Evidence map›Paper›PMID 23142870›Full record

ArticleNature methods2012

Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals.

Shakeel Ahmad Shahid, Benjamin Bardiaux, W Trent Franks, Ludwig Krabben, Michael Habeck, Barth-Jan van Rossum, Dirk Linke

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In one paragraph

Article in Nature methods, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
9.3field-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

66 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Challenges of Protein-Protein Docking of the Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Precursor Reagent Hydrophobicity Affects Membrane Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Identification of the adhesive domain of AtaA fromFrontiers in bioengineering and biotechnology · 2022
    Article
  14. Comparative analysis ofJournal of biomolecular NMR · 2021
    Article
  15. Transferred-Rotational-Echo Double Resonance.The journal of physical chemistry. A · 2021
    Article
  16. Article
  17. Article
  18. BamA is required for autotransporter secretion.Biochimica et biophysica acta. General subjects · 2020
    Article
  19. Review
  20. Article

6 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

7 authors at 3 institutions in 1 country.

Shakeel Ahmad ShahidLeibniz-Institut für Molekulare Pharmakologie, Abteilung Strukturbiologie, Berlin, Germany.
Benjamin Bardiaux
W Trent Franks
Ludwig Krabben
Michael Habeck
Barth-Jan van Rossum
Dirk Linke
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DEMax Planck Institute for Developmental Biology · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins are largely underrepresented among available atomic-resolution structures. The use of detergents in protein purification procedures hinders the formation of well-ordered crystals for X-ray crystallography and leads to slower molecular tumbling, impeding the application of solution-state NMR. Solid-state magic-angle spinning NMR spectroscopy is an emerging method for membrane-protein structural biology that can overcome these technical problems. Here we present the solid-state NMR structure of the transmembrane domain of the Yersinia enterocolitica adhesin A (YadA). The sample was derived from crystallization trials that yielded only poorly diffracting microcrystals. We solved the structure using a single, uniformly (13)C- and (15)N-labeled sample. In addition, solid-state NMR allowed us to acquire information on the flexibility and mobility of parts of the structure, which, in combination with evolutionary conservation information, presents new insights into the autotransport mechanism of YadA.

Indexed as

Adhesins, BacterialCrystallizationMembrane ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularAdhesins, BacterialMembrane ProteinsYadA protein, Yersinia

Identifiers

PMID23142870
OpenAlexW1980873042

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.