ReviewPlants (Basel, Switzerland)2025
Protein Prenylation in Plants: Mechanisms and Functional Implications.
Review in Plants (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- From Isoprene Units to Polyprenols and Dolichols: 70 Years of Polyisoprenoid Biosynthesis Research.Cell biochemistry and biophysics · 2026Review
- Farnesol and geranylgeraniol in plant reproduction: insights from Arabidopsis and beyond.Journal of experimental botany · 2026Review
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Protein prenylation is a crucial post-translational modification that involves the formation of a covalent bond between isoprenoid lipids and the cysteine residues of specific proteins. This modification plays a significant role in determining protein localization, facilitating protein-protein interactions, and ultimately influencing protein function within the cellular context. Prenylation is a conserved process observed across various kingdoms of life, including plants, animals, fungi, and protists. This review aims to consolidate existing knowledge regarding the mechanisms underlying protein prenylation, encompassing the biosynthetic pathways of isoprenoids in plants and the processing involved in the prenylation modification. Furthermore, it highlights the implications of alterations in protein prenylation on plant development, signaling pathways, and stress responses. The review also addresses the similarities in modification mechanisms between plants and animals, as well as the diversity of their functional implications. Finally, it outlines prospective research directions of the plant prenylation mechanisms and the potential applications in the field of biotechnology.
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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.