Evidence map›Paper›PMID 25460269›Full record

ReviewCurrent opinion in structural biology2014

Structure and mechanism of lanthipeptide biosynthetic enzymes.

Wilfred A van der Donk, Satish K Nair

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Leveraging latent space models for enzyme discovery and sampling.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Structure and Activity of Class II Lanthipeptides From a Thermophilic Bacterium.Chembiochem : a European journal of chemical biology · 2026
    Article
  5. Article
  6. Article
  7. Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. RiPP Enzymes for Biosynthetically Derived Cyclic Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. Genome Mining ofMicroorganisms · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023
    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

2 authors.

Wilfred A van der DonkDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; The Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: vddonk@illinois.edu.
Satish K NairDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: s-nair@life.uiuc.edu.

Funding

Posttranslational Modifications in Natural Product BiosynthesisR01GM058822 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 1999 to 2015
$3.8M
Structural /Mechanistic Study of Lantibiotic Biosynthetic Enzymes & AutoimmunityR01GM079038 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI NAIR, SATISH K · 2006 to 2023
$3.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM 058822NIGMS NIH HHS R01 GM058822NIGMS NIH HHS R01 GM 079038NIGMS NIH HHS R01 GM079038
6 · The paper itself

Abstract

Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.

Indexed as

Protein Processing, Post-TranslationalAnti-Bacterial AgentsBacteriaBacteriocinsHydro-LyasesOxidoreductasesPeptide HydrolasesPeptidesProtein ConformationRibosomesAnti-Bacterial AgentsBacteriocinsepilancin 15XHydro-LyasesOxidoreductasesPeptide HydrolasesPeptides

Identifiers

PMID25460269
PMCPMC4267917

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.