ReviewInternational journal of molecular sciences2022
Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization.
Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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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
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.
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Who cites it
38 citing papers in PubMed, 47 citations in OpenAlex.
- Downregulation of prenylation machinery genes in peripheral blood of patients with Parkinson's disease: A pilot study.IBRO neuroscience reports · 2026Article
- Skeletal muscle-specific deficiency of Rab geranylgeranyl transferase beta subunit induces myopathy and exacerbates the symptoms caused by HMG-CoA reductase deficiency in mice.Molecular metabolism · 2026Article
- Farnesol and geranylgeraniol in plant reproduction: insights from Arabidopsis and beyond.Journal of experimental botany · 2026Review
- Renaissance of farnesyltransferase inhibitors in cancer.Journal of translational medicine · 2026Review
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
- The role of protein prenylation in kidney diseases: Molecular basis and therapeutic implications.Molecular biology reports · 2026Review
- Rab geranylgeranyl transferase activity is required for proper sterol biosynthesis in Arabidopsis thaliana.Plant & cell physiology · 2026Article
- Shared Plant-human Biology: Herbicide Effects and New Biomarkers Perspectives.Current environmental health reports · 2026Review
- Farnesyltransferase inhibitor LB42708 disables oncogenic RAS signaling and overcomes gefitinib resistance in NSCLC via FTase α-subunit and RAS degradation.Cell communication and signaling : CCS · 2026Article
- KLF2 Promotes Ellagic Acid-Mediated Osteogenic Differentiation of Dental Pulp-Derived Stem Cells via Autophagy and Mitochondrial Regulation.Diseases & research · 2026Article
- Comparative study of palmitoleic acid, sea buckthorn oil, and lovastatin in hepatocellular steatosis model.Scientific reports · 2026Article
- RHOA at the intersection of inflammation-driven and sporadic colorectal cancer.Frontiers in immunology · 2026Review
- Integrative computational approach to farnesyltransferase inhibition toward anti-liver cancer drug candidate fromMolecular biology research communications · 2026Article
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
- Modulating Subcellular Localization to Preserve the Stability and Functionality of Intracellular Nanobodies.Antibodies (Basel, Switzerland) · 2025Article
- Protein prenylation in islet β-cell function in health and metabolic stress.Biochemical pharmacology · 2025Review
- Protein Prenylation in Plants: Mechanisms and Functional Implications.Plants (Basel, Switzerland) · 2025Review
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Examining Farnesyltransferase Interaction With Cell-Permeable CaaX Peptides and the Role of the CaaX Motif in Biological Activity.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Synthesis, Bioproduction and Bioactivity of Perillic Acid-A Review.Molecules (Basel, Switzerland) · 2025Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein prenylation is a post-translational modification controlling the localization, activity, and protein-protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase-I), Rab geranylgeranyltransferase (GGTase-II), and recently discovered geranylgeranyltransferase type III (GGTase-III). Blocking small GTPase activity, namely inhibiting prenyltransferases, has been proposed as a potential disease treatment method. Inhibitors of prenyltransferase have resulted in substantial therapeutic benefits in various diseases, such as cancer, neurological disorders, and viral and parasitic infections. In this review, we overview the structure of FTase, GGTase-I, GGTase-II, and GGTase-III and summarize the current status of research on their inhibitors.
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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 Socratic graph.