Evidence map›Paper›PMID 27385633›Full record

ArticleChemical communications (Cambridge, England)2016

Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.

Vilius Kurauskas, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F Gauto, Jérôme Boisbouvier, Paul Schanda

Open access · greenAbstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Chemical reviews · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    Article
  7. Article
  8. Article
  9. Single-Molecule Fluorescence Applied to Translation.Cold Spring Harbor perspectives in biology · 2019
    Review
  10. Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2018
    Article
  11. Review
  12. Article
  13. Article
  14. 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

7 authors at 2 institutions in 2 countries.

Vilius KurauskasUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
Elodie CrubletUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
Pavel MacekUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
Rime KerfahNMR-Bio. 5 place Robert Schumann, F-38025 Grenoble, France.
Diego F GautoUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
Jérôme BoisbouvierUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
Paul SchandaUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
Centre National de la Recherche Scientifique · FRRobert Schumann University of Music and Media · DE

Funding

European Research Council 260887European Research Council 311318
6 · The paper itself

Abstract

Solid-state NMR spectroscopy allows the characterization of the structure, interactions and dynamics of insoluble and/or very large proteins. Sensitivity and resolution are often major challenges for obtaining atomic-resolution information, in particular for very large protein complexes. Here we show that the use of deuterated, specifically CH3-labelled proteins result in significant sensitivity gains compared to previously employed CHD2 labelling, while line widths increase only marginally. We apply this labelling strategy to a 468 kDa-large dodecameric aminopeptidase, TET2, and the 1.6 MDa-large 50S ribosome subunit of Thermus thermophilus.

Identifiers

PMID27385633
PMCPMC4958370
OpenAlexW2460800736

What OpenQuestion holds

Textmetadata
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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.