ReviewNature chemical biology2006
Therapeutic intervention based on protein prenylation and associated modifications.
Review in Nature chemical biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 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
84 citing papers in PubMed, 191 citations in OpenAlex.
- Phytochemistry and Pharmacological Potential of the GenusPharmaceuticals (Basel, Switzerland) · 2026Review
- Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Stem cell-associated osteogenic deficiency causes craniofacial deformities with progeroid accumulation of prelamin A.JCI insight · 2026Article
- Artificial lipidation of proteins and peptides: from mechanism to clinical applications.The FEBS journal · 2026Review
- Novel GαGTP Sensors Reveal Endogenous and Subcellular G Protein Signaling Dynamics.bioRxiv : the preprint server for biology · 2026Article
- De Novo Discovery of Prenylated Macrocyclic Peptide Ligands.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Farnesol, the farnesol pathway, and the immune-gut-brain axis.Frontiers in pharmacology · 2026Review
- Immunomodulatory effects of atorvastatin on peripheral blood mononuclear cells infected withFrontiers in immunology · 2025Article
- Roles of the lamin A-specific tail region in the localization to sites of nuclear envelope rupture.PNAS nexus · 2024Article
- Protein lipidation in health and disease: molecular basis, physiological function and pathological implication.Signal transduction and targeted therapy · 2024Review
- Article
- CaaX-motif adjacent residues control G protein prenylation under suboptimal conditions.bioRxiv : the preprint server for biology · 2023Article
- Polyisoprenylated cysteinyl amide inhibitors deplete singly polyisoprenylated monomeric G-proteins in lung and breast cancer cell lines.Oncotarget · 2023Article
- Photoswitchable Isoprenoid Lipids Enable Optical Control of Peptide Lipidation.ACS chemical biology · 2022Article
- Combining Isoprenoid Probes with Antibody Markers for Mass Cytometric Analysis of Prenylation in Single Cells.Analytical chemistry · 2022Article
- Analyzing the postulated inhibitory effect of Manumycin A on farnesyltransferase.Frontiers in chemistry · 2022Article
- Tyrosine phosphorylation of lamin A by Src promotes disassembly of nuclear lamina in interphase.Life science alliance · 2021Article
- Review
- Protein farnesylation negatively regulates brassinosteroid signaling via reducing BES1 stability in Arabidopsis thaliana.Journal of integrative plant biology · 2021Article
- Subtype-dependent regulation of Gβγ signalling.Cellular signalling · 2021Review
24 more citing papers are in PubMed but not listed here.
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 at 5 institutions in 2 countries.
Funding
Abstract
In eukaryotic cells, a specific set of proteins are modified by C-terminal attachment of 15-carbon farnesyl groups or 20-carbon geranylgeranyl groups that function both as anchors for fixing proteins to membranes and as molecular handles for facilitating binding of these lipidated proteins to other proteins. Additional modification of these prenylated proteins includes C-terminal proteolysis and methylation, and attachment of a 16-carbon palmitoyl group; these modifications augment membrane anchoring and alter the dynamics of movement of proteins between different cellular membrane compartments. The enzymes in the protein prenylation pathway have been isolated and characterized. Blocking protein prenylation is proving to be therapeutically useful for the treatment of certain cancers, infection by protozoan parasites and the rare genetic disease Hutchinson-Gilford progeria syndrome.
Indexed as
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.