ArticleACS catalysis2018
Predicting Productive Binding Modes for Substrates and Carbocation Intermediates in Terpene Synthases-Bornyl Diphosphate Synthase as a Representative Case.
Article in ACS catalysis, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed.
- Chemoenzymatic Synthesis of (4R,7R)-Zingiberene Enables Construction of nor-Sesquiterpene Semiochemical Analogs.Chembiochem : a European journal of chemical biology · 2026Article
- Article
- Reinvestigation of the mechanism and selectivity of 1,8-cineole synthase usingChemical science · 2026Article
- A methionine-lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase.FEBS letters · 2026Article
- Dock & design: engineering specificity for an alternative pimaradiene outcome with theChemical science · 2026Article
- Peeking behind the carbocation: identification of (alternative) catalytic bases in the class II active site of conifer resin acid diterpene synthases.The Biochemical journal · 2026Article
- Docking in the Abies grandis abietaenol synthase to investigate the mechanism underlying conifer resin acid diterpene synthase evolution.The Biochemical journal · 2026Article
- Basic importance: mechanistic molecular modeling of theOrganic & biomolecular chemistry · 2026Article
- Template-Based Docking Using Automated Maximum Common Substructure Identification with EnzyDock: Mechanistic and Inhibitor Docking.Journal of chemical information and modeling · 2025Article
- Characterization and functional reconstruction of a highly productive germacrene A synthase from Liriodendron chinense.Plant biotechnology journal · 2025Article
- Physics-based modeling in the new era of enzyme engineering.Nature computational science · 2025Review
- Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues.Chemical communications (Cambridge, England) · 2025Review
- Fine-Tuning the Function of Farnesene Synthases for Selective Synthesis of Farnesene Stereoisomers.Journal of agricultural and food chemistry · 2024Article
- Article
- Cyclization mechanism of monoterpenes catalyzed by monoterpene synthases in dipterocarpaceae.Synthetic and systems biotechnology · 2024Article
- Mechanistic docking in terpene synthases using EnzyDock.Methods in enzymology · 2024Review
- Decoding Catalysis by Terpene Synthases.ACS catalysis · 2023Review
- Thirteen Dipterocarpoideae genomes provide insights into their evolution and borneol biosynthesis.Plant communications · 2022Article
- Investigation of Acid-Base Catalysis in Halimadienyl Diphosphate Synthase Involved inACS bio & med chem Au · 2022Article
- Predictive Engineering of Class I Terpene Synthases Using Experimental and Computational Approaches.Chembiochem : a European journal of chemical biology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Terpene synthases comprise a family of enzymes that convert acyclic oligo-isoprenyl diphosphates to terpene natural products with complex, polycyclic carbon backbones via the generation and protection of carbocation intermediates. To accommodate this chemistry, terpene synthase active sites generally are lined with alkyl and aromatic, i.e., nonpolar, sidechains. Predicting the correct, mechanistically relevant binding modes for entire terpene synthase reaction pathways remains an unsolved challenge. Here we describe a method for identifying such modes:
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.