Evidence map›Paper›PMID 21120863›Full record

ArticleProteins2011

In-cell protein NMR and protein leakage.

Christopher O Barnes, Gary J Pielak

Abstract read
In one paragraph

Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. In-Cell Dynamics: The Next Focus of All-Atom Simulations.The journal of physical chemistry. B · 2023
    Review
  3. Review
  4. Review
  5. The intracellular environment affects protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020
    Article
  7. Article
  8. Controlling and quantifying protein concentration in Escherichia coli.Protein science : a publication of the Protein Society · 2019
    Article
  9. Review
  10. Review
  11. Review
  12. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    Review
  13. Review
  14. Article
  15. Hydrogen exchange of disordered proteins in Escherichia coli.Protein science : a publication of the Protein Society · 2015
    Article
  16. Article
  17. Understanding the mechanism of proteasome 20S core particle gating.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Amide proton exchange of a dynamic loop in cell extracts.Protein science : a publication of the Protein Society · 2013
    Article
  19. Article
  20. Soft interactions and crowding.Biophysical reviews · 2013
    Review
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

2 authors.

Christopher O BarnesDepartment of Chemistry, University of North Carolina at Chapel Hill, North Carolina 27599, USA.
Gary J Pielak

Funding

NIH Director's Pioneer AwardDP1OD000783 · OD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PIELAK, GARY JOSEPH · 2006 to 2010
$3.7M
NIH HHS DP1 OD000783NIH HHS DP1OD783
6 · The paper itself

Abstract

In-cell nuclear magnetic resonance spectroscopy is a tool for studying proteins under physiologically relevant conditions. In some instances, however, protein signals from leaked protein are observed in the liquid surrounding the cells. Here, we examine the expression of four proteins in Escherichia coli. We describe the controls that should be used for in-cell NMR experiments and show that leakage is likely when the protein being studied exceeds ∼20% of the total cellular protein.

Indexed as

alpha-SynucleinEscherichia coliEscherichia coli ProteinsHumansNuclear Magnetic Resonance, BiomolecularPeptidesPlant ProteinsProtein BiosynthesisProtein Structure, TertiaryRecombinant ProteinsUbiquitinalpha-Synucleinchymotrypsin inhibitor 2Escherichia coli ProteinshdeA protein, E coliPeptidesPlant ProteinsRecombinant ProteinsUbiquitin

Identifiers

PMID21120863
PMCPMC3016450

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.