ArticleArchives of microbiology2024
Prediction of virus-host interactions and identification of hot spot residues of DENV-2 and SH3 domain interactions.
Article in Archives of microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Phosphoproteome-Entailed Kinase-Substrate Landscape of Human-DENV-2 Interaction.International journal of molecular sciences · 2026Article
- VHI-Pred: A Multi-Feature-Based Tool for Predicting Human-Virus Protein-Protein Interactions.Molecular biotechnology · 2026Article
- Exploiting host kinases to combat dengue virus infection and disease.Antiviral research · 2025Review
- Predicting Motif-Mediated Interactions Based on Viral Genomic Composition.International journal of molecular sciences · 2025Article
- Computational insights into the targeted inhibition of lipoxygenase in Pseudomonas aeruginosa: hints for drug design.Archives of microbiology · 2025Article
- Ascariasis in a child with recurrent gastrointestinal hemorrhage: case report and literature review.Frontiers in pediatrics · 2025Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dengue virus, particularly serotype 2 (DENV-2), poses a significant global health threat, and understanding the molecular basis of its interactions with host cell proteins is imperative for developing targeted therapeutic strategies. This study elucidated the interactions between proline-enriched motifs and Src homology 3 (SH3) domain. The SH3 domain is pivotal in mediating protein-protein interactions, particularly by recognizing and binding to proline-rich regions in partner proteins. Through a computational pipeline, we analyzed the interactions and binding modes of proline-enriched motifs with SH3 domains, identified new potential DENV-2 interactions with the SH3 domain, and revealed potential hot spot residues, underscoring their significance in the viral life cycle. This comprehensive analysis provides crucial insights into the molecular basis of DENV-2 infection, highlighting conserved and serotype-specific interactions. The identified hot spot residues offer potential targets for therapeutic intervention, laying the foundation for developing antiviral strategies against Dengue virus infection. These findings contribute to the broader understanding of viral-host interactions and provide a roadmap for future research on Dengue virus pathogenesis and treatment.
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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.