Evidence map›Paper›PMID 10930133›Full record

ArticleCellular and molecular neurobiology2000

Forskolin modulates acetylcholine receptor gating by interacting with the small extracellular loop between the M2 and M3 transmembrane domains.

Z Chen, M M White

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular neurobiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Z ChenDepartment of Pharmacology and Physiology, MCP Hahnemann University, Philadelphia, Pennsylvania 19129, USA.
M M White
Drexel University · US

Funding

STRUCTURAL ASPECTS OF ION CHANNEL FUNCTION AND ASSEMBLYR01NS023885 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI WHITE, MICHAEL MCCORMICK · 1986 to 1999
–
NINDS NIH HHS NS23885
6 · The paper itself

Abstract

1. Forskolin acts as an allosteric modulator of muscle-type nicotinic acetylcholine receptors. Receptors from mouse muscle and Torpedo electroplax demonstrate differential sensitivity to inhibition by forskolin. Previous work from this laboratory suggested that the gamma subunit is responsible for this differential sensitivity. 2. We have used a series of mouse/Torpedo species-chimeric gamma subunits to further define the site of forskolin interaction with the gamma subunit. Analysis of the patterns of forskolin inhibition of receptors containing mouse/Torpedo chimeric gamma subunits along with the mouse alpha, beta, and delta subunits suggests that forskolin interacts with the small extracellular domain that links the M2 and M3 transmembrane domains (the M2-M3 linker). 3. We suggest that the M2-M3 linker domain plays an important role in the transduction of ligand binding to the conformational changes that result in channel opening.

Indexed as

Allosteric RegulationAnimalsColforsinElectrophysiologyIon Channel GatingMiceOocytesProtein Structure, TertiaryReceptors, NicotinicRecombinant Fusion ProteinsTorpedoXenopusColforsinReceptors, NicotinicRecombinant Fusion Proteins

Identifiers

PMID10930133
PMCPMC11537508
OpenAlexW288453037

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.