ArticleThe Journal of biological chemistry2014
Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 141 citations in OpenAlex.
- The SARS-CoV-2 envelope PDZ binding motif acts as a virulence factor disrupting host's epithelial cell-cell junctions.Cellular & molecular biology letters · 2025Article
- Ion channel structure and function of the MERS coronavirus E protein.Science advances · 2025Article
- Molecular Dynamics Simulation of SARS-CoV-2 E Ion Channel: The Study of Lone Protein and its Conformational Changes in Complex with Potential Cage Inhibitors.Current computer-aided drug design · 2025Article
- Prediction of conformational states in a coronavirus channel using Alphafold-2 and DeepMSA2: Strengths and limitations.Computational and structural biotechnology journal · 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
- Membrane Activity and Viroporin Assembly for the SARS-CoV-2 E Protein Are Regulated by Cholesterol.Biomolecules · 2024Article
- Flavivirus Zika NS4A protein forms large oligomers in liposomes and in mild detergent.Scientific reports · 2024Article
- Transmembrane conformation of the envelope protein of an alpha coronavirus, NL63.Protein science : a publication of the Protein Society · 2024Article
- SARS-CoV-2 outbreak: role of viral proteins and genomic diversity in virus infection and COVID-19 progression.Virology journal · 2024Review
- Developing inhibitory peptides against SARS-CoV-2 envelope protein.PLoS biology · 2024Article
- Membrane Condensation and Curvature Induced by SARS-CoV-2 Envelope Protein.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Distinguishing Different Hydrogen-Bonded Helices in Proteins by EfficientBiochemistry · 2024Article
- Compounds based on Adamantyl-substituted Amino Acids and Peptides as Potential Antiviral Drugs Acting as Viroporin Inhibitors.Current pharmaceutical design · 2024Review
- A short sequence in the tail of SARS-CoV-2 envelope protein controls accessibility of its PDZ-binding motif to the cytoplasm.The Journal of biological chemistry · 2024Article
- Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein.Communications biology · 2023Article
- Atomic structure of the open SARS-CoV-2 E viroporin.Science advances · 2023Article
- Hexamethylene amiloride binds the SARS-CoV-2 envelope protein at the protein-lipid interface.Protein science : a publication of the Protein Society · 2023Article
- The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization.International journal of molecular sciences · 2023Article
- In Silico Screening of Drugs That Target Different Forms of E Protein for Potential Treatment of COVID-19.Pharmaceuticals (Basel, Switzerland) · 2023Article
- The envelope proteins from SARS-CoV-2 and SARS-CoV potently reduce the infectivity of human immunodeficiency virus type 1 (HIV-1).Retrovirology · 2022Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.
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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.