ReviewChimia2026
Expanding Biological Roles of Post-translational Arginylation.
Review in Chimia, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Protein arginylation is a conserved post-translational modification in eukaryotes, involving the conjugation of arginine residues to proteins by the enzyme arginyl-tRNA transferase. Historically associated with targeted degradation, recent studies have expanded this view by uncovering its broader regulatory influence across diverse cellular functions. This review first examines the established roles of arginylation in protein degradation through the Ubiquitin-Proteasome System and Autophagy-Lysosome System. It then highlights its non-degradative functions, including the modulation of protein-protein interactions, complex assembly, protein stability, and crosstalk with other post-translational modifications. Emerging evidence supports the notion that arginylation functions in a context dependent manner, simultaneously affecting both the stability and functional behaviour of proteins. Together, these works reveal arginylation as a dynamic and versatile mechanism that extends well beyond proteolysis, positioning it as a key global regulator of cellular functioning.
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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.