ArticleInternational journal of molecular sciences2022
Oligomerization-Dependent Beta-Structure Formation in SARS-CoV-2 Envelope Protein.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Full-length SARS-CoV-2 envelope protein adopts an interfacial topology in lipid bilayers.Biochimica et biophysica acta. Biomembranes · 2026Article
- Membrane Depth Measurements of E Protein byBiophysica · 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
- Transmembrane conformation of the envelope protein of an alpha coronavirus, NL63.Protein science : a publication of the Protein Society · 2024Article
- Developing inhibitory peptides against SARS-CoV-2 envelope protein.PLoS biology · 2024Article
- Distinguishing Different Hydrogen-Bonded Helices in Proteins by EfficientBiochemistry · 2024Article
- The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization.International journal of molecular sciences · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the current COVID-19 pandemic. In SARS-CoV-2, the channel-forming envelope (E) protein is almost identical to the E protein in SARS-CoV, and both share an identical α-helical channel-forming domain. Structures for the latter are available in both detergent and lipid membranes. However, models of the extramembrane domains have only been obtained from solution NMR in detergents, and show no β-strands, in contrast to secondary-structure predictions. Herein, we have studied the conformation of purified SARS-CoV-2 E protein in lipid bilayers that mimic the composition of ER-Golgi intermediate compartment (ERGIC) membranes. The full-length E protein at high protein-to-lipid ratios produced a clear shoulder at 1635 cm
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