mechanisms that endow biological protein fibers with their respective mechanical properties. Generally, stiff biological protein fibers have a Young's modulus on the order of a few Gigapascal and are not very extensible (epsilon(max) < 20%). They also display a very regular arrangement of their monomeric units. Soft biological protein fibers have a Young's modulus on the order of a few Megapascal and are very extensible (epsilon(max) > 100%). These soft, extensible fibers employ a variety of molecular mechanisms, such as extending amorphous regions or unfolding protein domains, to accommodate large strains. We conclude our review by proposing a novel model of how fibrin fibers might achieve their extremely large extensibility, despite the regular arrangement of the monomeric fibrin units within a fiber. We propose that fibrin fibers accommodate large strains by two major mechanisms: (1) an alpha-helix to beta-strand conversion of the coiled coils; (2) a partial unfolding of the globular C-terminal domain of the gamma-chain.
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