Evidence map›Paper›PMID 36223470›Full record

ArticleScience advances2022

The ABC transporter MsbA adopts the wide inward-open conformation in

Laura Galazzo, Gianmarco Meier, Dovile Januliene, Kristian Parey, Dario De Vecchis, Bianca Striednig, Hubert Hilbi, Lars V Schäfer, Ilya Kuprov, Arne Moeller and 2 more

Abstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
  2. Review
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  4. A dual sensor regulates P-glycoprotein's structural plasticity.bioRxiv : the preprint server for biology · 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

12 authors.

Laura GalazzoFaculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0001-8440-1757
Gianmarco MeierInstitute of Medical Microbiology, University of Zurich, 8006 Zurich, Switzerland.ORCID 0000-0002-4455-430X
Dovile JanulieneDepartment of Structural Biology, Osnabrück University, 49076 Osnabrück, Germany.ORCID 0000-0002-3279-7590
Kristian PareyDepartment of Structural Biology, Osnabrück University, 49076 Osnabrück, Germany.ORCID 0000-0002-4842-6479
Dario De VecchisCenter for Theoretical Chemistry, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0002-7732-5095
Bianca StriednigInstitute of Medical Microbiology, University of Zurich, 8006 Zurich, Switzerland.ORCID 0000-0001-7575-8965
Hubert HilbiInstitute of Medical Microbiology, University of Zurich, 8006 Zurich, Switzerland.ORCID 0000-0002-5462-9301
Lars V SchäferCenter for Theoretical Chemistry, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0002-8498-3061
Ilya KuprovSchool of Chemistry, University of Southampton, Southampton SO17 1BJ, UK.ORCID 0000-0003-0430-2682
Arne MoellerDepartment of Structural Biology, Osnabrück University, 49076 Osnabrück, Germany.
Enrica BordignonFaculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0003-2450-5161
Markus A SeegerInstitute of Medical Microbiology, University of Zurich, 8006 Zurich, Switzerland.ORCID 0000-0003-1761-8571

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to truly understand the biophysical properties of membrane proteins in a physiological environment, they must be investigated within living cells. Here, we used a spin-labeled nanobody to interrogate the conformational cycle of the ABC transporter MsbA by double electron-electron resonance. Unexpectedly, the wide inward-open conformation of MsbA, commonly considered a nonphysiological state, was found to be prominently populated in

Indexed as

ATP-Binding Cassette TransportersEscherichia coliEscherichia coli ProteinsAdenosine TriphosphateBacterial ProteinsDetergentsLipid ALiposomesMembrane ProteinsProtein ConformationAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsDetergentsEscherichia coli ProteinsLipid ALiposomesMembrane ProteinsMsbA protein, Bacteria

Identifiers

PMID36223470
PMCPMC9555771

What OpenQuestion holds

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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.