ArticleiScience2025
Functional-proteomics-based investigation of the cellular response to farnesyltransferase inhibition in lung cancer.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
The trial behind it
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Who cites it
7 citing papers in PubMed.
- Differential protein expression analysis of quantitative mass spectrometry data using DEqMS.Nature protocols · 2026Review
- Functional profiling of ovarian cancer models reveals Bcl-xL/NOTCH targeting to overcome resistance.NPJ precision oncology · 2026Article
- Renaissance of farnesyltransferase inhibitors in cancer.Journal of translational medicine · 2026Review
- Organotellurium Probes Enable One-step Single-cell Analysis of Post-translational Modification.Journal of the American Chemical Society · 2026Article
- Integrative computational approach to farnesyltransferase inhibition toward anti-liver cancer drug candidate fromMolecular biology research communications · 2026Article
- Protein farnesylation: from molecular mechanisms to therapeutic targeting in cancer, aging, and beyond.Frontiers in pharmacology · 2026Review
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Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Farnesylation is a lipid post-translational modification of proteins crucial for protein membrane anchoring and cellular signaling. Farnesyltransferase inhibitors (FTIs), such as tipifarnib, are being tested in cancer therapy. However, the full impact of FTIs on farnesylation substrates remains poorly understood, thus limiting their use in precision medicine. In this study, we performed a global proteomics analysis to investigate farnesylation and the effects of tipifarnib in lung cancer cell lines. Using metabolic labeling and mass spectrometry, we identified farnesylated proteins and mapped their subcellular localization. We also analyzed tipifarnib-dependent protein relocalization and proteome-wide changes. Key findings include the potential therapeutic value of FTIs for NRAS-mutated melanoma and GNAQ/GNA11-mutated uveal melanoma by inhibiting INPP5A farnesylation. Additionally, we identified a synergistic drug combination involving tipifarnib and a ferroptosis inducer and discovered PTP4A1 as a regulator of interferon signaling. Our data, covering 15,080 proteins, offer valuable insights for future studies of farnesylation and FTIs.
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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.