ArticleACS omega2025
Uncovering the Binding Mechanism of Mutated Omicron Variants via Computational Strategies.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Allosteric effects of CDR-H3 mutations modulate binding and neutralization of a conserved SARS-CoV-2 RBD-targeting antibody.Microbiology spectrum · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The COVID-19 pandemic, triggered by the SARS-CoV-2 virus, has resulted in nearly 630 million cases and 6.60 million fatalities globally, as of November 2022. SARS-CoV-2, a species of the Coronaviridae family, has a single-stranded positive-sense RNA genome as well as four main structural proteins (S, E, M, and N) required for viral entrance into target cells. The spike protein (S) influences this entry through interactions with human angiotensin-converting enzyme 2 (hACE2) receptor. The World Health Organization (WHO) recognized numerous variants of concern (VOCs) that involve Alpha, Beta, Gamma, Delta, and Omicron, having multiple mutations within the spike protein, altering infection rates and immunity evasion. The Omicron variant, featuring 50 mutations, mainly within the spike protein's receptor-binding domain (RBD), has a higher transmission rate as compared to other variants. This study focused on two recent Omicron subvariants, XBB.1.5 and CH.1.1, which are known for their high affinity for the human ACE2 receptor. Utilizing an in silico strategy, a total of 1.65 μs molecular dynamics (MD) simulations were performed to assess the stability as well as binding details of these subvariants along with the wild-type Omicron variants. The comprehensive structural stability of the spike protein-hACE2 complexes was evaluated by using numerous parameters including root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), radius of gyration (
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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.