Evidence map›Paper›PMID 31233270›Full record

ArticleAngewandte Chemie (International ed. in English)2019

DNP-Supported Solid-State NMR Spectroscopy of Proteins Inside Mammalian Cells.

Siddarth Narasimhan, Stephan Scherpe, Alessandra Lucini Paioni, Johan van der Zwan, Gert E Folkers, Huib Ovaa, Marc Baldus

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. 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
–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

66 citing papers in PubMed.

  1. Article
  2. Targeted NMR signal enhancement of RNA by site-directed bis-nitroxide labeling.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  5. Pushing Sensitivity and Specificity Limits in Native Structural Biology:Journal of the American Chemical Society · 2025
    Article
  6. Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Siddarth NarasimhanNMR Spectroscopy group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands.ORCID 0000-0001-5712-2701
Stephan ScherpeOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center (LUMC), Einthovenweg 20, 2333 ZC, Leiden, The Netherlands.ORCID 0000-0003-0532-5229
Alessandra Lucini PaioniNMR Spectroscopy group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands.ORCID 0000-0001-6609-6672
Johan van der ZwanNMR Spectroscopy group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands.ORCID 0000-0002-6336-8174
Gert E FolkersNMR Spectroscopy group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands.ORCID 0000-0003-1070-0505
Huib OvaaOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center (LUMC), Einthovenweg 20, 2333 ZC, Leiden, The Netherlands.ORCID 0000-0002-0068-054X
Marc BaldusNMR Spectroscopy group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands.ORCID 0000-0001-7068-5613

Funding

Nederlandse Organisatie voor Wetenschappelijk Onderzoek 700.10.443
6 · The paper itself

Abstract

Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid-state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high-sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in-cell solution-state NMR spectroscopy due to molecular size limitations.

Indexed as

Amino Acid SequenceHeLa CellsHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsUbiquitinUbiquitinationProteinsUbiquitindynamic nuclear polarizationin-cell NMRprotein-protein interactionssolid-state NMRubiquitination

Identifiers

PMID31233270
PMCPMC6772113

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.