Evidence map›Paper›PMID 36460747›Full record

ArticleCommunications biology2022

Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression.

Juan A Gerez, Natalia C Prymaczok, Harindranath Kadavath, Dhiman Ghosh, Matthias Bütikofer, Yanick Fleischmann, Peter Güntert, Roland Riek

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. 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
1.6field-weighted citation impact, top 16% 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, 21 citations in OpenAlex.

  1. Review
  2. Revealing 3-hydroxybenzoate-4-hydroxylase from Pseudarthrobacter phenanthrenivorans Sphe3 via In-Cell NMR analysis and molecular cloning.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
    Article
  3. Live Metabolomics with NMR.Analytical chemistry · 2026
    Review
  4. Review
  5. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Protein dynamics: The future is bright and complicated!Structural dynamics (Melville, N.Y.) · 2023
    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

8 authors at 2 institutions in 3 countries.

Juan A GerezLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland. juan.gerez@phys.chem.ethz.ch.ORCID 0000-0002-3326-2897
Natalia C PrymaczokLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.
Harindranath KadavathLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.
Dhiman GhoshLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.
Matthias BütikoferLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.
Yanick FleischmannLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.ORCID 0000-0002-5629-295X
Peter GüntertLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland.ORCID 0000-0002-2911-7574
Roland RiekLaboratory of Physical Chemistry, ETH Zürich, 8093, Zürich, Switzerland. roland.riek@phys.chem.ethz.ch.ORCID 0000-0002-6333-066X
ETH Zurich · CHGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most experimental methods for structural biology proceed in vitro and therefore the contribution of the intracellular environment on protein structure and dynamics is absent. Studying proteins at atomic resolution in living mammalian cells has been elusive due to the lack of methodologies. In-cell nuclear magnetic resonance spectroscopy (in-cell NMR) is an emerging technique with the power to do so. Here, we improved current methods of in-cell NMR by the development of a reporter system that allows monitoring the delivery of exogenous proteins into mammalian cells, a process that we called here "transexpression". The reporter system was used to develop an efficient protocol for in-cell NMR which enables spectral acquisition with higher quality for both disordered and folded proteins. With this method, the 3D atomic resolution structure of the model protein GB1 in human cells was determined with a backbone root-mean-square deviation (RMSD) of 1.1 Å.

Indexed as

Magnetic Resonance ImagingAnimalsHumansMagnetic Resonance SpectroscopyMammals

Identifiers

PMID36460747
PMCPMC9718737
OpenAlexW4311116803

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.