Evidence map›Paper›PMID 26338443›Full record

ArticleBiophysical journal2015

Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?

Tom C B McLeish, Martin J Cann, Thomas L Rodgers

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  5. Article
  6. Article
  7. Review
  8. Interaction ofToxins · 2022
    Article
  9. Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Ancient thioredoxins evolved to modern-day stability-function requirement by altering native state ensemble.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
  17. 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
  18. Review
  19. A non-equilibrium approach to allosteric communication.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  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

3 authors at 2 institutions in 1 country.

Tom C B McLeishBiophysical Sciences Institute, Durham University, Durham, United Kingdom; Department of Physics, Durham University, Durham, United Kingdom. Electronic address: t.c.b.mcleish@durham.ac.uk.
Martin J CannBiophysical Sciences Institute, Durham University, Durham, United Kingdom; School of Biological and Biomedical Sciences, Durham University, Durham, United Kingdom.
Thomas L RodgersSchool of Chemical Engineering and Analytical Sciences, University of Manchester, Manchester, United Kingdom.
Durham University · GBUniversity of Manchester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examine the contrast between mechanisms for allosteric signaling that involve structural change, and those that do not, from the perspective of allosteric pathways. In particular we treat in detail the case of fluctuation-allostery by which amplitude modulation of the thermal fluctuations of the elastic normal modes conveys the allosteric signal, and address the question of what an allosteric pathway means in this case. We find that a perturbation theory of thermal elastic solids and nonperturbative approach (by super-coarse-graining elasticity into internal bending modes) have opposite signatures in their structure of correlated pathways. We illustrate the effect from analysis of previous results from GlxR of Corynebacterium glutamicum, an example of the CRP/FNR transcription family of allosteric homodimers. We find that the visibility of both correlated pathways and disconnected sites of correlated motion in this protein suggests that mechanisms of local elastic stretch and bend are recruited for the purpose of creating and controlling allosteric cooperativity.

Indexed as

Allosteric RegulationBacterial ProteinsComputer SimulationCorynebacterium glutamicumDimerizationElasticityModels, MolecularMutationBacterial Proteins

Identifiers

PMID26338443
PMCPMC4576321
OpenAlexW2103629368

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.