ArticleJournal of medical virology2021
Mutations in membrane-fusion subunit of spike glycoprotein play crucial role in the recent outbreak of COVID-19.
Article in Journal of medical virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- The role of intrinsically disordered regions of SARS-CoV-2 nucleocapsid and non-structural protein 1 proteins.Frontiers in chemistry · 2025Review
- Fluorometric and Colorimetric Method for SARS-CoV-2 Detection Using Designed Aptamer Display Particles.Biosensors · 2024Article
- Ultra-sensitive label-free SERS biosensor with high-throughput screened DNA aptamer for universal detection of SARS-CoV-2 variants from clinical samples.Biosensors & bioelectronics · 2023Article
- SARS-CoV-2 E protein: Pathogenesis and potential therapeutic development.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Review
- Review
- Antiviral effects of azithromycin: A narrative review.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
- Mutations in membrane-fusion subunit of spike glycoprotein play crucial role in the recent outbreak of COVID-19.Journal of medical virology · 2021Article
- HiSpike Method for High-Throughput Cost Effective Sequencing of the SARS-CoV-2 Spike Gene.Frontiers in medicine · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coronavirus disease-2019 (COVID-19), the ongoing pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a major threat to the entire human race. It is reported that SARS-CoV-2 seems to have relatively low pathogenicity and higher transmissibility than previously outbroke SARS-CoV. To explore the reason of the increased transmissibility of SARS-CoV-2 compared with SARS-CoV, we have performed a comparative analysis on the structural proteins (spike, envelope, membrane, and nucleoprotein) of two viruses. Our analysis revealed that extensive substitutions of hydrophobic to polar and charged amino acids in spike glycoproteins of SARS-CoV2 creates an intrinsically disordered region (IDR) at the beginning of membrane-fusion subunit and intrinsically disordered residues in fusion peptide. IDR provides a potential site for proteolysis by furin and enriched disordered residues facilitate prompt fusion of the SARS-CoV2 with host membrane by recruiting molecular recognition features. Here, we have hypothesized that mutation-driven accumulation of intrinsically disordered residues in spike glycoproteins play dual role in enhancing viral transmissibility than previous SARS-coronavirus. These analyses may help in epidemic surveillance and preventive measures against COVID-19.
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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.