Evidence map›Paper›PMID 36295771›Full record

ArticleMembranes2022

Expression of Mutant Glycine Receptors in

Sarah C R Lummis, Dennis A Dougherty

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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 at 2 institutions in 2 countries.

Sarah C R LummisDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Dennis A DoughertyDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
California Institute of Technology · USUniversity of Cambridge · GB

Funding

PROBING RECEPTOR STRUCTURES WITH UNNATURAL AMINO ACIDSR01NS034407 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DOUGHERTY, DENNIS A · 1995 to 2016
$3.1M
Probing Receptor Structures with Unnatural Amino AcidsR37NS034407 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DOUGHERTY, DENNIS A · 2004 to 2010
$2.7M
Medical Research Council MR/L021676Medical Research Council MR/L021676/1NIH HHS NS-34407
6 · The paper itself

Abstract

Pentameric ligand-gated ion channels (pLGIC) play important roles in fast neuronal signal transmission. Functional receptors are pentamers, with each subunit having an extracellular domain (ECD), a transmembrane domain (TMD) and an intracellular domain. The binding of the agonist to the ECD induces a structural change that is transduced to the TMD to open the channel. Molecular details of this process are emerging, but a comprehensive understanding is still lacking. Proline (Pro) is one amino acid that has attracted much interest; its unusual features generate bends in loops and kinks and bulges in helices, which can be essential for function in some pLGICs. Here, we explore the roles of four conserved Pros in the glycine receptor (GlyR), creating substitutions with canonical and noncanonical amino acids, characterizing them using two electrode voltage clamp electrophysiology in

Indexed as

cis prolyl peptide bondCys-loop receptorelectrophysiologyligand-gated ion channelmutagenesisnoncanonical amino acid

Identifiers

PMID36295771
PMCPMC9607081
OpenAlexW4306849882

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.