Evidence map›Paper›PMID 25492389›Full record

ArticleProtein science : a publication of the Protein Society2015

Specific ion effects on macromolecular interactions in Escherichia coli extracts.

Ciara Kyne, Brian Ruhle, Virginie W Gautier, Peter B Crowley

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. RNA Structure: Past, Future, and Gene Therapy Applications.International journal of molecular sciences · 2024
    Review
  3. Article
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  5. Article
  6. Article
  7. Review
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  9. Article
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  11. Review
  12. Quinary interactions with an unfolded state ensemble.Protein science : a publication of the Protein Society · 2017
    Article
  13. Article
  14. A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.Protein science : a publication of the Protein Society · 2017
    Review
  15. Review
  16. Protein charge determination and implications for interactions in cell extracts.Protein science : a publication of the Protein Society · 2017
    Article
  17. Article
  18. A Unique Tool for Cellular Structural Biology: In-cell NMR.The Journal of biological chemistry · 2016
    Review
  19. Intracellular pH modulates quinary structure.Protein science : a publication of the Protein Society · 2015
    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 2 institutions in 1 country.

Ciara KyneSchool of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland.
Brian Ruhle
Virginie W Gautier
Peter B Crowley
Ollscoil na Gaillimhe – University of Galway · IEUniversity College Dublin · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein characterization in situ remains a major challenge for protein science. Here, the interactions of ΔTat-GB1 in Escherichia coli cell extracts were investigated by NMR spectroscopy and size exclusion chromatography (SEC). ΔTat-GB1 was found to participate in high molecular weight complexes that remain intact at physiologically-relevant ionic strength. This observation helps to explain why ΔTat-GB1 was not detected by in-cell NMR spectroscopy. Extracts pre-treated with RNase A had a different SEC elution profile indicating that ΔTat-GB1 predominantly interacted with RNA. The roles of biological and laboratory ions in mediating macromolecular interactions were studied. Interestingly, the interactions of ΔTat-GB1 could be disrupted by biologically-relevant multivalent ions. The most effective shielding of interactions occurred in Mg(2+) -containing buffers. Moreover, a combination of RNA digestion and Mg(2+) greatly enhanced the NMR detection of ΔTat-GB1 in cell extracts.

Indexed as

ArginineBacterial ProteinsCell ExtractsChromatography, GelEscherichia coliMagnesiumNuclear Localization SignalsNuclear Magnetic Resonance, BiomolecularOsmolar ConcentrationRecombinant Fusion Proteinstat Gene Products, Human Immunodeficiency VirusArginineBacterial ProteinsCell ExtractsMagnesiumNuclear Localization SignalsRecombinant Fusion Proteinstat Gene Products, Human Immunodeficiency Virusargininecell extractsin-cell NMRprotein interactionssize exclusion chromatography

Identifiers

PMID25492389
PMCPMC4353357
OpenAlexW2142417893

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.