Evidence map›Paper›PMID 24013819›Full record

ArticleNature methods2013

Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.

Shenlin Wang, Rachel A Munro, Lichi Shi, Izuru Kawamura, Takashi Okitsu, Akimori Wada, So-Young Kim, Kwang-Hwan Jung, Leonid S Brown, Vladimir Ladizhansky

Abstract read
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In one paragraph

Article in Nature methods, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
12.7field-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

101 citing papers in PubMed, 226 citations in OpenAlex.

  1. A random fractionalMagnetic resonance letters · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Challenges of Protein-Protein Docking of the Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Chemical reviews · 2022
    Review
  12. Review
  13. Article
  14. Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  15. Review
  16. Review
  17. Extensively sparseJournal of biomolecular NMR · 2021
    Article
  18. Article
  19. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    Article
  20. Review

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

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

10 authors at 3 institutions in 3 countries.

Shenlin Wang1] Department of Physics, University of Guelph, Guelph, Ontario, Canada. [2] Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.
Rachel A Munro
Lichi Shi
Izuru Kawamura
Takashi Okitsu
Akimori Wada
So-Young Kim
Kwang-Hwan Jung
Leonid S Brown
Vladimir Ladizhansky
University of Guelph · CAKobe Pharmaceutical University · JPSogang University · KR

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning solid-state NMR spectroscopy can be used to determine structures of membrane proteins reconstituted in synthetic lipids, an environment similar to the natural membrane. We combined a large number of experimentally determined interatomic distances and local torsional restraints to solve the structure of an oligomeric membrane protein of common seven-helical fold, Anabaena sensory rhodopsin (ASR). We determined the atomic resolution detail of the oligomerization interface of the ASR trimer, and the arrangement of helices, side chains and the retinal cofactor in the monomer.

Indexed as

Amino Acid SequenceAnabaenaCrystallography, X-RayLipidsMembrane ProteinsModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein MultimerizationSensory RhodopsinsLipidsMembrane ProteinsSensory Rhodopsins

Identifiers

PMID24013819
OpenAlexW2110461335

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.