Evidence map›Paper›PMID 34560053›Full record

ArticleBiochemical pharmacology2021

Probing the molecular basis for signal transduction through the Zinc-Activated Channel (ZAC).

Nawid Madjroh, Eleni Mellou, Laura Æbelø, Paul A Davies, Pella C Söderhielm, Anders A Jensen

Open access · hybridAbstract read
In one paragraph

Article in Biochemical pharmacology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Cryo-EM structure of the zinc-activated channel (ZAC) in the Cys-loop receptor superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. Review
  6. The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.British journal of pharmacology · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. 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

6 authors at 1 institution in 1 country.

Nawid MadjrohDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen Ø 2100, Denmark.
Eleni MellouDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen Ø 2100, Denmark.
Laura ÆbeløDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen Ø 2100, Denmark.
Paul A DaviesDepartment of Neuroscience, Tufts University School of Medicine, Boston, MA, United States.
Pella C SöderhielmDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen Ø 2100, Denmark.
Anders A JensenDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen Ø 2100, Denmark. Electronic address: aaj@sund.ku.dk.
Tufts University · US

Funding

Novel actions of neurosteroids on GABA (A) receptor traffickingR01MH097446 · NIMH · TUFTS UNIVERSITY BOSTON · PI DAVIES, PAUL ANDREW, MOSS, STEPHEN J · 2013 to 2017
$2.1M
Novel actions of neurosteroids on GABA (A) receptor traffickingR01NS108378 · NINDS · TUFTS UNIVERSITY BOSTON · PI DAVIES, PAUL ANDREW, MOSS, STEPHEN J · 2018 to 2022
$2.0M
Determining the effects of human KCC2 mutations on neuronal excitabilityR21NS111338 · NINDS · TUFTS UNIVERSITY BOSTON · PI DAVIES, PAUL ANDREW · 2019 to 2020
$454k
Sensory Hypersensitivity in Fragile X Syndrome Due to Deficits in Tonic Inhibition Reversed by Neuroactive SteroidsR21NS111064 · NINDS · TUFTS UNIVERSITY BOSTON · PI DAVIES, PAUL ANDREW · 2020 to 2021
$450k
NIMH NIH HHS R01 MH097446NINDS NIH HHS R01 NS108378NINDS NIH HHS R21 NS111064NINDS NIH HHS R21 NS111338
6 · The paper itself

Abstract

The molecular basis for the signal transduction through the classical Cys-loop receptors (CLRs) has been delineated in great detail. The Zinc-Activated Channel (ZAC) constitutes a so far poorly elucidated fifth branch of the CLR superfamily, and in this study we explore the molecular mechanisms underlying ZAC signaling in Xenopus oocytes by two-electrode voltage clamp electrophysiology. In studies of chimeric receptors fusing either the extracellular domain (ECD) or the transmembrane/intracellular domain (TMD-ICD) of ZAC with the complementary domains of 5-HT

Indexed as

AnimalsCysteine Loop Ligand-Gated Ion Channel ReceptorsGene Expression RegulationHumansMutationNerve Tissue ProteinsOocytesProtein SubunitsRecombinant Fusion ProteinsSignal TransductionXenopusZincCysteine Loop Ligand-Gated Ion Channel ReceptorsNerve Tissue ProteinsProtein SubunitsRecombinant Fusion ProteinsZACN protein, humanZincAgonist bindingChimeric subunitsCys-loop receptor (CLR)Leu9′ residuePentameric ligand-gated ion channel (pLGIC)Zinc-Activated Channel (ZAC)

Identifiers

PMID34560053
PMCPMC11359809
OpenAlexW3201299622

What OpenQuestion holds

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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.