ArticleMolecules (Basel, Switzerland)2021
Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions.
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
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- Temperature-Dependent Binding of Forxiga to Human Serum Albumin: Fluorescence, Competitive Displacement and Thermodynamic Analysis.Current issues in molecular biology · 2026Article
- VHI-Pred: A Multi-Feature-Based Tool for Predicting Human-Virus Protein-Protein Interactions.Molecular biotechnology · 2026Article
- Molecular characterization of human respiratory syncytial virus in Mexico (season 2023-2024) through whole-genome sequencing.Scientific reports · 2025Article
- Article
- Some new insights into the biological activities of carboxymethylated polysaccharides from Lasiodiplodia theobromae.BMC complementary medicine and therapies · 2023Article
- Spectroscopic, Thermodynamic and Molecular Docking Studies on Molecular Mechanisms of Drug Binding to Proteins.Molecules (Basel, Switzerland) · 2022Article
- Mutation in the CX3C Motif of G Protein Disrupts Its Interaction with Heparan Sulfate: A Calorimetric, Spectroscopic, and Molecular Docking Study.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The global burden of disease caused by a respiratory syncytial virus (RSV) is becoming more widely recognized in young children and adults. Heparan sulfate helps in attaching the virion through G protein with the host cell membrane. In this study, we examined the structural changes of ectodomain G protein (edG) in a wide pH range. The absorbance results revealed that protein maintains its tertiary structure at physiological and highly acidic and alkaline pH. However, visible aggregation of protein was observed in mild acidic pH. The intrinsic fluorescence study shows no significant change in the λ
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Registered trials
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