Evidence map›Paper›PMID 26725230›Full record

ArticleThe Journal of biological chemistry2016

The Lipid Bilayer Modulates the Structure and Function of an ATP-binding Cassette Exporter.

Maria E Zoghbi, Rebecca S Cooper, Guillermo A Altenberg

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mobile barrier mechanisms for NabioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Article
  9. Glyco-Steroidal Amphiphiles (GSAs) for Membrane Protein Structural Study.Chembiochem : a European journal of chemical biology · 2022
    Article
  10. Article
  11. Detergent-Free Membrane Protein Purification Using SMA Polymer.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Biological insights from SMA-extracted proteins.Biochemical Society transactions · 2021
    Review
  16. Article
  17. Article
  18. Review
  19. Production of a human mitochondrial ABC transporter in E. coli.Protein expression and purification · 2021
    Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Maria E ZoghbiFrom the Department of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, Texas 79430-6551.
Rebecca S CooperFrom the Department of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, Texas 79430-6551.
Guillermo A AltenbergFrom the Department of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, Texas 79430-6551 g.altenberg@ttuhsc.edu.
Texas Tech University · USTexas Tech University Health Sciences Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP-binding cassette exporters use the energy of ATP hydrolysis to transport substrates across membranes by switching between inward- and outward-facing conformations. Essentially all structural studies of these proteins have been performed with the proteins in detergent micelles, locked in specific conformations and/or at low temperature. Here, we used luminescence resonance energy transfer spectroscopy to study the prototypical ATP-binding cassette exporter MsbA reconstituted in nanodiscs at 37 °C while it performs ATP hydrolysis. We found major differences when comparing MsbA in these native-like conditions with double electron-electron resonance data and the crystal structure of MsbA in the open inward-facing conformation. The most striking differences include a significantly smaller separation between the nucleotide-binding domains and a larger fraction of molecules with associated nucleotide-binding domains in the nucleotide-free apo state. These studies stress the importance of studying membrane proteins in an environment that approaches physiological conditions.

Indexed as

Models, BiologicalAdenosine TriphosphateAmino Acid SubstitutionATP-Binding Cassette TransportersBacterial ProteinsBinding SitesBioluminescence Resonance Energy Transfer TechniquesEnzyme StabilityHydrolysisKineticsLipid BilayersMembrane MicrodomainsMembrane ProteinsMutationNanostructuresProtein ConformationAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsLipid BilayersMembrane ProteinsMsbA protein, BacteriaRecombinant Fusion ProteinsABC transporterfluorescence resonance energy transfer (FRET)FRETLRETluminescence resonance energy transfermembrane bilayerMsbAmultidrug transporternanodiscspectroscopy

Identifiers

PMID26725230
PMCPMC4813473
OpenAlexW2204708969

What OpenQuestion holds

Textmetadata
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.