Evidence map›Paper›PMID 24218610›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Impact of reconstituted cytosol on protein stability.

Mohona Sarkar, Austin E Smith, Gary J Pielak

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 189 citations in OpenAlex.

  1. Review
  2. Residue-level mapping of crowding effects on protein phase separation.Protein science : a publication of the Protein Society · 2026
    Article
  3. Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025
    Article
  4. Role of Aqueous Media in Macromolecular Crowding.Sub-cellular biochemistry · 2025
    Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
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  14. Article
  15. Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Virus Mechanics under Molecular Crowding.The journal of physical chemistry. B · 2021
    Article
  20. Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020
    Article

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

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

3 authors at 1 institution in 2 countries.

Mohona SarkarDepartments of Chemistry and Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599.
Austin E Smith
Gary J Pielak
UNC Lineberger Comprehensive Cancer Center

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein stability is usually studied in simple buffered solutions, but most proteins function inside cells, where the heterogeneous and crowded environment presents a complex, nonideal system. Proteins are expected to behave differently under cellular crowding owing to two types of contacts: hard-core repulsions and weak, chemical interactions. The effect of hard-core repulsions is purely entropic, resulting in volume exclusion owing to the mere presence of the crowders. The weak interactions can be repulsive or attractive, thus enhancing or diminishing the excluded volume, respectively. We used a reductionist approach to assess the effects of intracellular crowding. Escherichia coli cytoplasm was dialyzed, lyophilized, and resuspended at two concentrations. NMR-detected amide proton exchange was then used to quantify the stability of the globular protein chymotrypsin inhibitor 2 (CI2) in these crowded solutions. The cytosol destabilizes CI2, and the destabilization increases with increasing cytosol concentration. This observation shows that the cytoplasm interacts favorably, but nonspecifically, with CI2, and these interactions overcome the stabilizing hard-core repulsions. The effects of the cytosol are even stronger than those of homogeneous protein crowders, reinforcing the biological significance of weak, nonspecific interactions.

Indexed as

Models, BiologicalChromatography, High Pressure LiquidCytoplasmEscherichia coliMacromolecular SubstancesMass SpectrometryNuclear Magnetic Resonance, BiomolecularPeptidesPlant ProteinsProtein Interaction MapsProtein Stabilitychymotrypsin inhibitor 2Macromolecular SubstancesPeptidesPlant Proteins

Identifiers

PMID24218610
PMCPMC3845188
OpenAlexW2020426274

What OpenQuestion holds

Textmetadata
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.