ArticleUkrainian biochemical journal
Structure and function of fibrinogen BβN-domains.
Article in Ukrainian biochemical journal. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
The trial behind it
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Identification of Amino Acid Residues Critical for the Interaction of Fibrin with N-Cadherin.Biochemistry · 2025Article
- Formation and elimination of soluble fibrin and D-dimer in the bloodstream.Croatian medical journal · 2023Review
- Current View on the Molecular Mechanisms Underlying Fibrin(ogen)-Dependent Inflammation.Thrombosis and haemostasis · 2022Review
- Dual functions of the fibrin βN-domains in the VLDL receptor-dependent pathway of transendothelial migration of leukocytes.Thrombosis research · 2022Article
- Structural Basis for the Interaction of Fibrin with the Very Low-Density Lipoprotein Receptor Revealed by NMR and Site-Directed Mutagenesis.Biochemistry · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Two BβN-domains of fibrinogen are formed by the N-terminal portions of its two Bβ chains including amino acid residues Bβ1-65. Although their folding status is not well understood and the recombinant disulfide-linked (Bβ1-66)
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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.