Evidence map›Paper›PMID 29249608›Full record

ArticleStructure (London, England : 1993)2018

Combined

Lindsay A Baker, Tessa Sinnige, Pascale Schellenberger, Jeanine de Keyzer, C Alistair Siebert, Arnold J M Driessen, Marc Baldus, Kay Grünewald

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
  2. Review
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Probing Cell-Surface Interactions in Fungal Cell Walls by High-ResolutionChemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  11. Chemical reviews · 2022
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Lindsay A BakerNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, the Netherlands; Oxford Particle Imaging Centre, Division of Structural Biology, University of Oxford, The Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address: lindsay@strubi.ox.ac.uk.
Tessa SinnigeNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, the Netherlands.
Pascale SchellenbergerOxford Particle Imaging Centre, Division of Structural Biology, University of Oxford, The Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, UK.
Jeanine de KeyzerDepartment of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, the Netherlands; The Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 11, 9747 AG Groningen, the Netherlands.
C Alistair SiebertOxford Particle Imaging Centre, Division of Structural Biology, University of Oxford, The Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, UK.
Arnold J M DriessenDepartment of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, the Netherlands; The Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 11, 9747 AG Groningen, the Netherlands.
Marc BaldusNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, the Netherlands. Electronic address: m.baldus@uu.nl.
Kay GrünewaldOxford Particle Imaging Centre, Division of Structural Biology, University of Oxford, The Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address: kay@strubi.ox.ac.uk.

Funding

Wellcome Trust
6 · The paper itself

Abstract

Membrane proteins remain challenging targets for structural biology, despite much effort, as their native environment is heterogeneous and complex. Most methods rely on detergents to extract membrane proteins from their native environment, but this removal can significantly alter the structure and function of these proteins. Here, we overcome these challenges with a hybrid method to study membrane proteins in their native membranes, combining high-resolution solid-state nuclear magnetic resonance spectroscopy and electron cryotomography using the same sample. Our method allows the structure and function of membrane proteins to be studied in their native environments, across different spatial and temporal resolutions, and the combination is more powerful than each technique individually. We use the method to demonstrate that the bacterial membrane protein YidC adopts a different conformation in native membranes and that substrate binding to YidC in these native membranes differs from purified and reconstituted systems.

Indexed as

Cell MembraneCryoelectron MicroscopyDetergentsElectron Microscope TomographyEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProteolipidsDetergentsEscherichia coli ProteinsMembrane Transport ProteinsProteolipidsproteoliposomesYIDC protein, E colielectron cryotomographyhybrid methodsMASmembrane proteinsnative membranessolid-state NMRYidC

Identifiers

PMID29249608
PMCPMC5758107

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.