Evidence map›Paper›PMID 29735740›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018

A non-equilibrium approach to allosteric communication.

Gerhard Stock, Peter Hamm

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. 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. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Real-time observation of ligand-induced allosteric transitions in a PDZ domain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Supertertiary protein structure affects an allosteric network.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020
    Review
  18. Review
  19. Article
  20. Allostery in Its Many Disguises: From Theory to Applications.Structure (London, England : 1993) · 2019
    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.

Gerhard StockBiomolecular Dynamics, Institute of Physics, Albert Ludwigs University, Freiburg, Germany stock@physik.uni-freiburg.de.ORCID 0000-0002-3302-3044
Peter HammDepartment of Chemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-1106-6032

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While the theory of protein folding is well developed, including concepts such as rugged energy landscape, folding funnel, etc., the same degree of understanding has not been reached for the description of the dynamics of allosteric transitions in proteins. This is not only due to the small size of the structural change upon ligand binding to an allosteric site, but also due to challenges in designing experiments that directly observe such an allosteric transition. On the basis of recent pump-probe-type experiments (Buchli

Indexed as

Allosteric RegulationProtein FoldingModels, MolecularMolecular Dynamics SimulationProtein Interaction MapsProteinsProteinsallosteric transitiondownhill foldingdynamic contentfree-energy landscapenon-equilibrium molecular dynamics simulationstime-resolved vibrational spectroscopy

Identifiers

PMID29735740
PMCPMC5941181

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.