Evidence map›Paper›PMID 28884954›Full record

ArticleAngewandte Chemie (International ed. in English)2017

Native Desorption Electrospray Ionization Liberates Soluble and Membrane Protein Complexes from Surfaces.

Stephen Ambrose, Nicholas G Housden, Kallol Gupta, Jieyuan Fan, Paul White, Hsin-Yung Yen, Julien Marcoux, Colin Kleanthous, Jonathan T S Hopper, Carol V Robinson

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 58 citations in OpenAlex.

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  5. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
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  19. Cryo-LESA Mass Spectrometry-a Step Towards Truly Native Surface Sampling of Proteins.Journal of the American Society for Mass Spectrometry · 2019
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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

10 authors at 2 institutions in 2 countries.

Stephen AmbroseDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Nicholas G HousdenDepartment of Biochemistry, University of Oxford, Oxford, UK.
Kallol GuptaDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Jieyuan FanDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Paul WhiteDepartment of Biochemistry, University of Oxford, Oxford, UK.
Hsin-Yung YenDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Julien MarcouxDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford, UK.
Jonathan T S HopperDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Carol V RobinsonDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
University of Oxford · GBInstitut de Pharmacologie et de Biologie Structurale · FR

Funding

European Research Council 641317Medical Research Council G1000819Medical Research Council MC_PC_15029Medical Research Council MR/N020413/1Wellcome TrustWellcome Trust 104633/Z/14/ZWellcome Trust 201505/Z/16/Z
6 · The paper itself

Abstract

Mass spectrometry (MS) applications for intact protein complexes typically require electrospray (ES) ionization and have not been achieved via direct desorption from surfaces. Desorption ES ionization (DESI) MS has however transformed the study of tissue surfaces through release and characterisation of small molecules. Motivated by the desire to screen for ligand binding to intact protein complexes we report the development of a native DESI platform. By establishing conditions that preserve non-covalent interactions we exploit the surface to capture a rapid turnover enzyme-substrate complex and to optimise detergents for membrane protein study. We demonstrate binding of lipids and drugs to membrane proteins deposited on surfaces and selectivity from a mix of related agonists for specific binding to a GPCR. Overall therefore we introduce this native DESI platform with the potential for high-throughput ligand screening of some of the most challenging drug targets including GPCRs.

Indexed as

LigandsLipid MetabolismMembrane ProteinsMolecular WeightPharmaceutical PreparationsProtein BindingSolubilitySpectrometry, Mass, Electrospray IonizationSurface PropertiesLigandsMembrane ProteinsPharmaceutical Preparationsdesorptionelectrospray ionisationG-protein coupled receptorsmass spectrometrymembrane protein complexes

Identifiers

PMID28884954
PMCPMC5813186
OpenAlexW2752884742

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.