Evidence map›Paper›PMID 30673909›Full record

ReviewJournal of industrial microbiology & biotechnology2019

Refining and expanding nonribosomal peptide synthetase function and mechanism.

Matt McErlean, Jonathan Overbay, Steven Van Lanen

Abstract readReview
In one paragraph

Review in Journal of industrial microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Antimicrobial Activity ofInternational journal of molecular sciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Microbial metabolites: cause or consequence in gastrointestinal disease?American journal of physiology. Gastrointestinal and liver physiology · 2022
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

3 authors.

Matt McErleanDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, 40536, USA.
Jonathan OverbayDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, 40536, USA.
Steven Van LanenDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, 40536, USA. svanlanen@uky.edu.

Funding

Biosynthesis of nucleoside antibiotics targeting bacterial translocase IR01AI087849 · NIAID · UNIVERSITY OF KENTUCKY · PI VAN LANEN, STEVEN GARY · 2011 to 2020
$3.3M
Studies to understand and exploit 10-membered enediyne biosynthesisR01CA217255 · NCI · UNIVERSITY OF KENTUCKY · PI PHILLIPS, GEORGE NEAL, THORSON, JON SCOTT · 2017 to 2021
$2.6M
Biosynthesis and medicinal chemistry of the capuramycin antimycobacterial antibioticsR01AI128862 · NIAID · UNIVERSITY OF KENTUCKY · PI THORSON, JON SCOTT, VAN LANEN, STEVEN GARY · 2017 to 2021
$1.0M
NCI NIH HHS CA217255NCI NIH HHS R01 CA217255NIAID NIH HHS R01 AI087849NIAID NIH HHS R01 AI128862
6 · The paper itself

Abstract

Nonribosomal peptide synthetases (NRPSs) are involved in the biosynthesis of numerous peptide and peptide-like natural products that have been exploited in medicine, agriculture, and biotechnology, among other fields. As a consequence, there have been considerable efforts aimed at understanding how NRPSs orchestrate the assembly of these natural products. This review highlights several recent examples that continue to expand upon the fundamental knowledge of NRPS mechanism and includes (1) the discovery of new NRPS substrates and the mechanism by which these sometimes structurally complex substrates are made, (2) the characterization of new NRPS activities and domains that function during the process of peptide assembly, and (3) the various catalytic strategies that are utilized to release the NRPS product. These findings continue to strengthen the predictive power for connecting genes to products, thereby facilitating natural product discovery and development in the Genomics Era.

Indexed as

BacteriaBiosynthetic PathwaysCarrier ProteinsGenome, BacterialKeto AcidsMethylationMultigene FamilyOxidation-ReductionPeptidesPeptide SynthasesS-AdenosylmethionineCarrier ProteinsKeto Acidsnon-ribosomal peptide synthasePeptidesPeptide SynthasesS-AdenosylmethionineBioinformaticsDiscoveryDomainMechanismNatural productsNRPS

Identifiers

PMID30673909
PMCPMC6460464

What OpenQuestion holds

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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.