Evidence map›Paper›PMID 33823110›Full record

ArticleJournal of the American Chemical Society2021

Cell-Free Biosynthesis to Evaluate Lasso Peptide Formation and Enzyme-Substrate Tolerance.

Yuanyuan Si, Ashley M Kretsch, Laura M Daigh, Mark J Burk, Douglas A Mitchell

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
10.0field-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

52 citing papers in PubMed, 83 citations in OpenAlex.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. De novo Folding Mechanisms of Lasso Peptides.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Structure of a lasso peptide bound ETNature communications · 2025
    Article
  14. Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. BeyondChemical reviews · 2025
    Review
  17. Article
  18. Article
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  20. Review
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

5 authors at 1 institution in 1 country.

Yuanyuan SiCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, Illinois 61801, United States of America.ORCID 0000-0001-6437-9249
Ashley M KretschCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, Illinois 61801, United States of America.ORCID 0000-0002-4320-6776
Laura M DaighCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, Illinois 61801, United States of America.ORCID 0000-0003-4676-1852
Mark J BurkLassogen, Inc., San Diego, California 92121, United States of America.ORCID 0000-0002-2045-2691
Douglas A MitchellCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, Illinois 61801, United States of America.ORCID 0000-0002-9564-0953
University of Illinois Urbana-Champaign · US

Funding

A Genes-to-Molecules Platform for Expanding Natural Product DiversityR41AT010852 · NCCIH · LASSOGEN, INC. · PI BURK, MARK J, MITCHELL, DOUGLAS ALAN · 2020 to 2020
$225k
NCCIH NIH HHS R41 AT010852
6 · The paper itself

Abstract

Lasso peptides are ribosomally synthesized and post-translationally modified peptide (RiPP) natural products that display a unique lariat-like, threaded conformation. Owing to a locked three-dimensional structure, lasso peptides can be unusually stable toward heat and proteolytic degradation. Some lasso peptides have been shown to bind human cell-surface receptors and exhibit anticancer properties, while others display antibacterial or antiviral activities. All known lasso peptides are produced by bacteria and genome-mining studies indicate that lasso peptides are a relatively prevalent class of RiPPs; however, the discovery, isolation, and characterization of lasso peptides are constrained by the lack of an efficient production system. In this study, we employ a cell-free biosynthesis (CFB) strategy to address longstanding challenges associated with lasso peptide production. We report the successful use of CFB for the formation of an array of sequence-diverse lasso peptides that include known examples as well as a new predicted lasso peptide from

Indexed as

Amino Acid SequenceBacterial ProteinsBiological ProductsCell-Free SystemCyclizationMultigene FamilyPeptide HydrolasesPeptidesProtein Processing, Post-TranslationalRibosomesSubstrate SpecificityThermobifidaBacterial ProteinsBiological ProductsPeptide HydrolasesPeptides

Identifiers

PMID33823110
PMCPMC8062304
OpenAlexW3128100426

What Socratic 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 Socratic graph.