Evidence map›Paper›PMID 26000062›Full record

ArticleBiophysical reviews

Global low-frequency motions in protein allostery: CAP as a model system.

Philip D Townsend, Thomas L Rodgers, Ehmke Pohl, Mark R Wilson, Tom C B McLeish, Martin J Cann

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical reviews. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Seeing the light with BLUF proteins.Biophysical reviews · 2017
    Review
  7. NMR Methods to Study Dynamic Allostery.PLoS computational biology · 2016
    Review
  8. Review
  9. Article
  10. Article
  11. 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

6 authors.

Philip D TownsendBiophysical Sciences Institute, Durham University, Durham, UK ; School of Biological and Biomedical Sciences, Durham University, Durham, UK.
Thomas L RodgersBiophysical Sciences Institute, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK ; School of Chemical Engineering and Analytical Sciences, University of Manchester, Manchester, UK.
Ehmke PohlBiophysical Sciences Institute, Durham University, Durham, UK ; School of Biological and Biomedical Sciences, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK.
Mark R WilsonBiophysical Sciences Institute, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK.
Tom C B McLeishBiophysical Sciences Institute, Durham University, Durham, UK ; Department of Chemistry, Durham University, Durham, UK ; Department of Physics, Durham University, Durham, UK.
Martin J CannBiophysical Sciences Institute, Durham University, Durham, UK ; School of Biological and Biomedical Sciences, Durham University, Durham, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of

Indexed as

AllosteryCatabolite activator proteinDynamicsElastic network modelNormal modesProtein

Identifiers

PMID26000062
PMCPMC4432019

What OpenQuestion holds

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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.