ArticleBiochemistry2011
Structure, stability, and interaction of fibrin αC-domain polymers.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- Mechanically Spatio-Chimeric Fibrin Assembly Enables Vascular-Integrated Muscle Reconstruction for Volumetric Muscle Loss Repair.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Systematic mapping of the conformational landscape and dynamism of soluble fibrinogen.Journal of thrombosis and haemostasis : JTH · 2023Article
- Article
- The Story of the Fibrin(ogen) αC-Domains: Evolution of Our View on Their Structure and Interactions.Thrombosis and haemostasis · 2022Review
- A Fibrinogen Alpha Fragment Mitigates Chemotherapy-InducedFrontiers in oncology · 2021Article
- Fibrinogen and Fibrin.Sub-cellular biochemistry · 2021Review
- Mass spectrometry-based molecular mapping of native FXIIIa cross-links in insoluble fibrin clots.The Journal of biological chemistry · 2019Article
- Atomic Structural Models of Fibrin Oligomers.Structure (London, England : 1993) · 2018Article
- Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.Nanoscale · 2017Article
- The provisional matrix: setting the stage for tissue repair outcomes.Matrix biology : journal of the International Society for Matrix Biology · 2017Review
- Fibrin Formation, Structure and Properties.Sub-cellular biochemistry · 2017Review
- Polymerisation of fibrin αC-domains promotes endothelial cell migration and proliferation.Thrombosis and haemostasis · 2014Article
- Structural effects of methionine oxidation on isolated subdomains of human fibrin D and αC regions.PloS one · 2014Article
- Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry.Biochemistry · 2013Article
- Review
- Characterization of Anopheles gambiae transglutaminase 3 (AgTG3) and its native substrate Plugin.The Journal of biological chemistry · 2013Article
- Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen.Biophysical journal · 2012Article
- On the mechanism of αC polymer formation in fibrin.Biochemistry · 2012Article
- Identification of respective lysine donor and glutamine acceptor sites involved in factor XIIIa-catalyzed fibrin α chain cross-linking.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Our previous studies revealed that in fibrinogen the αC-domains are not reactive with their ligands, suggesting that their binding sites are cryptic and become exposed upon its conversion to fibrin, in which these domains form αC polymers. On the basis of this finding, we hypothesized that polymerization of the αC-domains in fibrin results in the exposure of their binding sites and that these domains adopt the physiologically active conformation only in αC-domain polymers. To test this hypothesis, we prepared a recombinant αC region (residues Aα221-610) including the αC-domain (Aα392-610), demonstrated that it forms soluble oligomers in a concentration-dependent and reversible manner, and stabilized such oligomers by covalently cross-linking them with factor XIIIa. Cross-linked Aα221-610 oligomers were stable in solution and appeared as ordered linear, branching filaments when analyzed by electron microscopy. Spectral studies revealed that the αC-domains in such oligomers were folded into compact structures of high thermal stability with a significant amount of β-sheets. These findings indicate that cross-linked Aα221-610 oligomers are highly ordered and mimic the structure of fibrin αC polymers. The oligomers also exhibited functional properties of polymeric fibrin because, in contrast to the monomeric αC-domain, they bound tPA and plasminogen and stimulated activation of the latter by the former. Altogether, the results obtained with cross-linked Aα221-610 oligomers clarify the structure of the αC-domains in fibrin αC polymers and confirm our hypothesis that their binding sites are exposed upon polymerization. Such oligomers represent a stable, soluble model of fibrin αC polymers that can be used for further structure-function studies of fibrin αC-domains.
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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.