Evidence map›Paper›PMID 35887302›Full record

ArticleInternational journal of molecular sciences2022

Disruption of a Conservative Motif in the C-Terminal Loop of the KCNQ1 Channel Causes LQT Syndrome.

Maria Karlova, Denis V Abramochkin, Ksenia B Pustovit, Tatiana Nesterova, Valery Novoseletsky, Gildas Loussouarn, Elena Zaklyazminskaya, Olga S Sokolova

Open access · goldAbstract readCase Reports
In one paragraph

Article in International journal of molecular sciences, 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
0.8field-weighted citation impact, top 26% 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, 6 citations in OpenAlex.

  1. Mapping the Functional Landscape ofmedRxiv : the preprint server for health sciences · 2025
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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

8 authors at 4 institutions in 2 countries.

Maria KarlovaFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Denis V AbramochkinFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Ksenia B PustovitFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Tatiana NesterovaInstitute of Immunology and Physiology, Ural Branch of Russian Academy of Sciences, 620049 Ekaterinburg, Russia.
Valery NovoseletskyFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Gildas LoussouarnNantes Université, CNRS, INSERM, l'institut du Thorax, F-44000 Nantes, France.
Elena ZaklyazminskayaPetrovsky National Research Center of Surgery, 119991 Moscow, Russia.
Olga S SokolovaFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.ORCID 0000-0003-4678-232X
Lomonosov Moscow State University · RUCentre National de la Recherche Scientifique · FRRussian Scientific Center of Surgery · RUUral Federal University · RU

Funding

Russian Science Foundation 22-14-00088
6 · The paper itself

Abstract

We identified a single nucleotide variation (SNV) (c.1264A > G) in the KCNQ1 gene in a 5-year-old boy who presented with a prolonged QT interval. His elder brother and mother, but not sister and father, also had this mutation. This missense mutation leads to a p.Lys422Glu (K422E) substitution in the Kv7.1 protein that has never been mentioned before. We inserted this substitution in an expression plasmid containing Kv7.1 cDNA and studied the electrophysiological characteristics of the mutated channel expressed in CHO-K1, using the whole-cell configuration of the patch-clamp technique. Expression of the mutant Kv7.1 channel in both homo- and heterozygous conditions in the presence of auxiliary subunit KCNE1 results in a significant decrease in tail current densities compared to the expression of wild-type (WT) Kv7.1 and KCNE1. This study also indicates that K422E point mutation causes a dominant negative effect. The mutation was not associated with a trafficking defect; the mutant channel protein was confirmed to localize at the cell membrane. This mutation disrupts the poly-Lys strip in the proximal part of the highly conserved cytoplasmic A−B linker of Kv7.1 that was not shown before to be crucial for channel functioning.

Indexed as

KCNQ1 Potassium ChannelLong QT SyndromeAgedChild, PreschoolHeterozygoteHumansMaleMutationPoint MutationKCNQ1 Potassium ChannelKCNQ1 protein, humanIKsinherited channelopathyKCNQ1Kv7.1LQTSpatch-clamp

Identifiers

PMID35887302
PMCPMC9316142
OpenAlexW4286218462

What Socratic 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 Socratic graph.