Evidence map›Paper›PMID 41930951›Full record

ArticlemBio2026

AexB is an aromatic amino acid exporter that functions as a metabolic safety valve.

Blake A Everett, Arthur Prindle

Abstract read
In one paragraph

Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Blake A EverettDepartment of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Chicago, Illinois, USA.ORCID 0000-0001-6014-9163
Arthur PrindleDepartment of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Chicago, Illinois, USA.ORCID 0009-0004-2804-3077

Funding

Emergent metabolic coordination and cell-to-cell signaling in bacterial biofilms-ADMIN SUPP for EquipmentR35GM147170 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Arthur Prindle · 2022 to 2026
$2.1M
Army Research Office W911NF-19-1-013National Science Foundation NSF 2239567NIGMS NIH HHS R35 GM147170
6 · The paper itself

Abstract

Aromatic amino acids-tryptophan, tyrosine, phenylalanine, and histidine-are essential for bacterial growth and are among the most energetically expensive metabolites to synthesize. Despite this cost, it has been recently shown that bacteria possess exporters for these amino acids. Here, we identify IMPORTANCE: Identification and characterization of amino acid exporters is a broadly relevant topic. Amino acid synthesis is energetically costly, and thus functional relevance for their export is unintuitive. Identification of the molecular components that allow export may offer new engineering opportunities to improve biomanufacturing and metabolic engineering. Characterization of these exporters may also provide a more complete understanding of the human microbiome where amino acids, especially tryptophan, have been established as nodes of crosstalk between host and microbiota.

Indexed as

Amino Acids, AromaticAmino Acid Transport SystemsBacillus subtilisBacterial ProteinsTryptophanAmino Acids, AromaticAmino Acid Transport SystemsBacterial ProteinsTryptophanamino acidsBacillus subtilisbacteriametabolismtransporters

Identifiers

PMID41930951
PMCPMC13170310

What OpenQuestion holds

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LicenceCC BY
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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.