Evidence map›Paper›PMID 25505495›Full record

ArticleBiophysical reviews

Protein dynamics and the allosteric transitions of pentameric receptor channels.

Jean-Pierre Changeux

Open access · hybridAbstract read
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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Monod-Wyman-Changeux Analysis of Ligand-Gated Ion Channel Mutants.The journal of physical chemistry. B · 2017
    Article
  5. Article
  6. Article
  7. 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

1 author at 1 institution in 1 country.

Jean-Pierre ChangeuxUMR 3571 CNRS, Institut Pasteur, 25 rue du Docteur Roux, 75015 Paris, France ; Collège de France, 11 Place Marcelin Berthelot, 75005 Paris, France ; Kavli Brain-Mind Institute University of California, San Diego, CA USA.
Collège de France · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent application of molecular dynamics (MD) methodology to investigate the allosteric transitions of the acetylcholine receptor and its prokaryotic and eukaryotic pentameric homologs has yielded new insights into the mechanisms of signal transduction by these receptors. Combined with available data on X-ray structures, MD techniques enable description of the dynamics of the conformational change at the atomic level, intra-molecular propagation of this signal transduction mechanism as a concerted stepwise process at physiological timescales and the control of this process by allosteric modulators, thereby offering new perspectives for drug design.

Indexed as

Acetylcholine receptorAllosteric interactionsConformational changesMolecular dynamics

Identifiers

PMID25505495
PMCPMC4256460
OpenAlexW2075186394

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.