ArticleInternational journal of molecular sciences2020
Spectroscopic Investigation of the Kinetic Mechanism Involved in the Association of Potyviral VPg with the Host Plant Translation Initiation Factor eIF4E.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Conserved Arginine of the Potyviridae Viral Genome-Linked Proteins (VPg) as a Key Determinant for eIF4E Binding.International journal of molecular sciences · 2026Article
- Article
- The Naturally Occurring Amino Acid Substitution in the VPg α1-α2 Loop Breaks eIF4E-Mediated Resistance to PRSV by Enabling VPg to Re-Hijack Another eIF4E Isoform eIF(iso)4E in Watermelon.Molecular plant pathology · 2024Article
- Protein Nucleotidylylation in +ssRNA Viruses.Viruses · 2021Review
- Phosphorylation of eukaryotic initiation factor eIFiso4E enhances the binding rates to VPg of turnip mosaic virus.PloS one · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The infectious cycle of potyviruses requires the formation of a complex between the viral genome-linked protein VPg and the host eukaryotic translation initiation factor 4E, eIF4E. Mutations associated with plant resistance to potyviruses were previously mapped at the eIF4E surface, while on the virus side, mutations leading to plant resistance breaking were identified within the VPg. In the present study, fluorescence spectroscopy was used to probe the contribution of the VPg intrinsically disordered region bearing amino acids determinant of the resistance breaking, to the VPg-eIF4E binding mechanism. Synthetic peptides encompassing the VPg
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