Evidence map›Paper›PMID 30626643›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin.

Nathaniel R Braffman, Frank J Piscotta, Jesse Hauver, Elizabeth A Campbell, A James Link, Seth A Darst

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
10.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

79 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  6. RNA polymerase inhibitors reveal active-site motions essential for the nucleotide addition cycle.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. De novo Folding Mechanisms of Lasso Peptides.bioRxiv : the preprint server for biology · 2026
    Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Lasso Peptides-A New Weapon Against Superbugs.International journal of molecular sciences · 2025
    Review

19 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Nathaniel R BraffmanLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065.
Frank J PiscottaDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544.
Jesse HauverLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065.
Elizabeth A CampbellLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065.
A James LinkDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544.ORCID 0000-0001-5066-9691
Seth A DarstLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065; darst@rockefeller.edu.ORCID 0000-0002-8241-3153
Rockefeller University · USPrinceton University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structure, function, and regulation of the bacterial transcription cycleR35GM118130 · NIGMS · ROCKEFELLER UNIVERSITY · PI DARST, SETH A. · 2016 to 2025
$8.9M
Lasso Peptide DiscoveryR01GM107036 · NIGMS · PRINCETON UNIVERSITY · PI LINK, AARON JAMES · 2014 to 2022
$2.9M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Crystallization Robot for the Structural Biology Resource Center at RockefellerS10RR027037 · NCRR · ROCKEFELLER UNIVERSITY · PI OREN, DEENA ABELLS · 2010 to 2010
$147k
NCRR NIH HHS S10 RR027037NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM107036NIGMS NIH HHS R35 GM118130
6 · The paper itself

Abstract

We report crystal structures of the antibacterial lasso peptides microcin J25 (MccJ25) and capistruin (Cap) bound to their natural enzymatic target, the bacterial RNA polymerase (RNAP). Both peptides bind within the RNAP secondary channel, through which NTP substrates enter the RNAP active site, and sterically block trigger-loop folding, which is essential for efficient catalysis by the RNAP. MccJ25 binds deep within the secondary channel in a manner expected to interfere with NTP substrate binding, explaining the partial competitive mechanism of inhibition with respect to NTPs found previously [Mukhopadhyay J, Sineva E, Knight J, Levy RM, Ebright RH (2004)

Indexed as

Anti-Bacterial AgentsBacteriaBacteriocinsCatalytic DomainDNA-Directed RNA PolymerasesPeptidesProtein ConformationTranscription, GeneticAnti-Bacterial AgentsBacteriocinscapistruinDNA-Directed RNA PolymerasesmicrocinPeptidescapistruinlasso peptidemicrocin J25RNA polymeraseX-ray crystallography

Identifiers

PMID30626643
PMCPMC6347699
OpenAlexW2911011185

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.