ReviewCellular and molecular life sciences : CMLS2009
New insights into short-chain prenyltransferases: structural features, evolutionary history and potential for selective inhibition.
Review in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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
63 citing papers in PubMed, 118 citations in OpenAlex.
- Review
- From Isoprene Units to Polyprenols and Dolichols: 70 Years of Polyisoprenoid Biosynthesis Research.Cell biochemistry and biophysics · 2026Review
- Whole-genome analyses illuminate demographic history and lineage differentiation of polymorphic swallowtail butterfly Papilio bootes.BMC genomics · 2026Article
- Genomic Analysis of Carotenoid and Vitamin E Biosynthetic Pathways in the Extremophilic Red AlgaAntioxidants (Basel, Switzerland) · 2025Article
- Sucrose supplementation influences gut microbial diversity and functional shifts inFrontiers in microbiology · 2025Article
- Systematic characterization and functional analysis ofFrontiers in plant science · 2025Article
- The Property of a Key Amino Acid Determines the Function of Farnesyl Pyrophosphate Synthase inCurrent issues in molecular biology · 2024Article
- Article
- Transcriptome Analyses Reveal the Aroma Terpeniods Biosynthesis Pathways ofInternational journal of molecular sciences · 2023Article
- Metal-dependent enzyme symmetry guides the biosynthetic flux of terpene precursors.Nature chemistry · 2023Article
- The functional evolution of architecturally different plant geranyl diphosphate synthases from geranylgeranyl diphosphate synthase.The Plant cell · 2023Article
- Volatile Composition and Classification ofInternational journal of molecular sciences · 2023Article
- A cytosolic bifunctional geranyl/farnesyl diphosphate synthase provides MVA-derived GPP for geraniol biosynthesis in rose flowers.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Emergence of terpene chemical communication in insects: Evolutionary recruitment of isoprenoid metabolism.Protein science : a publication of the Protein Society · 2023Article
- Comparative Genomic Analysis ofMicroorganisms · 2023Article
- Molecular characterization of cyanobacterial short-chain prenyltransferases and discovery of a novel GGPP phosphatase.The FEBS journal · 2022Article
- Functional Prediction ofInternational journal of molecular sciences · 2022Article
- Functional verification and characterization of a type-III geranylgeranyl diphosphate synthase gene fromFrontiers in microbiology · 2022Article
- Role of female-predominant MYB39-bHLH13 complex in sexually dimorphic accumulation of taxol inHorticulture research · 2022Article
- Metabolome and transcriptome associated analysis of sesquiterpenoid metabolism inFrontiers in plant science · 2022Article
3 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
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isoprenoids form an extensive group of natural products involved in a number of important biological processes. Their biosynthesis proceeds through sequential 1'-4 condensations of isopentenyl diphosphate (C5) with an allylic acceptor, the first of which is dimethylallyl diphosphate (C5). The reactions leading to the production of geranyl diphosphate (C10), farnesyl diphosphate (C15) and geranylgeranyl diphosphate (C20), which are the precursors of mono-, sesqui- and diterpenes, respectively, are catalyzed by a group of highly conserved enzymes known as short-chain isoprenyl diphosphate synthases, or prenyltransferases. In recent years, the sequences of many new prenyltransferases have become available, including those of several plant and animal geranyl diphosphate synthases, revealing novel mechanisms of product chain-length selectivity and an intricate evolutionary path from a putative common ancestor. Finally, there is considerable interest in designing inhibitors specific to short-chain prenyltransferases, for the purpose of developing new drugs or pesticides that target the isoprenoid biosynthetic pathway.
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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.