Evidence map›Paper›PMID 41575181›Full record

ArticleJournal of the American Chemical Society2026

Radical

Bach X Nguyen, Melissa M Bollmeyer, Hai Nguyen, Sergey Milikisiyants, Alex I Smirnov, R David Britt, Kenichi Yokoyama

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Emerging classes of copper enzymes.Current opinion in chemical biology · 2026
    Review
  2. The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. 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

7 authors.

Bach X NguyenDepartment of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Melissa M BollmeyerDepartment of Chemistry, University of California, Davis, Davis, California 95616, United States.
Hai NguyenDepartment of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Sergey MilikisiyantsDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Alex I SmirnovDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.ORCID 0000-0002-0037-2555
R David BrittDepartment of Chemistry, University of California, Davis, Davis, California 95616, United States.ORCID 0000-0003-0889-8436
Kenichi YokoyamaDepartment of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, United States.ORCID 0000-0001-5625-469X

Funding

Supplement:Spectroscopy Investigations of Metalloenzyme MechanismsR35GM126961 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI R. David Britt · 2018 to 2026
$3.7M
Mechanism of cofactor biosynthesis required for chronic bacterial infectionR01GM112838 · NIGMS · DUKE UNIVERSITY · PI YOKOYAMA, KENICHI · 2015 to 2023
$2.8M
Functions and mechanisms of metalloenzymes in natural product and cofactor biosynthesisR35GM161291 · NIGMS · DUKE UNIVERSITY · PI Kenichi Yokoyama · 2026 to 2026
$737k
Upgrade of Bruker Time-domain EPR SpectrometerS10OD032355 · OD · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI SMIRNOV, ALEX I. · 2022 to 2022
$600k
Time-domain/ELDOR EPR SpectrometerS10RR023614 · NCRR · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI SMIRNOV, ALEX I. · 2009 to 2009
$500k
NCRR NIH HHS S10 RR023614NIGMS NIH HHS R01 GM112838NIGMS NIH HHS R35 GM126961NIGMS NIH HHS R35 GM161291NIH HHS S10 OD032355
6 · The paper itself

Abstract

Darobactins are ribosomally synthesized and post-translationally modified peptides (RiPPs) with potent activity against Gram-negative pathogens. Their antibiotic function depends on a distinctive β-strand architecture stabilized by an ether cross-link between two tryptophan residues. Unlike most ether linkages in natural products, which arise from hydroxylated precursors, the darobactin ether bond is formed between two unmodified Trp residues by the radical

Indexed as

EthersOxygenasesS-AdenosylmethionineTryptophanFree RadicalsModels, MolecularEthersFree RadicalsOxygenasesS-AdenosylmethionineTryptophan

Identifiers

PMID41575181
PMCPMC12887971

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.