ArticleBiochimica et biophysica acta2016
Structure and interaction with lipid membrane models of Semliki Forest virus fusion peptide.
Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Review
- Conjugative Coupling Proteins and the Role of Their Domains in Conjugation, Secondary Structure andFrontiers in molecular biosciences · 2020Article
- NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.Biochimica et biophysica acta. Biomembranes · 2018Article
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3 authors at 1 institution in 1 country.
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Abstract
Semliki Forest virus (SFV) is a well-characterized alphavirus that infects cells via endocytosis and an acid-triggered fusion step using class II fusion proteins. Membrane fusion is mediated by the viral spike protein, a heterotrimer of two transmembrane subunits, E1 and E2, and a peripheral protein, E3. Sequence analysis of the E1 ectodomain of a number of alphaviruses demonstrated the presence of a highly conserved hydrophobic domain on the E1 ectodomain. This sequence was proposed to be the fusion peptide of SFV and is believed to be the domain of E1 that interacts with the target membrane and triggers fusion. Here, we investigate the structure and the interaction with lipid membrane models of
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