Evidence map›Paper›PMID 33580357›Full record

ArticleJournal of biomolecular NMR2021

Protein in-cell NMR spectroscopy at 1.2 GHz.

Enrico Luchinat, Letizia Barbieri, Matteo Cremonini, Lucia Banci

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
7.0field-weighted citation impact, top 2% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Nuclear-Spin Hyperpolarization of Biomolecules by Optically Enhanced NMR at Ultra-High Field.Journal of the Chinese Chemical Society. Zhongguo hua xue hui (Taipei, Taiwan) · 2026
    Article
  4. Review
  5. Live Metabolomics with NMR.Analytical chemistry · 2026
    Review
  6. Article
  7. Article
  8. OptimizedInternational journal of molecular sciences · 2025
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. OptimalNature protocols · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Multinuclear 1D and 2D NMR withNature communications · 2023
    Article
  18. Review
  19. Direct Expression of Fluorinated Proteins in Human Cells forJournal of the American Chemical Society · 2023
    Article
  20. 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

4 authors at 3 institutions in 1 country.

Enrico LuchinatUniversità degli Studi di Firenze, Via Luigi sacconi 6, 50019, Sesto Fiorentino, Italy. eluchinat@cerm.unifi.it.ORCID http://orcid.org/0000-0003-4183-4311
Letizia BarbieriUniversità degli Studi di Firenze, Via Luigi sacconi 6, 50019, Sesto Fiorentino, Italy.
Matteo CremoniniUniversità degli Studi di Firenze, Via Luigi sacconi 6, 50019, Sesto Fiorentino, Italy.
Lucia BanciUniversità degli Studi di Firenze, Via Luigi sacconi 6, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it.
University of Florence · ITConsorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase · ITInteruniversity Consortium for Magnetic Resonance · IT

Funding

Horizon 2020 Framework Programme 731005Horizon 2020 Framework Programme 871037Ministero dell'Istruzione, dell'Università e della Ricerca 20177XJCHX
6 · The paper itself

Abstract

In-cell NMR spectroscopy provides precious structural and functional information on biological macromolecules in their native cellular environment at atomic resolution. However, the intrinsic low sensitivity of NMR imposes a big limitation in the applicability of the methodology. In this respect, the recently developed commercial 1.2 GHz NMR spectrometer is expected to introduce significant benefits. However, cell samples may suffer from detrimental effects at ultrahigh fields, that must be carefully evaluated. Here we show the first in-cell NMR spectra recorded at 1.2 GHz on human cells, and we compare resolution and sensitivity against those obtained at 900 and 950 MHz. To evaluate the effects of different spin relaxation rates, SOFAST-HMQC and BEST-TROSY spectra were recorded on intracellular α-synuclein and carbonic anhydrase. Major improvements are observed at 1.2 GHz when analyzing unfolded proteins, such as α-synuclein, while the TROSY scheme improves the resolution for both globular and unfolded proteins.

Indexed as

Nuclear Magnetic Resonance, Biomolecularalpha-SynucleinCarbonic Anhydrase IIHEK293 CellsHumansProteinsProton Magnetic Resonance Spectroscopyalpha-SynucleinCarbonic Anhydrase IIProteinsCellular structural biologyIn-cell NMRTROSYUltrahigh field NMRα-Synuclein

Identifiers

PMID33580357
PMCPMC8018933
OpenAlexW3126211499

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.