ArticleMedChemComm2013
Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.
Article in MedChemComm, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 68 citations in OpenAlex.
- Article
- 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
- Click Chemistry Methodology: The Novel Paintbrush of Drug Design.ACS chemical biology · 2025Review
- In Vitro synergy of Farnesyltransferase inhibitors in combination with colistin against ESKAPE bacteria.PloS one · 2025Article
- Functional screening revealsmBio · 2023Article
- Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization.International journal of molecular sciences · 2022Review
- Lipoproteins and cancer: The role of HDL-C, LDL-C, and cholesterol-lowering drugs.Biochemical pharmacology · 2022Review
- RAC1 Activation as a Potential Therapeutic Option in Metastatic Cutaneous Melanoma.Biomolecules · 2021Review
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Molecular and Pharmacological Characterization of the Interaction between Human Geranylgeranyltransferase Type I and Ras-Related Protein Rap1B.International journal of molecular sciences · 2021Article
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- Bacteria Are New Targets for Inhibitors of Human Farnesyltransferase.Frontiers in microbiology · 2021Article
- Joining forces: Leveraging novel combination therapies to combat infections with eukaryotic pathogens.PLoS pathogens · 2020Article
- Inhibiting Fungal Echinocandin Resistance by Small-Molecule Disruption of Geranylgeranyltransferase Type I Activity.Antimicrobial agents and chemotherapy · 2020Article
- Targeting prenylation inhibition through the mevalonate pathway.RSC medicinal chemistry · 2020Review
- Differential requirements of protein geranylgeranylation for the virulence of human pathogenic fungi.Virulence · 2019Article
- The chaperone SmgGDS-607 has a dual role, both activating and inhibiting farnesylation of small GTPases.The Journal of biological chemistry · 2019Article
- Membrane Lipid Composition: Effect on Membrane and Organelle Structure, Function and Compartmentalization and Therapeutic Avenues.International journal of molecular sciences · 2019Review
- Ni(ii)-catalyzed mono-selectiveRSC advances · 2019Article
- Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor.Methods in enzymology · 2019Article
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 at 1 institution in 1 country.
Funding
Abstract
The posttranslational modification of protein prenylation is a covalent lipid modification on the C-terminus of substrate proteins that serves to enhance membrane affinity. Oncogenic proteins such as Ras have this modification and significant effort has been placed into developing inhibitors of the prenyltransferase enzymes for clinical therapy. In addition to cancer therapy, prenyltransferase inhibitors have begun to find important therapeutic uses in other diseases, including progeria, hepatitis C and D, parasitic infections, and other maladies. This review will trace the evolution of prenyltransferase inhibitors from their initial use as cancer therapeutics to their expanded applications for other diseases.
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.