Evidence map›Paper›PMID 21115636›Full record

ArticleMolecular pharmacology2011

Glycine hinges with opposing actions at the acetylcholine receptor-channel transmitter binding site.

Prasad Purohit, Anthony Auerbach

Abstract read
In one paragraph

Article in Molecular pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  8. Article
  9. The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013
    Review
  10. Article
  11. Article
  12. Article
  13. Sources of energy for gating by neurotransmitters in acetylcholine receptor channels.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Article
  15. Design and control of acetylcholine receptor conformational change.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Prasad PurohitDepartment of Physiology and Biophysics, SUNY at Buffalo, Buffalo, NY 14214, USA.
Anthony Auerbach
University at Buffalo, State University of New York · US

Funding

Engineering a Transmitter Binding SiteR01NS064969 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI AUERBACH, ANTHONY L · 2009 to 2018
$4.1M
NINDS NIH HHS NS064969NINDS NIH HHS R01 NS064969
6 · The paper itself

Abstract

The extent to which agonists activate synaptic receptor-channels depends on both the intrinsic tendency of the unliganded receptor to open and the amount of agonist binding energy realized in the channel-opening process. We examined mutations of the nicotinic acetylcholine receptor transmitter binding site (α subunit loop B) with regard to both of these parameters. αGly147 is an "activation" hinge where backbone flexibility maintains high values for intrinsic gating, the affinity of the resting conformation for agonists and net ligand binding energy. αGly153 is a "deactivation" hinge that maintains low values for these parameters. αTrp149 (between these two glycines) serves mainly to provide ligand binding energy for gating. We propose that a concerted motion of the two glycine hinges (plus other structural elements at the binding site) positions αTrp149 so that it provides physiologically optimal binding and gating function at the nerve-muscle synapse.

Indexed as

GlycineAnimalsBinding SitesHEK293 CellsHumansIon Channel GatingIon ChannelsKineticsLigandsMembrane PotentialsMutationNicotinic AgonistsProtein ConformationReceptors, NicotinicTorpedoGlycineIon ChannelsLigandsNicotinic AgonistsReceptors, Nicotinic

Identifiers

PMID21115636
PMCPMC3061369
OpenAlexW2164750874

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.