Evidence map›Paper›PMID 24956197›Full record

ArticlePloS one2014

From pan-reactive KV7 channel opener to subtype selective opener/inhibitor by addition of a methyl group.

Sigrid Marie Blom, Mario Rottländer, Jan Kehler, Christoffer Bundgaard, Nicole Schmitt, Henrik Sindal Jensen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 13 citations in OpenAlex.

  1. Chemical modulation of Kv7 potassium channels.RSC medicinal chemistry · 2021
    Review
  2. Activation of KCNQ4 as a Therapeutic Strategy to Treat Hearing Loss.International journal of molecular sciences · 2021
    Review
  3. 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 3 institutions in 1 country.

Sigrid Marie BlomDivision of Neuroscience Drug Discovery, H. Lundbeck A/S, Copenhagen, Denmark; Department of Biomedical Sciences and Danish National Research Foundation Centre for Cardiac Arrhythmia, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Mario RottländerDivision of Discovery Chemistry and DMPK, H. Lundbeck A/S, Copenhagen, Denmark.
Jan KehlerDivision of Discovery Chemistry and DMPK, H. Lundbeck A/S, Copenhagen, Denmark.
Christoffer BundgaardDivision of Discovery Chemistry and DMPK, H. Lundbeck A/S, Copenhagen, Denmark.
Nicole SchmittDepartment of Biomedical Sciences and Danish National Research Foundation Centre for Cardiac Arrhythmia, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Henrik Sindal JensenDivision of Neuroscience Drug Discovery, H. Lundbeck A/S, Copenhagen, Denmark.
Lundbeck (Denmark) · DKDanish National Research Foundation · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The voltage-gated potassium channels of the KV7 family (KV7.1-5) play important roles in controlling neuronal excitability and are therefore attractive targets for treatment of CNS disorders linked to hyperexcitability. One of the main challenges in developing KV7 channel active drugs has been to identify compounds capable of discriminating between the neuronally expressed subtypes (KV7.2-5), aiding the identification of the subunit composition of KV7 currents in various tissues, and possessing better therapeutic potential for particular indications. By taking advantage of the structure-activity relationship of acrylamide KV7 channel openers and the effects of these compounds on mutant KV7 channels, we have designed and synthesized a novel KV7 channel modulator with a unique profile. The compound, named SMB-1, is an inhibitor of KV7.2 and an activator of KV7.4. SMB-1 inhibits KV7.2 by reducing the current amplitude and increasing the time constant for the slow component of the activation kinetics. The activation of KV7.4 is seen as an increase in the current amplitude and a slowing of the deactivation kinetics. Experiments studying mutant channels with a compromised binding site for the KV7.2-5 opener retigabine indicate that SMB-1 binds within the same pocket as retigabine for both inhibition of KV7.2 and activation of KV7.4. SMB-1 may serve as a valuable tool for KV7 channel research and may be used as a template for further design of better subtype selective KV7 channel modulators. A compound with this profile could hold novel therapeutic potential such as the treatment of both positive and cognitive symptoms in schizophrenia.

Indexed as

KCNQ2 Potassium ChannelKCNQ Potassium ChannelsMutation, MissenseAmino Acid SubstitutionAnimalsHumansMembrane Transport ModulatorsXenopus laevisKCNQ2 Potassium ChannelKCNQ4 protein, humanKCNQ5 protein, humanKCNQ Potassium ChannelsMembrane Transport Modulators

Identifiers

PMID24956197
PMCPMC4067310
OpenAlexW2018007163

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.