ArticleNature communications2018
Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
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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
34 citing papers in PubMed, 54 citations in OpenAlex.
- Genome-wide mapping of DCP2-dependent 5' cap footprints inNAR genomics and bioinformatics · 2026Article
- Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.bioRxiv : the preprint server for biology · 2026Article
- Conserved and divergent features of human mRNA decapping revealed by biochemical reconstitution.Nature communications · 2026Article
- The trypanosome mRNA decapping enzyme ALPH1 prefers caps without m7G methylation and produces diphosphate RNA.Nucleic acids research · 2026Article
- Cytoplasmic mRNA decay and quality control machineries in eukaryotes.Nature reviews. Genetics · 2025Review
- Article
- Biochemical analysis of human eIF4E-DCP2 interaction: Implications for the relationship between translation initiation and decapping.PloS one · 2025Article
- Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functions.eLife · 2024Article
- Readers of RNA Modification in Cancer and Their Anticancer Inhibitors.Biomolecules · 2024Review
- Selective Characterization of mRNA 5' End-Capping by DNA Probe-Directed Enrichment with Site-Specific Endoribonucleases.ACS pharmacology & translational science · 2023Article
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- Structure and function of molecular machines involved in deadenylation-dependent 5'-3' mRNA degradation.Frontiers in genetics · 2023Review
- mRNA 5' terminal sequences drive 200-fold differences in expression through effects on synthesis, translation and decay.PLoS genetics · 2022Article
- Intrinsically disordered regions of tristetraprolin and DCP2 directly interact to mediate decay of ARE-mRNA.Nucleic acids research · 2022Article
- RNase H-based analysis of synthetic mRNA 5' cap incorporation.RNA (New York, N.Y.) · 2022Article
- Fluorescence-Based Activity Screening Assay Reveals Small Molecule Inhibitors of Vaccinia Virus mRNA Decapping Enzyme D9.ACS chemical biology · 2022Article
- Dcp2 C-terminaleLife · 2022Article
- Structure of the poxvirus decapping enzyme D9 reveals its mechanism of cap recognition and catalysis.Structure (London, England : 1993) · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Astrocytic IGF-1 and IGF-1R Orchestrate Mitophagy in Traumatic Brain Injury via Exosomal miR-let-7e.Oxidative medicine and cellular longevity · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The conserved decapping enzyme Dcp2 recognizes and removes the 5' eukaryotic cap from mRNA transcripts in a critical step of many cellular RNA decay pathways. Dcp2 is a dynamic enzyme that functions in concert with the essential activator Dcp1 and a diverse set of coactivators to selectively and efficiently decap target mRNAs in the cell. Here we present a 2.84 Å crystal structure of K. lactis Dcp1-Dcp2 in complex with coactivators Edc1 and Edc3, and with substrate analog bound to the Dcp2 active site. Our structure shows how Dcp2 recognizes cap substrate in the catalytically active conformation of the enzyme, and how coactivator Edc1 forms a three-way interface that bridges the domains of Dcp2 to consolidate the active conformation. Kinetic data reveal Dcp2 has selectivity for the first transcribed nucleotide during the catalytic step. The heterotetrameric Edc1-Dcp1-Dcp2-Edc3 structure shows how coactivators Edc1 and Edc3 can act simultaneously to activate decapping catalysis.
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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.