Evidence map›Paper›PMID 25970849›Full record

ArticleProtein science : a publication of the Protein Society2015

Collisional unfolding of multiprotein complexes reveals cooperative stabilization upon ligand binding.

Shuai Niu, Brandon T Ruotolo

Abstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Crowding beyond excluded volume: A tale of two dimers.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
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  5. Article
  6. Article
  7. Article
  8. Structural modeling of a novel membrane-bound globin-coupled sensor inComputational and structural biotechnology journal · 2021
    Article
  9. Review
  10. A Tilted Surface and Ion Carpet Array for SID.Journal of the American Society for Mass Spectrometry · 2020
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
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  19. Article
  20. Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016
    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.

Shuai NiuDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109.
Brandon T RuotoloDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cooperative binding mechanisms are a common feature in biology, enabling a diverse range of protein-based molecular machines to regulate activities ranging from oxygen uptake to cellular membrane transport. Much, however, is not known about such cooperative binding mechanisms, including how such events typically add to the overall stability of such protein systems. Measurements of such cooperative stabilization events are challenging, as they require the separation and resolution of individual protein complex bound states within a mixture of potential stoichiometries to individually assess protein stabilities. Here, we report ion mobility-mass spectrometry results for the concanavalin A tetramer bound to a range of polysaccharide ligands. We use collision induced unfolding, a relatively new methodology that functions as a gas-phase analog of calorimetry experiments in solution, to individually assess the stabilities of concanavalin A bound states. By comparing the differences in activation voltage required to unfold different concanavalin A-ligand stoichiometries, we find evidence suggesting a cooperative stabilization of concanavalin A occurs upon binding most carbohydrate ligands. We critically evaluate this observation by assessing a broad range of ligands, evaluating the unfolding properties of multiple protein charge states, and by comparing our gas-phase results with those obtained from calorimetry experiments carried out in solution.

Indexed as

Protein UnfoldingCanavaliaCarbohydrate SequenceConcanavalin ALigandsMolecular Sequence DataPolysaccharidesProtein BindingProtein ConformationProtein MultimerizationProtein StabilityConcanavalin ALigandsPolysaccharidescarbohydrate bindingcollision induced dissociationion mobilitymass spectrometry

Identifiers

PMID25970849
PMCPMC4534178

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.