ArticleScientific reports2021
Protein residue network analysis reveals fundamental properties of the human coagulation factor VIII.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Exploring proteins and protein-ligand complexes through residue interaction networks.Nature protocols · 2026Review
- Artificial Intelligence in the Management of Hereditary and Acquired Hemophilia: From Genomics to Treatment Optimization.International journal of molecular sciences · 2025Review
- Using residue interaction networks to understand protein function and evolution and to engineer new proteins.Current opinion in structural biology · 2024Review
- Full-scale network analysis reveals properties of the FV protein structure organization.Scientific reports · 2023Article
- A graph-based machine learning framework identifies critical properties of FVIII that lead to hemophilia A.Frontiers in bioinformatics · 2023Article
- Computational analyses reveal fundamental properties of the AT structure related to thrombosis.Bioinformatics advances · 2023Article
- A Machine Learning Framework Predicts the Clinical Severity of Hemophilia B Caused by Point-Mutations.Frontiers in bioinformatics · 2022Article
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Authors and funding
4 authors.
Funding
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Abstract
Hemophilia A is an X-linked inherited blood coagulation disorder caused by the production and circulation of defective coagulation factor VIII protein. People living with this condition receive either prophylaxis or on-demand treatment, and approximately 30% of patients develop inhibitor antibodies, a serious complication that limits treatment options. Although previous studies performed targeted mutations to identify important residues of FVIII, a detailed understanding of the role of each amino acid and their neighboring residues is still lacking. Here, we addressed this issue by creating a residue interaction network (RIN) where the nodes are the FVIII residues, and two nodes are connected if their corresponding residues are in close proximity in the FVIII protein structure. We studied the characteristics of all residues in this network and found important properties related to disease severity, interaction to other proteins and structural stability. Importantly, we found that the RIN-derived properties were in close agreement with in vitro and clinical reports, corroborating the observation that the patterns derived from this detailed map of the FVIII protein architecture accurately capture the biological properties of FVIII.
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