Evidence map›Paper›PMID 29533845›Full record

ReviewCurrent opinion in microbiology2018

RiPP antibiotics: biosynthesis and engineering potential.

Graham A Hudson, Douglas A Mitchell

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in Current opinion in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 102 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed, 1 pooled it
15.8field-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

102 citing papers in PubMed, 1 synthesis or guideline pooled it, 208 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Draft genome sequences of threeMicrobiology resource announcements · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026
    Article
  10. A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Graham A HudsonDepartment of Chemistry, University of Illinois, 600 S Mathews Ave, Urbana, IL 61801, United States.
Douglas A MitchellDepartment of Chemistry, University of Illinois, 600 S Mathews Ave, Urbana, IL 61801, United States; Carl R. Woese Institute for Genomic Biology, University of Illinois, 600 S Mathews Ave, Urbana, IL 61801, United States; Department of Microbiology, University of Illinois, 600 S Mathews Ave, Urbana, IL 61801, United States. Electronic address: douglasm@illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

Enzyme Chemistry and Biological Function of RiPP-like Modifications.R01GM097142 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2012 to 2024
$4.1M
NIGMS NIH HHS R01 GM097142
6 · The paper itself

Abstract

The threat of antibiotic resistant bacterial infections continues to underscore the need for new treatment options. Historically, small molecule metabolites from microbes have provided a rich source of antibiotic compounds, and as a result, significant effort has been invested in engineering the responsible biosynthetic pathways to generate novel analogs with attractive pharmacological properties. Unfortunately, biosynthetic stringency has limited the capacity of non-ribosomal peptide synthetases and polyketide synthases from producing substantially different analogs in large numbers. Another class of natural products, the ribosomally synthesized and post-translationally modified peptides (RiPPs), have rapidly expanded in recent years with many natively displaying potent antibiotic activity. RiPP biosynthetic pathways are modular and intrinsically tolerant to alternative substrates. Several prominent RiPPs with antibiotic activity will be covered in this review with a focus on their biosynthetic plasticity. While only a few RiPP enzymes have been thoroughly investigated mechanistically, this knowledge has already been harnessed to generate new-to-nature compounds. Through the use of synthetic biology approaches, on-going efforts in RiPP engineering hold great promise in unlocking the potential of this natural product class.

Indexed as

Anti-Bacterial AgentsBacteriaBacterial InfectionsBiosynthetic PathwaysHumansPeptidesProtein Processing, Post-TranslationalRibosomesAnti-Bacterial AgentsPeptides

Identifiers

PMID29533845
PMCPMC6131089
OpenAlexW2794743485

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.