Evidence map›Paper›PMID 37569445›Full record

ArticleInternational journal of molecular sciences2023

Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking.

Koichiro Oishi, Mayu Nagamori, Yasuhiro Kashino, Hiroshi Sekiguchi, Yuji C Sasaki, Atsuo Miyazawa, Yuri Nishino

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. 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 37% 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, 2 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

7 authors at 2 institutions in 1 country.

Koichiro OishiGraduate School of Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Kobe 678-1297, Hyogo, Japan.
Mayu NagamoriGraduate School of Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Kobe 678-1297, Hyogo, Japan.
Yasuhiro KashinoGraduate School of Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Kobe 678-1297, Hyogo, Japan.
Hiroshi SekiguchiCenter for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Sayo 679-5198, Hyogo, Japan.ORCID 0000-0001-7590-3624
Yuji C SasakiCenter for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Sayo 679-5198, Hyogo, Japan.ORCID 0000-0003-3403-237X
Atsuo MiyazawaGraduate School of Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Kobe 678-1297, Hyogo, Japan.
Yuri NishinoGraduate School of Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Kobe 678-1297, Hyogo, Japan.
University of Hyogo · JPJapan Synchrotron Radiation Research Institute · JP

Funding

Japan Society for the Promotion of Science JP16K21289Nakatani FoundationShimadzu Science Foundation
6 · The paper itself

Abstract

Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that play an important role in signal transduction at the neuromuscular junction (NMJ). Movement of the nAChR extracellular domain following agonist binding induces conformational changes in the extracellular domain, which in turn affects the transmembrane domain and opens the ion channel. It is known that the surrounding environment, such as the presence of specific lipids and proteins, affects nAChR function. Diffracted X-ray tracking (DXT) facilitates measurement of the intermolecular motions of receptors on the cell membranes of living cells, including all the components involved in receptor function. In this study, the intramolecular motion of the extracellular domain of native nAChR proteins in living myotube cells was analyzed using DXT for the first time. We revealed that the motion of the extracellular domain in the presence of an agonist (e.g., carbamylcholine, CCh) was restricted by an antagonist (i.e., alpha-bungarotoxin, BGT).

Indexed as

Receptors, NicotinicLigandsMuscle Fibers, SkeletalProtein DomainsX-RaysLigandsReceptors, Nicotinicdiffracted X-ray trackingintramolecular motionligand-dependent gatingliving cellnicotinic acetylcholine receptor

Identifiers

PMID37569445
PMCPMC10418694
OpenAlexW4385347835

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.