Evidence map›Paper›PMID 26901650›Full record

ArticleNature methods2016

High-resolution mass spectrometry of small molecules bound to membrane proteins.

Joseph Gault, Joseph A C Donlan, Idlir Liko, Jonathan T S Hopper, Kallol Gupta, Nicholas G Housden, Weston B Struwe, Michael T Marty, Todd Mize, Cherine Bechara and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature methods, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
23.2field-weighted citation impact, top 1% 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

142 citing papers in PubMed, 244 citations in OpenAlex.

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82 more citing papers are in PubMed but not listed here.

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

17 authors at 3 institutions in 3 countries.

Joseph GaultDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7686-2983
Joseph A C DonlanDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Idlir LikoDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Jonathan T S HopperDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Kallol GuptaDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Nicholas G HousdenDepartment of Biochemistry, University of Oxford, Oxford, UK.
Weston B StruweDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Michael T MartyDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Todd MizeDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Cherine BecharaDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Ya ZhuCAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Pudong, China.
Beili WuCAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Pudong, China.
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford, UK.
Mikhail BelovThermo Fisher Scientific, Bremen, Germany.
Eugen DamocThermo Fisher Scientific, Bremen, Germany.
Alexander MakarovThermo Fisher Scientific, Bremen, Germany.
Carol V RobinsonDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
University of Oxford · GBThermo Fisher Scientific (Germany) · DEChinese Academy of Sciences · CN

Funding

Biotechnology and Biological Sciences Research Council BB/L021234/1European Research Council 268851Medical Research Council G1000819Wellcome TrustWellcome Trust 104633/Z/14/Z
6 · The paper itself

Abstract

Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry-based method for analyzing intact membrane protein-ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length.

Indexed as

HumansLipidsMass SpectrometryMembrane ProteinsModels, MolecularPeptide FragmentsProtein BindingSmall Molecule LibrariesLipidsMembrane ProteinsPeptide FragmentsSmall Molecule Libraries

Identifiers

PMID26901650
PMCPMC4856209
OpenAlexW2276080164

What OpenQuestion holds

Textmetadata
LicenceTDM
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.