ArticleBiochimica et biophysica acta. Biomembranes2018
Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.
Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- SARS-CoV-2 envelope protein mitochondrial localization reveals host metabolic disruption.The Journal of biological chemistry · 2026Article
- Blood pH Analysis in Combination with Molecular Medical Tools in Relation to COVID-19 Symptoms.Biomedicines · 2023Article
- Ultrafast one-minute electronic detection of SARS-CoV-2 infection by 3CLNature communications · 2022Article
- Characterization of the SARS-CoV-2 E Protein: Sequence, Structure, Viroporin, and Inhibitors.Protein science : a publication of the Protein Society · 2021Review
- Current methods for diagnosis of human coronaviruses: pros and cons.Analytical and bioanalytical chemistry · 2021Review
- Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain.Biophysical chemistry · 2020Review
- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
In recent years, several studies based on the interaction of self-assembling short peptides derived from viroporins with model membranes, have improved our understanding of the molecular mechanism of corona virus (CoV) infection under physiological conditions. In this study, we have characterized the mechanism of membrane interaction of a short, 9-residue peptide TK9 (T
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Registered trials
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