The E Protein Is a Multifunctional Membrane Protein of SARS-CoV
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Summary
The authors' phylogenetic analyses of the E protein sequences in all published coronaviruses place SARS-CoV in an independent group in Coronaviridae and suggest a non-human animal origin.
- Type
- article
- Published
- 2003-05-01
- Cited by
- 50
- References
- 22
- OpenAlex
- https://openalex.org/W303494310
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4479097
Keywords
Transmembrane protein, Phylogenetic tree, Transmembrane domain, Protein sequencing, Biology
References
- Induction of Apoptosis in Murine Coronavirus-Infected Cultured Cells and Demonstration of E Protein as an Apoptosis Inducer
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- Two Amino Acid Changes at the N-Terminus of Transmissible Gastroenteritis Coronavirus Spike Protein Result in the Loss of Enteric Tropism
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- Coronavirus Spike Proteins in Viral Entry and Pathogenesis
- SARS-associated coronavirus.
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- Membrane Topology of Coronavirus E Protein
- Targeted Recombination within the Spike Gene of Murine Coronavirus Mouse Hepatitis Virus-A59: Q159 Is a Determinant of Hepatotropism
- Generation of a Replication-Competent, Propagation-Deficient Virus Vector Based on the Transmissible Gastroenteritis Coronavirus Genome
- Coronavirus Pseudoparticles Formed with Recombinant M and E Proteins Induce Alpha Interferon Synthesis by Leukocytes
- A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01)
- Characterization of a Novel Coronavirus Associated with Severe Acute Respiratory Syndrome
- Targeted Recombination Demonstrates that the Spike Gene of Transmissible Gastroenteritis Coronavirus Is a Determinant of Its Enteric Tropism and Virulence
- Coronavirus Particle Assembly: Primary Structure Requirements of the Membrane Protein
- Characterization of the Coronavirus Mouse Hepatitis Virus Strain A59 Small Membrane Protein E
- Analysis of Constructed E Gene Mutants of Mouse Hepatitis Virus Confirms a Pivotal Role for E Protein in Coronavirus Assembly
- Infectious Bronchitis Virus E Protein Is Targeted to the Golgi Complex and Directs Release of Virus-Like Particles
- Virus Maturation by Budding
Cited by
- Dissection and identification of regions required to form pseudoparticles by the interaction between the nucleocapsid (N) and membrane (M) proteins of SARS coronavirus
- Molecular Advances in Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV)
- Genetics and functions of the SARS coronavirus spike protein
- Coronavirus envelope protein: current knowledge
- Molecular and Structural Insights into COVID-19 Pandemic
- Research progress on human coronavirus and antiviral drugs
- High stability of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) RNA under minimal storage conditions for detection by Real-Time PCR
- The discovery of a recombinant SARS2-like CoV strain provides insights into SARS and COVID-19 pandemics
- Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain
- Evolutionary Insights into the Envelope Protein of SARS-CoV-2
- COVID-19: Review of a 21st Century Pandemic from Etiology to Neuro-psychiatric Implications
- Clinical Evidence and Therapeutic Treatments at the Time of the Coronaviruses Responsible for SARS: A Perspective Point of View.
- Alcohol-based hand sanitisers as first line of defence against SARS-CoV-2: a review of biology, chemistry and formulations
- Distant sequence similarity between hepcidin and the novel coronavirus spike glycoprotein: a potential hint at the possibility of local iron dysregulation in COVID-19
- Repurposed drugs and nutraceuticals targeting envelope protein: A possible therapeutic strategy against COVID-19
- Probiotics as a Weapon in the Fight Against COVID-19
- Mutation Landscape of SARS COV2 in Africa
- Environmental Dependence of the Structure of the C-terminal Domain of the SARS-CoV-2 Envelope Protein
- Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins—A comparative study
- Potential immune epitope map for structural proteins of SARS-CoV-2
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