ArticleJournal of clinical medicine2021
Functional and Structural Characterization of Nucleic Acid Ligands That Bind to Activated Coagulation Factor XIII.
Article in Journal of clinical medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 8 citations in OpenAlex.
- Emerging role of nucleic acid aptamers in sepsis-induced coagulopathy: Future perspectives in diagnostics and therapeutics.Annals of intensive care · 2026Review
- Cardiac Troponin Biosensor Designs: Current Developments and Remaining Challenges.International journal of molecular sciences · 2022Review
- Aptamer loaded superparamagnetic beads for selective capturing and gentle release of activated protein C.Scientific reports · 2022Article
- Thrombomodulin activation driven by LXR agonist attenuates renal injury in diabetic nephropathy.Frontiers in medicine · 2022Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coagulation factor XIII (FXIII) is a protransglutaminase which plays an important role in clot stabilization and composition by cross-linking the α- and γ-chains of fibrin and increasing the resistance of the clot to mechanical and proteolytic challenges. In this study, we selected six DNA aptamers specific for activated FXIII (FXIIIa) and investigated the functional characterization of FXIIIa after aptamer binding. One of these aptamers, named FA12, efficiently captures FXIIIa even in the presence of zymogenic FXIII subunits. Furthermore, this aptamer inhibits the incorporation of FXIII and α2-antiplasmin (α2AP) into fibrin(ogen) with IC
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