ReviewThe Journal of biological chemistry2016
cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases.
Review in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 87 citations in OpenAlex.
- High Rate of Recurrent De Novo Mutations in Developmental and Epileptic Encephalopathies.American journal of human genetics · 2017Pooled it
- From Isoprene Units to Polyprenols and Dolichols: 70 Years of Polyisoprenoid Biosynthesis Research.Cell biochemistry and biophysics · 2026Review
- Mysterious giants in the world of lipids: long linear isoprenoid functions in plant physiology and reproduction.Journal of experimental botany · 2026Review
- Impaired glycosylation promotes rapid transition to hepatocellular carcinoma in model of diet-induced steatotic liver disease.The Journal of clinical investigation · 2026Article
- Evolutionary divergence and functional insights into the heteromeric cis-prenyltransferase of Paramecium tetraurelia.The FEBS journal · 2026Article
- Article
- Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex.Nature communications · 2025Article
- Rubber biosynthesis drives the biogenesis and development of rubber particles, the rubber-producing organelles.Plant biotechnology journal · 2025Article
- Identifying and quantifying membrane interactions of the protein human cis-prenyltransferase.Protein science : a publication of the Protein Society · 2025Article
- The cis-prenyltransferase protein family in Taraxacum koksaghyz.The Plant journal : for cell and molecular biology · 2025Article
- Genome-Wide Analysis of the Cis-Prenyltransferase (CPT) Gene Family inPlants (Basel, Switzerland) · 2025Article
- Article
- Loss of cis-PTase function in the liver promotes a highly penetrant form of fatty liver disease that rapidly transitions to hepatocellular carcinoma.bioRxiv : the preprint server for biology · 2023Article
- A Dhdds K42E knock-in RP59 mouse model shows inner retina pathology and defective synaptic transmission.Cell death & disease · 2023Article
- Structural basis for long-chain isoprenoid synthesis byScience advances · 2022Article
- De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.Brain : a journal of neurology · 2022Article
- cis-prenyltransferase 3 and α/β-hydrolase are new determinants of dolichol accumulation in Arabidopsis.Plant, cell & environment · 2022Article
- Glycoconjugate journal special issue on: the glycobiology of Parkinson's disease.Glycoconjugate journal · 2022Review
- Synthesis, function, and regulation of sterol and nonsterol isoprenoids.Frontiers in molecular biosciences · 2022Review
- Complex Neurological Phenotype Associated with a De NovoJournal of pediatric genetics · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
cis-Prenyltransferases (cis-PTs) constitute a large family of enzymes conserved during evolution and present in all domains of life. cis-PTs catalyze consecutive condensation reactions of allylic diphosphate acceptor with isopentenyl diphosphate (IPP) in the cis (Z) configuration to generate linear polyprenyl diphosphate. The chain lengths of isoprenoid carbon skeletons vary widely from neryl pyrophosphate (C10) to natural rubber (C>10,000). The homo-dimeric bacterial enzyme, undecaprenyl diphosphate synthase (UPPS), has been structurally and mechanistically characterized in great detail and serves as a model for understanding the mode of action of eukaryotic cis-PTs. However, recent experiments have revealed that mammals, fungal, and long-chain plant cis-PTs are heteromeric enzymes composed of two distantly related subunits. In this review, the classification, function, and evolution of cis-PTs will be discussed with a special emphasis on the role of the newly described NgBR/Nus1 subunit and its plants' orthologs as essential, structural components of the cis-PTs activity.
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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.