ReviewBiophysical chemistry2020
Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain.
Review in Biophysical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
- SARS-CoV-2 envelope protein mitochondrial localization reveals host metabolic disruption.The Journal of biological chemistry · 2026Article
- C-terminus-outward orientation of SARS-CoV-2 envelope proteins on viral capsid enables a novel virus-cell interaction pathway.Frontiers in cellular and infection microbiology · 2026Article
- The structure and function of membrane protein in coronavirus infection and its applications in the development of vaccines and therapeutic drugs.Frontiers in microbiology · 2026Review
- 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
- Subcellular localization of SARS-CoV-2 E and 3a proteins along the secretory pathway.Journal of molecular histology · 2025Article
- In Silico Design of a Trans-Amplifying RNA-Based Vaccine against SARS-CoV-2 Structural Proteins.Advances in virology · 2024Article
- Microscopic Observation of Membrane Fusion between Giant Liposomes and Baculovirus Budded Viruses Activated by the Release of a Caged Proton.Membranes · 2023Article
- Blood pH Analysis in Combination with Molecular Medical Tools in Relation to COVID-19 Symptoms.Biomedicines · 2023Article
- Review
- Antiviral peptides against SARS-CoV-2: therapeutic targets, mechanistic antiviral activity, and efficient delivery.Pharmacological reports : PR · 2022Review
- Non-uniform aspects of the SARS-CoV-2 intraspecies evolution reopen question of its origin.International journal of biological macromolecules · 2022Article
- Probing effects of the SARS-CoV-2 E protein on membrane curvature and intracellular calcium.Biochimica et biophysica acta. Biomembranes · 2022Article
- The effect of various compounds on the COVID mechanisms, from chemical to molecular aspects.Biophysical chemistry · 2022Review
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- Effect of pH on stability of dimer structure of the main protease of coronavirus-2.Biophysical chemistry · 2022Article
- Targeting Specific Checkpoints in the Management of SARS-CoV-2 Induced Cytokine Storm.Life (Basel, Switzerland) · 2022Review
- Atorvastatin Effectively Inhibits Ancestral and Two Emerging Variants of SARS-CoV-2Frontiers in microbiology · 2022Article
- Potential Genes Associated with COVID-19 and Comorbidity.International journal of medical sciences · 2022Article
- COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks.International journal of biological macromolecules · 2021Review
- Therapeutic targets and interventional strategies in COVID-19: mechanisms and clinical studies.Signal transduction and targeted therapy · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Envelope (E) protein in SARS Coronavirus (CoV) is a small structural protein, incorporated as part of the envelope. A major fraction of the protein has been known to be associated with the host membranes, particularly organelles related to intracellular trafficking, prompting CoV packaging and propagation. Studies have elucidated the central hydrophobic transmembrane domain of the E protein being responsible for much of the viroporin activity in favor of the virus. However, newer insights into the organizational principles at the membranous compartments within the host cells suggest further complexity of the system. The lesser hydrophobic Carboxylic-terminal of the protein harbors interesting amino acid sequences- suggesting at the prevalence of membrane-directed amyloidogenic properties that remains mostly elusive. These highly conserved segments indicate at several potential membrane-associated functional roles that can redefine our comprehensive understanding of the protein. This should prompt further studies in designing and characterizing of effective targeted therapeutic measures.
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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.