ArticlePlant direct2024
A phosphorylation-deficient ribosomal protein eS6 is largely functional in
Article in Plant direct, 2024. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Fully Tunable Phosphorylation of RPS6A Ensures the Successful Development of Arabidopsis Seedlings.Plant, cell & environment · 2026Article
- Proteomic Analysis of Mechanical Injury Effects in Papaya Fruit at Two Maturity Stages.Proteomes · 2025Article
- Phosphoglycerate dehydrogenase is required for kernel development and defines a predominant serine synthesis pathway in maize.The Plant cell · 2025Article
- DRMY1 promotes robust morphogenesis in Arabidopsis by sustaining the translation of cytokinin-signaling inhibitor proteins.Developmental cell · 2024Article
- START domains generate paralog-specific regulons from a single network architecture.Nature communications · 2024Article
- What, where, and how: Regulation of translation and the translational landscape in plants.The Plant cell · 2024Review
- A phosphorylation-deficient ribosomal protein eS6 is largely functional inPlant direct · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The eukaryote-specific ribosomal protein of the small subunit eS6 is phosphorylated through the target of rapamycin (TOR) kinase pathway. Although this phosphorylation event responds dynamically to environmental conditions and has been studied for over 50 years, its biochemical and physiological significance remains controversial and poorly understood. Here, we report data from
Indexed as
Identifiers
What OpenQuestion holds
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.