Evidence map›Paper›PMID 31751505›Full record

ArticleJournal of the American Chemical Society2019

Nonribosomal Peptide Extension by a Peptide Amino-Acyl tRNA Ligase.

Zhengan Zhang, Wilfred A van der Donk

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. PEARLs of wisdom for ribosome-independent peptide bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Unexpected Transformations during Pyrroloiminoquinone Biosynthesis.Journal of the American Chemical Society · 2024
    Article
  9. Review
  10. Unexpected transformations during pyrroloiminoquinone biosynthesis.bioRxiv : the preprint server for biology · 2024
    Article
  11. Review
  12. Review
  13. Biosynthesis of 3-thia-α-amino acids on a carrier peptide.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Substrate Recognition by the Peptidyl-(ACS chemical biology · 2022
    Article
  15. Article
  16. A [3Fe-4S] cluster and tRNA-dependent aminoacyltransferase BlsK in the biosynthesis of Blasticidin S.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Review
  18. Review
  19. 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 at 2 institutions in 1 country.

Zhengan ZhangDepartment of Chemistry , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.ORCID 0000-0003-3993-1163
Wilfred A van der DonkDepartment of Chemistry , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.ORCID 0000-0002-5467-7071
Howard Hughes Medical Institute · USUniversity of Illinois Urbana-Champaign · US

Funding

Posttranslational Modifications in Natural Product BiosynthesisR01GM058822 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 1999 to 2015
$3.8M
Posttranslational Modifications during Natural Product BiosynthesisR37GM058822 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2016 to 2025
$2.9M
NIGMS NIH HHS R01 GM058822NIGMS NIH HHS R37 GM058822
6 · The paper itself

Abstract

The catalytic use of a small peptide scaffold for the biosynthesis of amino acid-derived natural products is a recently discovered new biosynthetic strategy. During this process, a peptide-amino acyl tRNA ligase (PEARL) adds amino acids to the C-terminus of a small peptide scaffold in an ATP- and tRNA-dependent process. The mechanism of this unusual transformation is currently not known. In this study, we present a detailed biochemical and mechanistic study of TglB (UniProtKB-F3HQJ1), a PEARL that catalyzes the addition of Cys to the C-terminus of the peptide TglA in the biosynthesis of 3-thiaglutamate in the plant pathogen

Indexed as

BiocatalysisModels, MolecularPeptidesProtein ConformationRNA Ligase (ATP)RNA, Transfer, Amino AcylPeptidesRNA Ligase (ATP)RNA, Transfer, Amino Acyl

Identifiers

PMID31751505
PMCPMC6927032
OpenAlexW2989809047

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.