ArticleTravel medicine and infectious disease
Omicron N501Y mutation among SARS-CoV-2 lineages: Insilico analysis of potent binding to tyrosine kinase and hypothetical repurposed medicine.
Article in Travel medicine and infectious disease. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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The trial behind it
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.
- New variants of COVID-19 (XBB.1.5 and XBB.1.16, the "Arcturus"): A review of highly questioned concerns, a brief comparison between different peaks in the COVID-19 pandemic, with a focused systematic review on expert recommendations for prevention, vaccination, and treatment measures in the general population and at-risk groups.Immunity, inflammation and disease · 2024Pooled it
- Association Between ABO Blood Groups and SARS-CoV-2 RNAemia, Spike Protein Mutations, and Thrombotic Events in COVID-19 Patients.Pathogens (Basel, Switzerland) · 2025Article
- The BCL-2 inhibitor APG-2575 resets tumor-associated macrophages toward the M1 phenotype, promoting a favorable response to anti-PD-1 therapy via NLRP3 activation.Cellular & molecular immunology · 2024Article
- The spread of the omicron variant: Identification of knowledge gaps, virus diffusion modelling, and future research needs.Environmental research · 2023Article
- Genomic surveillance of SARS-CoV-2 strains circulating in Iran during six waves of the pandemic.Influenza and other respiratory viruses · 2023Article
- Article
- SARS-CoV-2 Omicron and its current known unknowns: A narrative review.Reviews in medical virology · 2023Review
- Recent advances on human mpox.New microbes and new infections · 2023Review
- Omicron variant: Current insights and future directions.Microbiological research · 2022Review
- Peimine inhibits variants of SARS-CoV-2 cell entry via blocking the interaction between viral spike protein and ACE2.Journal of food biochemistry · 2022Article
- A Systematic Review on the Emergence of Omicron Variant and Recent Advancement in Therapies.Vaccines · 2022Review
- Methodology-Centered Review of Molecular Modeling, Simulation, and Prediction of SARS-CoV-2.Chemical reviews · 2022Review
- Targeting omicron and other reported SARS-CoV-2 lineages by potent inhibitors of main protease 3CL Mpro: Molecular simulation analysis.The Journal of infection · 2022Article
- Emergence of SARS-CoV-2 Omicron (B.1.1.529) variant, salient features, high global health concerns and strategies to counter it amid ongoing COVID-19 pandemic.Environmental research · 2022Review
- Omicron variant (B.1.1.529) of SARS-CoV-2: understanding mutations in the genome, S-glycoprotein, and antibody-binding regions.GeroScience · 2022Article
- There is nothing exempt from the peril of mutation - The Omicron spike.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
- In Silico Screening of Bioactive Compounds of Representative Seaweeds to Inhibit SARS-CoV-2 ACE2-Bound Omicron B.1.1.529 Spike Protein Trimer.Marine drugs · 2022Article
- Protective antigenic epitopes revealed by immunosignatures after three doses of inactivated SARS-CoV-2 vaccine.Frontiers in immunology · 2022Article
- Is Omicron the end of pandemic or start of a new innings?Travel medicine and infectious diseaseReview
- Tracking and controlling the spatiotemporal spread of SARS-CoV-2 Omicron variant in South Africa.Travel medicine and infectious diseaseArticle
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Variants of SARS-CoV-2 lineages including the most recently circulated Omicron, and previous pandemic B.1.351, B.1.1.7, which have been public concerns, contain a N501Y mutation located in the spike receptor binding domain. However, the potential interactions with host cells linking N501Y mutation to pathogenic relevance remain elusive. Recently, we and others report that kinases such as PI3K/AKT signaling are essential in SARS-CoV-2 entry. Here we analyzed the predicted potential kinases interacting with the mutation. Bioinformatics tools including structure-prediction based molecular docking analysis were applied. We found kinases such as EGFR might potentially act as new factors involving the N501Y mutation binding through possible phosphorylation at Y501 and enhanced affinity in certain variants. To our surprise, the Omicron receptor binding domain harboring N501Y mutation did not enhance binding to EGFR which might be due to the mutations of charged polar to uncharged polar side chains located on the interaction interfaces. Similarly, potent gains of phosphorylation in B.1.351 and B.1.1.7 by mutations were predicted and interaction networks were analyzed with enrichment of pathways. Given kinases might be elevated in cancer patients, the N501Y mutation containing lineages may be possibly much more infectious and additional care for cancer management might be taken into consideration by precision prevention, therapy or recovery.
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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.