ArticleHeliyon2024
The sequence 581Ser-610Val in the fibrinogen Aα chain is responsible for the formation of complexes between plasminogen and αC-regions of fibrin(ogen).
Article in Heliyon, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Differences and Compatibility between Human and Porcine Fibrinolytic Components toward Plasmin Generation and Fibrin Degradation.TH open : companion journal to thrombosis and haemostasis · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Objective: This study aimed to identify the binding sites for plasminogen (Pg) and its kringle-containing fragments within the αC-region of fibrin(ogen). This investigation is crucial while the conversion of fibrinogen into fibrin induces conformational changes that expose binding sites for Pg and tissue-type Pg activator (tPA), facilitating effective zymogen activation on the fibrin surface. Methods: Two C-terminal fragments of the Aα chain ‒ 45 kDa (225Val-610Val) and 40 kDa (225Val-580Lys), were obtained through plasmin hydrolysis of human fibrinogen and subsequently characterized using MALDI TOF mass spectrometry. The interactions of Glu-Pg and Lys-Pg, as well as Pg kringle fragments (K1-3, K4, and K5), with the obtained αC truncated polypeptides were analyzed using ELISA and Western blot techniques with the use of specific antibodies. Results: It was demonstrated that Pg and its fragments K1-3, K4, and K5 interact exclusively with the 45-kDa fragment (225Val-610Val) of the αC region of fibrinogen with high affinity in a concentration-dependent manner (K Conclusions: It was shown that the sequence 581Ser-610Val of fibrinogen Aα-chain, which becomes exposed during the conversion of fibrinogen to fibrin, is essential for the formation of complexes between Pg and αC regions of fibrin(ogen), thereby contributing to the initiation and regulation of fibrinolysis.
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.