ArticleInternational journal of molecular sciences2023
The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization.
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 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.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Full-length SARS-CoV-2 envelope protein adopts an interfacial topology in lipid bilayers.Biochimica et biophysica acta. Biomembranes · 2026Article
- Carbon-13 Centerband-Only Detection of EXchange with Dynamic Nuclear Polarization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Screening and discovery of an antiviral candidate inhibiting the SARS-CoV-2 envelope (2-E) channel.Current research in microbial sciences · 2025Article
- The 6-kilodalton peptide 1 of the familyFrontiers in microbiology · 2025Review
- Prediction of conformational states in a coronavirus channel using Alphafold-2 and DeepMSA2: Strengths and limitations.Computational and structural biotechnology journal · 2024Article
- SARS-CoV-2 envelope protein alters calcium signaling via SERCA interactions.Scientific reports · 2024Article
- Oligomeric State and Drug Binding of the SARS-CoV-2 Envelope Protein Are Sensitive to the Ectodomain.Journal of the American Chemical Society · 2024Article
- Endocrine dysregulation in COVID-19: molecular mechanisms and insights.Frontiers in endocrinology · 2024Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The envelope (E) protein is a small polypeptide that can form ion channels in coronaviruses. In SARS coronavirus 2 (SARS-CoV-2), the agent that caused the recent COVID-19 pandemic, and its predecessor SARS-CoV-1, E protein is found in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC), where virion budding takes place. Several reports claim that E protein promotes the formation of "cation-selective channels". However, whether this term represents specificity to certain ions (e.g., potassium or calcium) or the partial or total exclusion of anions is debatable. Herein, we discuss this claim based on the available data for SARS-CoV-1 and -2 E and on new experiments performed using the untagged full-length E protein from SARS-CoV-2 in planar lipid membranes of different types, including those that closely mimic the ERGIC membrane composition. We provide evidence that the selectivity of the E-induced channels is very mild and depends strongly on lipid environment. Thus, despite past and recent claims, we found no indication that the E protein forms cation-selective channels that prevent anion transport, and even less that E protein forms
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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.