Evidence map›Paper›PMID 35665580›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Native Ambient Mass Spectrometry of an Intact Membrane Protein Assembly and Soluble Protein Assemblies Directly from Lens Tissue.

Oliver J Hale, Helen J Cooper

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 7% of its field
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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Pooled it
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  5. Endogenous Aquaporin-0 Lipid Binding in Ocular Lens Tissue via Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025
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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 at 1 institution in 1 country.

Oliver J HaleSchool of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK.
Helen J CooperSchool of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK.ORCID 0000-0003-4590-9384
University of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S019456/1
6 · The paper itself

Abstract

Membrane proteins constitute around two-thirds of therapeutic targets but present a significant challenge for structural analysis due to their low abundance and solubility. Existing methods for structural analysis rely on over-expression and/or purification of the membrane protein, thus removing any links back to actual physiological environment. Here, we demonstrate mass spectrometry analysis of an intact oligomeric membrane protein directly from tissue. Aquaporin-0 exists as a 113 kDa tetramer, with each subunit featuring six transmembrane helices. We report the characterisation of the intact assembly directly from a section of sheep eye lens without sample pre-treatment. Protein identity was confirmed by mass measurement of the tetramer and subunits, together with top-down mass spectrometry, and the spatial distribution was determined by mass spectrometry imaging. Our approach allows simultaneous analysis of soluble protein assemblies in the tissue.

Indexed as

Lens, CrystallineMembrane ProteinsAnimalsMass SpectrometrySheepMembrane ProteinsAmbient Mass SpectrometryAquaporinMass Spectrometry ImagingMembrane ProteinNative Mass Spectrometry

Identifiers

PMID35665580
PMCPMC9401010
OpenAlexW4281684177

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.