Evidence map›Paper›PMID 35787182›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Biosynthesis of 3-thia-α-amino acids on a carrier peptide.

Yue Yu, Wilfred A van der Donk

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.

  1. Pooled it
  2. Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Structural basis for iterative methylation by a cobalamin-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. PEARLs of wisdom for ribosome-independent peptide bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Review
  19. Biosynthesis of Macrocyclic Peptides by Formation and Crosslinking ofbioRxiv : the preprint server for biology · 2025
    Article
  20. Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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 1 institution in 1 country.

Yue YuDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.ORCID 0000-0001-8306-4648
Wilfred A van der DonkDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.ORCID 0000-0002-5467-7071
University of Illinois Urbana-Champaign · US

Funding

Posttranslational Modifications during Natural Product BiosynthesisR37GM058822 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2016 to 2025
$2.9M
Howard Hughes Medical Institute (HHMI) 079102NIGMS NIH HHS R37 GM058822
6 · The paper itself

Abstract

A subset of natural products, such as polyketides and nonribosomal peptides, is biosynthesized while tethered to a carrier peptide via a thioester linkage. Recently, we reported that the biosyntheses of 3-thiaglutamate and ammosamide, single amino acid-derived natural products, employ a very different type of carrier peptide to which the biosynthetic intermediates are bound via an amide linkage. During their biosyntheses, a peptide aminoacyl-transfer ribonucleic acid (tRNA) ligase (PEARL) first loads an amino acid to the C terminus of the carrier peptide for subsequent modification by other enzymes. Proteolytic removal of the modified C-terminal amino acid yields the mature product. We termed natural products that are biosynthesized using such pathways pearlins. To investigate the diversity of pearlins, in this study we experimentally characterized another PEARL-encoding biosynthetic gene cluster (BGC) from

Indexed as

Biological ProductsPeptide Biosynthesis, Nucleic Acid-IndependentPolyketidesAmino AcidsEscherichia coliPeptidesPeptide SynthasesRhodospirillaceaeS-AdenosylmethionineAmino AcidsBiological ProductsPeptidesPeptide SynthasesPolyketidesS-Adenosylmethionine3-thiahomoleucinecarrier proteinpearlinradical SAM methyltransferaseRiPP

Identifiers

PMID35787182
PMCPMC9303977
OpenAlexW4283830725

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.