Evidence map›Paper›PMID 30320551›Full record

ArticleeLife2018

Screening of candidate substrates and coupling ions of transporters by thermostability shift assays.

Homa Majd, Martin S King, Shane M Palmer, Anthony C Smith, Liam Dh Elbourne, Ian T Paulsen, David Sharples, Peter Jf Henderson, Edmund Rs Kunji

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.5field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 68 citations in OpenAlex.

  1. Structures of the sodium-coupled phosphate importer SLC34A2 reveal a distinct architecture and gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

9 authors at 3 institutions in 2 countries.

Homa Majd *Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-2048-1839
Martin S King *Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0001-6030-5154
Shane M PalmerMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, United Kingdom.
Anthony C SmithMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, United Kingdom.
Liam Dh ElbourneDepartment of Molecular Sciences, Macquarie University, Sydney, Australia.
Ian T PaulsenDepartment of Molecular Sciences, Macquarie University, Sydney, Australia.
David SharplesAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Peter Jf HendersonAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0002-9187-0938
Edmund Rs KunjiMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-0610-4500
University of Cambridge · GBMacquarie University · AUUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council MPSI BBS/B/14418Leverhulme Trust EM-2014 -045Medical Research Council MC_U105663139Medical Research Council MC_UU_00015/1Medical Research Council MC_UU_00015/7Wellcome JIF 062164/Z/00/ZWellcome TrustWellcome Trust JIF 062164/Z/00/Z
6 · The paper itself

Abstract

Substrates of most transport proteins have not been identified, limiting our understanding of their role in physiology and disease. Traditional identification methods use transport assays with radioactive compounds, but they are technically challenging and many compounds are unavailable in radioactive form or are prohibitively expensive, precluding large-scale trials. Here, we present a high-throughput screening method that can identify candidate substrates from libraries of unlabeled compounds. The assay is based on the principle that transport proteins recognize substrates through specific interactions, which lead to enhanced stabilization of the transporter population in thermostability shift assays. Representatives of three different transporter (super)families were tested, which differ in structure as well as transport and ion coupling mechanisms. In each case, the substrates were identified correctly from a large set of chemically related compounds, including stereo-isoforms. In some cases, stabilization by substrate binding was enhanced further by ions, providing testable hypotheses on energy coupling mechanisms.

Indexed as

Biological AssayTemperatureAdenosine DiphosphateAdenosine TriphosphateAnimalsHumansIonsLigandsMembrane Transport ProteinsMitochondriaProtein StabilityReproducibility of ResultsSubstrate SpecificityTetrahymenaAdenosine DiphosphateAdenosine TriphosphateIonsLigandsMembrane Transport ProteinsE. colihumanion couplingMicrobacterium liquefaciensmolecular biophysicsS. cerevisiaestructural biologysubstrate specificityTetrahymena thermophilathermostabilityThermothelomyces thermophila

Identifiers

PMID30320551
PMCPMC6211832
OpenAlexW2952756245

What OpenQuestion holds

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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.