Evidence map›Paper›PMID 41544198›Full record

ArticleJournal of the American Chemical Society2026

Integrated Native Mass Spectrometry Imaging of Soluble and Membrane Proteins.

Oliver J Hale, Helen J Cooper

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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Oliver J HaleSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.ORCID 0000-0002-2286-5780
Helen J CooperSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.ORCID 0000-0003-4590-9384

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Native ambient mass spectrometry enables the analysis of intact protein complexes directly from fresh frozen tissue sections together with visualization of their spatial distribution as part of a mass spectrometry imaging workflow. Native mass spectrometry imaging typically employs nanospray-desorption electrospray ionization (nano-DESI), a liquid junction sampling approach. Imaging of both soluble and membrane proteins has been demonstrated by native nano-DESI but, crucially, imaging of one protein type has always been at the expense of the other, requiring tailored sample preparation and multiple tissue sections. Here, we introduce a new mode of nano-DESI operation that combines soluble and membrane protein analysis into a single experiment, requiring no sample preparation and only a single tissue section, and which is compatible with mass spectrometry imaging. Chromatography-like separation of soluble and membrane protein signals, observed as varying elution profiles, occurs when the nano-DESI probe is parked in a fixed location on the tissue. The elution profiles of proteins in both kidney and brain tissue were explored. The results show that elution profiles are quick to record, offer insight into the classification of unknown proteins detected from tissue and enable signal-to-noise improvements to imaging and native top-down mass spectrometry workflows.

Indexed as

Membrane ProteinsSpectrometry, Mass, Electrospray IonizationAnimalsKidneyMass SpectrometrySolubilityMembrane Proteins

Identifiers

PMID41544198
PMCPMC12856882

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.