ArticleCell2013
Structural basis of transcriptional pausing in bacteria.
Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 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
103 citing papers in PubMed, 151 citations in OpenAlex.
- The -10 region adjacent to open reading frames is a common expression pattern inLife science alliance · 2025Article
- Structural insights into polymerase-catalyzed FAD capping of hepatitis C virus RNA.Nature communications · 2025Article
- Clues to transcription/replication collision-induced DNA damage: it was RNAP, in the chromosome, with the fork.FEBS letters · 2025Review
- Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.Nature structural & molecular biology · 2024Article
- Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.Nucleic acids research · 2024Article
- Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.bioRxiv : the preprint server for biology · 2024Article
- Variability of Inverted Repeats in All Available Genomes of Bacteria.Microbiology spectrum · 2023Article
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- Allosteric mechanism of transcription inhibition by NusG-dependent pausing of RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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- Structural basis of RNA polymerase inhibition by viral and host factors.Nature communications · 2021Article
- Clusters of hairpins induce intrinsic transcription termination in bacteria.Scientific reports · 2021Article
- Residence time analysis of RNA polymerase transcription dynamics: A Bayesian sticky HMM approach.Biophysical journal · 2021Article
- RNA polymerase clamp conformational dynamics: long-lived states and modulation by crowding, cations, and nonspecific DNA binding.Nucleic acids research · 2021Article
- Nascent RNA sequencing identifies a widespread sigma70-dependent pausing regulated by Gre factors in bacteria.Nature communications · 2021Article
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- Basic mechanisms and kinetics of pause-interspersed transcript elongation.Nucleic acids research · 2021Review
- Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ.Science (New York, N.Y.) · 2021Article
- Stringent control of the RNA-dependent RNA polymerase translocation revealed by multiple intermediate structures.Nature communications · 2020Article
43 more citing papers are in PubMed but not listed here.
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 1 country.
Funding
Abstract
Transcriptional pausing by multisubunit RNA polymerases (RNAPs) is a key mechanism for regulating gene expression in both prokaryotes and eukaryotes and is a prerequisite for transcription termination. Pausing and termination states are thought to arise through a common, elemental pause state that is inhibitory for nucleotide addition. We report three crystal structures of Thermus RNAP elemental paused elongation complexes (ePECs). The structures reveal the same relaxed, open-clamp RNAP conformation in the ePEC that may arise by failure to re-establish DNA contacts during translocation. A kinked bridge-helix sterically blocks the RNAP active site, explaining how this conformation inhibits RNAP catalytic activity. Our results provide a framework for understanding how RNA hairpin formation stabilizes the paused state and how the ePEC intermediate facilitates termination.
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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.