Evidence map›Paper›PMID 27768305›Full record

ArticleJournal of the American Chemical Society2016

Self-Assembly of Catenanes from Lasso Peptides.

Caitlin D Allen, A James Link

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  3. Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Lasso Peptide Benenodin-1 Is a Thermally Actuated [1]Rotaxane Switch.Journal of the American Chemical Society · 2017
    Article
  20. Article
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

2 authors.

Caitlin D AllenDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
A James LinkDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.

Funding

Lasso Peptide DiscoveryR01GM107036 · NIGMS · PRINCETON UNIVERSITY · PI LINK, AARON JAMES · 2014 to 2022
$2.9M
NIGMS NIH HHS R01 GM107036
6 · The paper itself

Abstract

Lasso peptides exist naturally in a threaded state as [1]rotaxanes, and we reasoned that lasso peptides cleaved in their loop region could serve as building blocks for catenanes. Mutagenesis of the lasso peptide microcin J25 (MccJ25) with two cysteine residues followed by cleavage of the peptide with trypsin led to a [2]rotaxane structure that self-assembled into a [3]catenane and [4]catenanes at room temperature in aqueous solution. The [3]catenane represents the smallest ring size of a catenane composed solely of polypeptide segments. The NMR structure of the [3]catenane was determined, suggesting that burial of hydrophobic residues may be a driving force for assembly of the catenane structure.

Indexed as

AnimalsCatenanesModels, MolecularPeptidesProtein ConformationTemperatureCatenanesPeptides

Identifiers

PMID27768305
PMCPMC5245162

What OpenQuestion holds

Textmetadata
LicenceTDM
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.