ArticleProceedings of the National Academy of Sciences of the United States of America1991
Enzymatic modification of proteins with a geranylgeranyl isoprenoid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 170 citations in OpenAlex.
- Article
- Profiling of C-terminal prenylated proteins using tandem mass tagging.Methods in enzymology · 2025Article
- Cell biology of protein-lipid conjugation.Cell structure and function · 2023Review
- Prenyl Transferases Regulate Secretory Protein Sorting and Parasite Morphology inInternational journal of molecular sciences · 2023Article
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Metabolic labeling with an alkyne probe reveals similarities and differences in the prenylomes of several brain-derived cell lines and primary cells.Scientific reports · 2021Article
- Statins decrease the expression of c-Myc protein in cancer cell lines.Molecular and cellular biochemistry · 2021Article
- Protein Farnesyltransferase Catalyzes Unanticipated Farnesylation and Geranylgeranylation of Shortened Target Sequences.Biochemistry · 2020Article
- Review
- Optimization of Metabolic Labeling with Alkyne-Containing Isoprenoid Probes.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Biochemical significance of limonene and its metabolites: future prospects for designing and developing highly potent anticancer drugs.Bioscience reports · 2018Review
- Metabolic Labeling of Prenylated Proteins Using Alkyne-Modified Isoprenoid Analogues.Current protocols in chemical biology · 2018Article
- Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer's disease.Critical reviews in biochemistry and molecular biology · 2018Review
- a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity.Bioconjugate chemistry · 2018Article
- Molecular docking and simulation of Curcumin with Geranylgeranyl Transferase1 (GGTase1) and Farnesyl Transferase (FTase).Bioinformation · 2015Article
- A Homology Based Model and Virtual Screening of Inhibitors for Human Geranylgeranyl Transferase 1 (GGTase1).Bioinformation · 2013Article
- A prenylated p47phox-p67phox-Rac1 chimera is a Quintessential NADPH oxidase activator: membrane association and functional capacity.The Journal of biological chemistry · 2010Article
- A novel geranylgeranyl transferase inhibitor in combination with lovastatin inhibits proliferation and induces autophagy in STS-26T MPNST cells.The Journal of pharmacology and experimental therapeutics · 2010Article
- Synergistic actions of atorvastatin with gamma-tocotrienol and celecoxib against human colon cancer HT29 and HCT116 cells.International journal of cancer · 2010Article
- Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities.Journal of molecular biology · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prenylation of several proteins involved in oncogenesis and signal transduction plays an essential role in regulating their biological activities. Two distinct isoprenoids are known to be involved in this modification, the 15-carbon farnesyl and 20-carbon geranylgeranyl groups. Thus far, identified farnesylated proteins contain methionine or serine at the COOH terminus, while those modified by geranylgeranyl end in leucine. This report describes the characterization of an enzyme activity that transfers the geranylgeranyl group to candidate proteins. The enzyme, termed a "protein geranylgeranyltransferase," exhibits a marked preference for substrate proteins that contain leucine at the COOH terminus. In fact, the enzyme will efficiently modify a normally farnesylated protein, Ha-ras, if its COOH-terminal amino acid is switched from serine to leucine. Additional studies characterize this enzyme and suggest that it is responsible for the geranylgeranyl modification of a number of GTP-binding proteins (or their subunits) that contain a consensus prenylation sequence ending in leucine.
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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.