ArticleNature structural & molecular biology2016
Structural basis of mRNA-cap recognition by Dcp1-Dcp2.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 62 citations in OpenAlex.
- Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodies.Journal of cell science · 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
- mRNA decapping enzyme2 DCP2 expression correlates with progression and prognosis of hepatocellular carcinoma.Scientific reports · 2025Article
- Aptamer-based assay for high-throughput substrate profiling of RNA decapping enzymes.Nucleic acids research · 2024Article
- Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functions.eLife · 2024Article
- Trinucleotide mRNA Cap AnalogueJournal of the American Chemical Society · 2024Article
- The Role of TGFBR3 in the Development of Lung Cancer.Protein and peptide letters · 2024Review
- Cordycepin delays postovulatory aging of oocytes through inhibition of maternal mRNAs degradation via DCP1A polyadenylation suppression.Cellular and molecular life sciences : CMLS · 2023Article
- MEX3B inhibits collagen production in eosinophilic nasal polyps by downregulating epithelial cell TGFBR3 mRNA stability.JCI insight · 2023Article
- Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- METTL3 promotes chemoresistance in small cell lung cancer by inducing mitophagy.Journal of experimental & clinical cancer research : CR · 2023Article
- Keeping development on time: Insights into post-transcriptional mechanisms driving oscillatory gene expression during vertebrate segmentation.Wiley interdisciplinary reviews. RNA · 2023Review
- Intrinsically disordered regions of tristetraprolin and DCP2 directly interact to mediate decay of ARE-mRNA.Nucleic acids research · 2022Article
- Non-canonical features of microRNAs: paradigms emerging from cardiovascular disease.Nature reviews. Cardiology · 2022Review
- YBX1 mediates alternative splicing and maternal mRNA decay during pre-implantation development.Cell & bioscience · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- miR-4293 upregulates lncRNA WFDC21P by suppressing mRNA-decapping enzyme 2 to promote lung carcinoma proliferation.Cell death & disease · 2021Article
- Discovery of cellular substrates of human RNA-decapping enzyme DCP2 using a stapled bicyclic peptide inhibitor.Cell chemical biology · 2021Article
- Pby1 is a direct partner of the Dcp2 decapping enzyme.Nucleic acids research · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Removal of the 5' cap on mRNA by the decapping enzyme Dcp2 is a critical step in 5'-to-3' mRNA decay. Understanding the structural basis of Dcp2 activity has been a challenge because Dcp2 is dynamic and has weak affinity for the cap substrate. Here we present a 2.6-Å-resolution crystal structure of a heterotrimer of fission yeast Dcp2, its essential activator Dcp1, and the human NMD cofactor PNRC2, in complex with a tight-binding cap analog. Cap binding is accompanied by a conformational change in Dcp2, thereby forming a composite nucleotide-binding site comprising conserved residues in the catalytic and regulatory domains. Kinetic analysis of PNRC2 revealed that a conserved short linear motif enhances both substrate affinity and the catalytic step of decapping. These findings explain why Dcp2 requires a conformational change for efficient catalysis and reveals that coactivators promote RNA binding and the catalytic step of decapping, possibly through different conformational states.
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.