Evidence map›Paper›PMID 31044174›Full record

ArticleCommunications biology2019

Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from

Denis Lacabanne, Cédric Orelle, Lauriane Lecoq, Britta Kunert, Claire Chuilon, Thomas Wiegand, Stéphanie Ravaud, Jean-Michel Jault, Beat H Meier, Anja Böckmann

Abstract read
In one paragraph

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. The Antidepressant Drug Clomipramine Inhibits the ABC Transporter BmrA.Chembiochem : a European journal of chemical biology · 2026
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  12. Myristic Acid Inhibits the Activity of the Bacterial ABC Transporter BmrA.International journal of molecular sciences · 2021
    Article
  13. Extensively sparseJournal of biomolecular NMR · 2021
    Article
  14. Review
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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.

Denis Lacabanne *1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.ORCID 0000-0002-8911-3794
Cédric Orelle *1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.
Lauriane Lecoq1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.
Britta Kunert1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.
Claire Chuilon1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.
Thomas Wiegand2Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland.
Stéphanie Ravaud1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.
Jean-Michel Jault1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.
Beat H Meier2Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland.ORCID 0000-0002-9107-4464
Anja Böckmann1Molecular Microbiology and Structural Biochemistry, UMR 5086 CNRS/Université de Lyon, Labex Ecofect, 7, passage de Vercors, 69367 Lyon, France.ORCID 0000-0001-8149-7941

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP-binding-cassette (ABC) transporters are molecular pumps that translocate molecules across the cell membrane by switching between inward-facing and outward-facing states. To obtain a detailed understanding of their mechanism remains a challenge to structural biology, as these proteins are notoriously difficult to study at the molecular level in their active, membrane-inserted form. Here we use solid-state NMR to investigate the multidrug ABC transporter BmrA reconstituted in lipids. We identify the chemical-shift differences between the inward-facing, and outward-facing state induced by ATP:Mg

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateATP-Binding Cassette TransportersBacillus subtilisBacterial ProteinsBinding SitesCell MembraneDrug Resistance, MultipleHydrolysisMagnesiumMagnetic Resonance SpectroscopyProtein ConformationAdenosine TriphosphatasesAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsMagnesiumBacteriaSolid-state NMR

Identifiers

PMID31044174
PMCPMC6488656

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.