Evidence map›Paper›PMID 22331896›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Cellular solid-state nuclear magnetic resonance spectroscopy.

Marie Renault, Ria Tommassen-van Boxtel, Martine P Bos, Jan Andries Post, Jan Tommassen, Marc Baldus

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

90 citing papers in PubMed, 207 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. bioRxiv : the preprint server for biology · 2025
    Article
  7. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  8. Article
  9. In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  12. Article
  13. Article
  14. New Vision of Cell Walls inJournal of fungi (Basel, Switzerland) · 2024
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Solid-state NMR molecular snapshots ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

30 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Marie RenaultBijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Ria Tommassen-van Boxtel
Martine P Bos
Jan Andries Post
Jan Tommassen
Marc Baldus
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Decrypting the structure, function, and molecular interactions of complex molecular machines in their cellular context and at atomic resolution is of prime importance for understanding fundamental physiological processes. Nuclear magnetic resonance is a well-established imaging method that can visualize cellular entities at the micrometer scale and can be used to obtain 3D atomic structures under in vitro conditions. Here, we introduce a solid-state NMR approach that provides atomic level insights into cell-associated molecular components. By combining dedicated protein production and labeling schemes with tailored solid-state NMR pulse methods, we obtained structural information of a recombinant integral membrane protein and the major endogenous molecular components in a bacterial environment. Our approach permits studying entire cellular compartments as well as cell-associated proteins at the same time and at atomic resolution.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsLipopolysaccharidesLipoproteinsMagnetic Resonance SpectroscopyMolecular Sequence DataPeptidoglycanProtein ConformationProteolipidsBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipopolysaccharidesLipoproteinsLpp protein, E coliPeptidoglycanProteolipidsproteoliposomes

Identifiers

PMID22331896
PMCPMC3323964
OpenAlexW2020016481

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.