ArticleNature2010
Single-molecule analysis of Mss116-mediated group II intron folding.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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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Who cites it
45 citing papers in PubMed, 80 citations in OpenAlex.
- Benchmarking dynamic analysis methods in diffusion-based single-molecule FRET.Cell reports methods · 2026Article
- Elucidating structure-function relationships in the mammalian nucleolus.Nature reviews. Molecular cell biology · 2026Review
- Disassembly of unstable RNA structures by an E. coli DEAD-box chaperone accelerates ribosome assembly.Nucleic acids research · 2025Article
- Two opposite abilities of the infectious bronchitis virus helicase Nsp13: separating the duplex and promoting the annealing of single-stranded nucleic acid.Frontiers in veterinary science · 2025Article
- Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.Biophysical journal · 2024Article
- Metal ions and sugar puckering balance single-molecule kinetic heterogeneity in RNA and DNA tertiary contacts.Nature communications · 2020Article
- Optimal molecular crowding accelerates group II intron folding and maximizes catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Expression and purification of nuclease-free protocatechuate 3,4-dioxygenase for prolonged single-molecule fluorescence imaging.Analytical biochemistry · 2018Article
- Normal mitochondrial function ineLife · 2018Article
- Specific phosphorothioate substitution within domain 6 of a group II intron ribozyme leads to changes in local structure and metal ion binding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the Dead-Box RNA Helicase Dbp2 at Actively Transcribed Chromatin.Journal of molecular biology · 2016Article
- A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo.RNA (New York, N.Y.) · 2016Article
- Analysis of Fluorescence Lifetime and Energy Transfer Efficiency in Single-Molecule Photon Trajectories of Fast-Folding Proteins.The journal of physical chemistry. B · 2016Article
- Article
- A transcriptomic analysis of Chrysanthemum nankingense provides insights into the basis of low temperature tolerance.BMC genomics · 2014Article
- Article
- DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Single-molecule fluorescence reveals the unwinding stepping mechanism of replicative helicase.Cell reports · 2014Article
- RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014Review
- Predicted group II intron lineages E and F comprise catalytically active ribozymes.RNA (New York, N.Y.) · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
DEAD-box helicases are conserved enzymes involved in nearly all aspects of RNA metabolism, but their mechanisms of action remain unclear. Here, we investigated the mechanism of the DEAD-box protein Mss116 on its natural substrate, the group II intron ai5γ. Group II introns are structurally complex catalytic RNAs considered evolutionarily related to the eukaryotic spliceosome, and an interesting paradigm for large RNA folding. We used single-molecule fluorescence to monitor the effect of Mss116 on folding dynamics of a minimal active construct, ai5γ-D135. The data show that Mss116 stimulates dynamic sampling between states along the folding pathway, an effect previously observed only with high Mg(2+) concentrations. Furthermore, the data indicate that Mss116 promotes folding through discrete ATP-independent and ATP-dependent steps. We propose that Mss116 stimulates group II intron folding through a multi-step process that involves electrostatic stabilization of early intermediates and ATP hydrolysis during the final stages of native state assembly.
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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.