Evidence map›Paper›PMID 24259450›Full record

ArticleAngewandte Chemie (International ed. in English)2014

Proteins with highly similar native folds can show vastly dissimilar folding behavior when desolvated.

Moritz Schennach, Kathrin Breuker

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Replacing HChemical science · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Unfolding and Folding of the Three-Helix Bundle Protein KIX in the Absence of Solvent.Journal of the American Society for Mass Spectrometry · 2016
    Article
  15. Article
  16. Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation.Journal of the American Society for Mass Spectrometry · 2015
    Article
  17. Article
  18. Review
  19. 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

2 authors.

Moritz SchennachInstitut für Organische Chemie and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Innrain 80-82, 6020 Innsbruck (Austria) http://www.bioms-breuker.at.
Kathrin Breuker

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins can be exposed to vastly different environments such as the cytosol or membranes, but the delicate balance between external factors and intrinsic determinants of protein structure, stability, and folding is only poorly understood. Here we used electron capture dissociation to study horse and tuna heart Cytochromes c in the complete absence of solvent. The significantly different stability of their highly similar native folds after transfer into the gas phase, and their strikingly different folding behavior in the gas phase, can be rationalized on the basis of electrostatic interactions such as salt bridges. In the absence of hydrophobic bonding, protein folding is far slower and more complex than in solution.

Indexed as

Amino AcidsAnimalsGasesHorsesMass SpectrometryProtein FoldingProteinsAmino AcidsGasesProteinselectron capture dissociationgas phasemass spectrometryproteinprotein folding

Identifiers

PMID24259450
PMCPMC4065370

What OpenQuestion holds

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Registered trials

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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.