Evidence map›Paper›PMID 29917302›Full record

ArticleChemphyschem : a European journal of chemical physics and physical chemistry2018

Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy.

Maximilian Zinke, Pascal Fricke, Sascha Lange, Sophie Zinn-Justin, Adam Lange

Abstract read
In one paragraph

Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021
    Article
  6. Article
  7. 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
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.

Maximilian ZinkeDepartment of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Pascal FrickeDepartment of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Sascha LangeDepartment of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.ORCID 0000-0002-7534-5973
Sophie Zinn-JustinInstitute for Integrative Biology of the Cell (I2BC) CEA, CNRS, Université Paris-Sud Université Paris-Saclay, Gif-sur-Yvette Cedex, France.
Adam LangeDepartment of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.

Funding

European Research Council 337490Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP)
6 · The paper itself

Abstract

Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has been proposed to detect intermolecular interfaces in these assemblies by proton detection. Herein, we introduce a concept based on methyl labeling that allows for the assignment of these moieties and for the study of protein-protein interfaces at atomic resolution.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid SequenceGlycoproteinsIsoleucineProteinsProtein Structure, TertiaryProtonsGlycoproteinsIsoleucineProteinsProtonsinterfacesmethyl labelingproteinsprotein structuressolid-state NMR

Identifiers

PMID29917302
PMCPMC6220863

What OpenQuestion holds

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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.