ArticleInternational journal of molecular sciences2023
A Protein Co-Conservation Network Model Characterizes Mutation Effects on SARS-CoV-2 Spike Protein.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
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
4 citing papers in PubMed, 7 citations in OpenAlex.
- Molecular Pharmacology at the Crossroads of Precision Medicine.Current issues in molecular biology · 2025Article
- AnnCovDB: a manually curated annotation database for mutations in SARS-CoV-2 spike protein.Database : the journal of biological databases and curation · 2025Article
- Article
- Progress of the "Molecular Informatics" Section in 2022.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The emergence of numerous variants of SARS-CoV-2 has presented challenges to the global efforts to control the COVID-19 pandemic. The major mutation is in the SARS-CoV-2 viral envelope spike protein that is responsible for virus attachment to the host, and is the main target for host antibodies. It is critically important to study the biological effects of the mutations to understand the mechanisms of how mutations alter viral functions. Here, we propose a protein co-conservation weighted network (PCCN) model only based on the protein sequence to characterize the mutation sites by topological features and to investigate the mutation effects on the spike protein from a network view. Frist, we found that the mutation sites on the spike protein had significantly larger centrality than the non-mutation sites. Second, the stability changes and binding free energy changes in the mutation sites were positively significantly correlated with their neighbors' degree and the shortest path length separately. The results indicate that our PCCN model provides new insights into mutations on spike proteins and reflects the mutation effects on protein function alternations.
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Registered trials
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