ArticleFrontiers in plant science2014
Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling.
Article in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 24 citations in OpenAlex.
- Viroids: Non-Coding Circular RNAs Able to Autonomously Replicate and Infect Higher Plants.Biology · 2023Review
- Effect of VIRP1 Protein on Nuclear Import of Citrus Exocortis Viroid (CEVd).Biomolecules · 2021Article
- Time-Resolved Observation of the Destination of Microinjected Potato Spindle Tuber Viroid (PSTVd) in the Abaxial Leaf Epidermal Cells ofMicroorganisms · 2020Article
- Emergence of Intronless Evolutionary Forms of Stress Response Genes: Possible Relation to Terrestrial Adaptation of Green Plants.Frontiers in plant science · 2019Article
- Innate Immunity Activation and RNAi Interplay in Citrus Exocortis Viroid-Tomato Pathosystem.Viruses · 2018Article
- Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31.Planta · 2017Article
- What has been happening with viroids?Virus genes · 2014Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Originally isolated as a result of its ability to interact with the movement protein of Tomato spotted wilt virus in a yeast two-hybrid system, the 4/1 protein is proving to be an excellent tool for studying intracellular protein trafficking and intercellular communication. Expression of 4/1 in vivo is tightly regulated, first appearing in the veins of the cotyledon and later in the vasculature of the leaf and stem in association with the xylem parenchyma and phloem parenchyma. Structural studies indicate that 4/1 proteins contain as many as five coiled-coil (CC) domains; indeed, the highest level of sequence identity among 4/1 proteins involves their C-terminal CC domains, suggesting that protein-protein interaction is important for biological function. Recent data predict that the tertiary structure of this C-terminal CC domain is strikingly similar to that of yeast protein She2p; furthermore, like She2p, 4/1 protein exhibits RNA-binding activity, and mutational analysis has shown that the C-terminal CC domain is responsible for RNA binding. The 4/1 protein contains a nuclear export signal. Additional microscopy studies involving leptomycin and computer prediction suggest the presence of a nuclear localization signal as well.
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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.