ArticleScience advances2016
Microscale spatial heterogeneity of protein structural transitions in fibrin matrices.
Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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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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.
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Who cites it
23 citing papers in PubMed.
- Decoupling phase separation and fibrillization preserves activity of biomolecular condensates.Nature communications · 2026Article
- Spatiotemporal evaluation of antithrombotic performance for biomaterials through monitoring β-sheet conformation changes at the blood interface.Bioactive materials · 2026Article
- Loading causes molecular damage in fibrin fibers.Soft matter · 2025Article
- Molecular Creep Induced Fatigue Rupture of Fibrin Clots.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Fatty acid albumin conjugates mechanically weaken and disrupt degradation of fibrin networks.Acta biomaterialia · 2025Article
- Rupture mechanics of blood clots: Influence of fibrin network structure on the rupture resistance.Acta biomaterialia · 2024Article
- 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
- Collagen organization and structure inBiomedical optics express · 2024Article
- Collagen organization and structure inbioRxiv : the preprint server for biology · 2024Article
- Visualizing molecular deformation in fibrin networks under tensile loadingChemical communications (Cambridge, England) · 2023Article
- Minimizing Molecular Misidentification in Imaging Low-Abundance Protein Interactions Using Spectroscopic Single-Molecule Localization Microscopy.Analytical chemistry · 2022Article
- Structural control of fibrin bioactivity by mechanical deformation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Engineered Molecular Therapeutics Targeting Fibrin and the Coagulation System: a Biophysical Perspective.Biophysical reviews · 2022Review
- Strength, deformability and toughness of uncrosslinked fibrin fibers from theoretical reconstruction of stress-strain curves.Acta biomaterialia · 2021Article
- Label-free imaging of fibroblast membrane interfaces and protein signatures with vibrational infrared photothermal and phase signals.Biomedical optics express · 2021Article
- Self-regulated hirudin delivery for anticoagulant therapy.Science advances · 2020Article
- The function and clinical application of extracellular vesicles in innate immune regulation.Cellular & molecular immunology · 2020Review
- FTIR, Raman and AFM characterization of the clinically valid biochemical parameters of the thrombi in acute ischemic stroke.Scientific reports · 2019Article
- Damped White Noise Diffusion with Memory for Diffusing Microprobes in Ageing Fibrin Gels.Biophysical journal · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Following an injury, a blood clot must form at the wound site to stop bleeding before skin repair can occur. Blood clots must satisfy a unique set of material requirements; they need to be sufficiently strong to resist pressure from the arterial blood flow but must be highly flexible to support large strains associated with tissue movement around the wound. These combined properties are enabled by a fibrous matrix consisting of the protein fibrin. Fibrin hydrogels can support large macroscopic strains owing to the unfolding transition of α-helical fibril structures to β sheets at the molecular level, among other reasons. Imaging protein secondary structure on the submicrometer length scale, we reveal that another length scale is relevant for fibrin function. We observe that the protein polymorphism in the gel becomes spatially heterogeneous on a micrometer length scale with increasing tensile strain, directly showing load-bearing inhomogeneity and nonaffinity. Supramolecular structural features in the hydrogel observed under strain indicate that a uniform fibrin hydrogel develops a composite-like microstructure in tension, even in the absence of cellular inclusions.
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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.