Evidence map›Paper›PMID 25956570›Full record

ArticleJournal of biomolecular NMR2015

Efficient cellular solid-state NMR of membrane proteins by targeted protein labeling.

Lindsay A Baker, Mark Daniëls, Elwin A W van der Cruijsen, Gert E Folkers, Marc Baldus

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2025
    Article
  3. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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
  12. Article
  13. Article
  14. CombinedStructure (London, England : 1993) · 2018
    Article
  15. Article
  16. Angewandte Chemie (International ed. in English) · 2016
    Article
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

5 authors at 1 institution in 2 countries.

Lindsay A BakerNMR Spectroscopy, Department of Chemistry, Faculty of Science, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Mark Daniëls
Elwin A W van der Cruijsen
Gert E Folkers
Marc Baldus
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solid-state NMR spectroscopy (ssNMR) has made significant progress towards the study of membrane proteins in their native cellular membranes. However, reduced spectroscopic sensitivity and high background signal levels can complicate these experiments. Here, we describe a method for ssNMR to specifically label a single protein by repressing endogenous protein expression with rifampicin. Our results demonstrate that treatment of E. coli with rifampicin during induction of recombinant membrane protein expression reduces background signals for different expression levels and improves sensitivity in cellular membrane samples. Further, the method reduces the amount of time and resources needed to produce membrane protein samples, enabling new strategies for studying challenging membrane proteins by ssNMR.

Indexed as

Bacterial ProteinsCloning, MolecularEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsNuclear Magnetic Resonance, BiomolecularPotassium ChannelsProtein ConformationProteolipidsRecombinant ProteinsRifampinSensitivity and SpecificityStreptomyces lividansBacterial ProteinsEscherichia coli ProteinsMembrane Transport ProteinsPotassium Channelsprokaryotic potassium channelProteolipidsproteoliposomesRecombinant ProteinsRifampinYIDC protein, E coli

Identifiers

PMID25956570
PMCPMC4451474
OpenAlexW604558270

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.