Evidence map›Paper›PMID 42224144›Full record

ArticleThe Journal of organic chemistry2026

Investigating the P450-Mediated Cross-Linking of the Atypical GPA Complestatin Using Alternate Peptide Probes.

Jemma Gullick, Hülya Aldemir, Yongwei Zhao, Manuel Einsiedler, Y T Candace Ho, Ralf B Schittenhelm, Julien Tailhades, Tobias A M Gulder, Max J Cryle

Abstract read
In one paragraph

Article in The Journal of organic chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

Jemma GullickDepartment of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.
Hülya AldemirChair of Technical Biochemistry, Technische Universität Dresden, Bergstraße 66, 01069 Dresden, Germany.
Yongwei ZhaoDepartment of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.
Manuel EinsiedlerChair of Technical Biochemistry, Technische Universität Dresden, Bergstraße 66, 01069 Dresden, Germany.ORCID 0000-0001-5275-3758
Y T Candace HoDepartment of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.
Ralf B SchittenhelmDepartment of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.ORCID 0000-0001-8738-1878
Julien TailhadesDepartment of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.ORCID 0000-0003-0391-2526
Tobias A M GulderDepartment of Natural Product Biotechnology, Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), PharmaScienceHub (PSH), Helmholtz Centre for Infection Research (HZI) and Department of Pharmacy at Saarland University, Campus E8.1, 66123 Saarbrücken, Germany.ORCID 0000-0001-6013-3161
Max J CryleDepartment of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.ORCID 0000-0002-9739-6157

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycopeptide antibiotics (GPAs) are clinically relevant antibiotics defined by their highly cross-linked structure, which is required for their antimicrobial activity. While GPAs are typically characterized as type I-IV GPAs - heptapeptides that bind to the d-Ala-d-Ala terminus of Lipid II - an expansion of these subtypes has recently been seen for type V GPAs that possess altered structural characteristics and mechanisms of action. The major structural changes seen with this class are due to varied cross-linking occurring between the aromatic side chain residues, with these cross-links installed by cytochrome P450 (Oxy) enzymes that are recruited to the peptide substrate during nonribosomal peptide synthesis by a specialized recruitment domain, known as the X-domain. Given the importance of these cross-links for the structural rigidity and activity of GPAs,

Indexed as

Anti-Bacterial AgentsCross-Linking ReagentsCytochrome P-450 Enzyme SystemGlycopeptidesPeptidesAnti-Bacterial AgentsCross-Linking ReagentsCytochrome P-450 Enzyme SystemGlycopeptidesPeptides

Identifiers

PMID42224144
PMCPMC13271087

What OpenQuestion holds

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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.