ArticleBiochemistry2017
Interaction of Fibrin with the Very Low-Density Lipoprotein (VLDL) Receptor: Further Characterization and Localization of the VLDL Receptor-Binding Site in Fibrin βN-Domains.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Activation of the Coagulation Cascade as a Universal Danger Sign.Current issues in molecular biology · 2025Review
- Identification of Amino Acid Residues Critical for the Interaction of Fibrin with N-Cadherin.Biochemistry · 2025Article
- 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
- Identifying Function Determining Residues in Neuroimmune Semaphorin 4A.International journal of molecular sciences · 2022Article
- Structural Basis for the Interaction of Fibrin with the Very Low-Density Lipoprotein Receptor Revealed by NMR and Site-Directed Mutagenesis.Biochemistry · 2021Article
- Fibrin-VLDL Receptor-Dependent Pathway Promotes Leukocyte Transmigration by Inhibiting Src Kinase Fyn and is a Target for Fibrin β15-42 Peptide.Thrombosis and haemostasis · 2019Article
- Article
- Effect of fibrinogen, fibrin, and fibrin degradation products on transendothelial migration of leukocytes.Thrombosis research · 2018Article
- Structure and function of fibrinogen BβN-domains.Ukrainian biochemical journalArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Our recent study revealed that fibrin and the very low-density lipoprotein receptor (VLDLR) interact with each other through a pair of fibrin βN-domains and CR domains of the receptor and this interaction promotes transendothelial migration of leukocytes and thereby inflammation. The major objectives of this study were to further clarify the molecular mechanism of fibrin-VLDLR interaction and to identify amino acid residues in the βN-domains involved in this interaction. Our binding experiments with the (β15-66)
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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.