ArticleScientific reports2017
Modelling the three-dimensional structure of the right-terminal domain of pospiviroids.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Derailing the host machinery to achieve replication: how viroid and viroid-like RNAs successfully copy their genomes in hostile territory.RNA biology · 2025Review
- Molecular Survey and Genetic Characterization of Hop Stunt Viroid (HSVd) in Fruit Trees in Kazakhstan.Viruses · 2025Article
- A nuclear import pathway exploited by pathogenic noncoding RNAs.The Plant cell · 2022Article
- Conserved Motifs and Domains in Members ofCells · 2022Article
- Predicting the Structure of a Viroid : Structure, Structure Distribution, Consensus Structure, and Structure Drawing.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Whole-Genome Deep Sequencing Reveals Host-DrivenInternational journal of molecular sciences · 2020Article
- In silico survey of the central conserved regions in viroids of theRNA (New York, N.Y.) · 2019Article
- Viroid research and its significance for RNA technology and basic biochemistry.Nucleic acids research · 2018Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viroids, the smallest know plant pathogens, consist solely of a circular, single-stranded, non-coding RNA. Thus for all of their biological functions, like replication, processing, and transport, they have to present sequence or structural features to exploit host proteins. Viroid binding protein 1 (Virp1) is indispensable for replication of pospiviroids, the largest genus of viroids, in a host plant as well as in protoplasts. Virp1 is known to bind at two sites in the terminal right (TR) domain of pospiviroids; each site consists of a purine- (R-) and a pyrimidine- (Y-)rich motif that are partially base-paired to each other. Here we model the important structural features of the domain and show that it contains an internal loop of two Y · Y cis Watson-Crick/Watson-Crick (cWW) pairs, an asymmetric internal loop including a cWW and a trans Watson/Hoogsteen pair, and a thermodynamically quite stable hairpin loop with several stacking interactions. These features are discussed in connection to the known biological functions of the TR domain.
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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.