ReviewiScience2025
The ubiquitin code of RAS proteins: Decoding its role in cancer progression.
Review in iScience, 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.
- Rewiring KRAS-driven cancers through the ubiquitin-proteasome system: therapeutic opportunities with a focus on deubiquitinase.Experimental & molecular medicine · 2026Review
- Non-canonical and constitutive activation of small GTPases: more than an exception to the rule?The Biochemical journal · 2026Review
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RAS proteins, as the most frequently mutated oncoproteins in human cancers, drive tumor proliferation, metastasis, and therapeutic resistance. Recent studies have revealed that ubiquitination dynamically regulates the stability, membrane localization, and signaling transduction of RAS proteins, profoundly impacting their oncogenic functions. A series of ubiquitination sites, E3 ligases, deubiquitinases, and regulatory proteins are involved in RAS ubiquitination. We also analyze the heterogeneity of ubiquitination patterns across distinct RAS isoforms (KRAS4A, KRAS4B, NRAS, and HRAS) and their functional disparities in cancers. Targeting the ubiquitination pathway offers novel strategies to overcome RAS proteins. Future research should integrate protein structure analysis and high-throughput screening to develop specific ubiquitination modulators and explore combination RAS ubiquitination targeting strategies with RAS inhibitors or immunotherapy, aiming to overcome RAS-driven malignant phenotypes.
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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.