Evidence map›Paper›PMID 26005781›Full record

ReviewCurrent opinion in structural biology2015

Probing allosteric mechanisms using native mass spectrometry.

Michal Sharon, Amnon Horovitz

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Merging different allosteric mechanisms: The case ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. On the Rational Design of Cooperative Receptors.Annual review of biophysics · 2023
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Double Mutant Cycles as a Tool to Address Folding, Binding, and Allostery.International journal of molecular sciences · 2021
    Review
  11. Mechanisms of ligand binding.Biophysics reviews · 2020
    Review
  12. Article
  13. Unpicking allosteric mechanisms of homo-oligomeric proteins by determining their successive ligand binding constants.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. Article
  15. Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. 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.

Michal SharonDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Amnon HorovitzDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address: Amnon.Horovitz@weizmann.ac.il.

Funding

European Research Council 636752
6 · The paper itself

Abstract

Native mass spectrometry (MS) and ion mobility MS provide a way to discriminate between various allosteric mechanisms that cannot be distinguished using ensemble measurements of ligand binding in bulk protein solutions. Native MS, which yields mass measurements of intact assemblies, can be used to determine the values of ligand binding constants of multimeric allosteric proteins, thereby providing a way to distinguish, for example, between concerted and sequential allosteric models. Native MS can also be employed to study cooperativity owing to ligand-modulated protein oligomerization. The rotationally averaged cross-section areas of complexes obtained by ion mobility MS can be used to distinguish between induced fit and conformational selection. Native MS and its allied techniques are, therefore, becoming increasingly powerful tools for dissecting allosteric mechanisms.

Indexed as

Allosteric RegulationLigandsMass SpectrometryModels, MolecularProtein BindingProtein ConformationProteinsLigandsProteins

Identifiers

PMID26005781
PMCPMC5702259

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.