Evidence map›Paper›PMID 42127265›Full record

ArticleJournal of the American Chemical Society2026

Covalent Chemical Tagging of Transmembrane Transport Proteins Illuminates the Internalization Pathways of Xenosiderophores.

Minhua Cao, Marie Huynh, Inokentijs Josts, Yichong Lao, Hung H Dang, Axia Marlin, Xuhui Huang, Henning Tidow, Eszter Boros

Abstract read
PubMed Full text at PMC Publisher
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. 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

9 authors.

Minhua CaoDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.
Marie HuynhDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.ORCID 0000-0001-7304-1119
Inokentijs JostsThe Hamburg Advanced Research Center for Bioorganic Chemistry, Hamburg 22761, Germany.
Yichong LaoDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.
Hung H DangDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.
Axia MarlinDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.
Xuhui HuangDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.ORCID 0000-0002-7119-9358
Henning TidowThe Hamburg Advanced Research Center for Bioorganic Chemistry, Hamburg 22761, Germany.
Eszter BorosDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53705, United States.ORCID 0000-0002-4186-6586

Funding

Laser-Enhanced NMR Instrumentation for Chemical and Biochemical ResearchS10OD012245 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI CAVAGNERO, SILVIA · 2013 to 2013
$1.0M
QExactive (Orbitrap) mass spectrometerS10OD020022 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI VESTLING, MARTHA M · 2015 to 2015
$483k
NIH HHS S10 OD012245NIH HHS S10 OD020022
6 · The paper itself

Abstract

Siderophore-mediated, transmembrane uptake of iron in bacteria is a complex mechanism of essential nutrient acquisition. In addition to transporters that specifically recognize and shuttle endogenous siderophores, bacteria possess transmembrane transporters that efficiently internalize siderophore-metal complexes produced by other organisms. The discovery of transmembrane transporters using indirect methods has enabled the identification of high-affinity transporters but limits access to lower-affinity, promiscuous transport systems. Therefore, covalent tagging strategies that enable the direct identification of target proteins are desirable. To this end, we examined the co-crystal structure of

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsMembrane Transport ProteinsSiderophoresDeferoxamineFerric CompoundsModels, MolecularPseudomonas aeruginosaReceptors, Cell SurfaceBacterial Outer Membrane ProteinsBacterial ProteinsDeferoxamineFerric Compoundsferrioxamine BFoxA protein, bacteriaMembrane Transport ProteinsReceptors, Cell SurfaceSiderophores

Identifiers

PMID42127265
PMCPMC13220308

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.