Evidence map›Paper›PMID 35411015›Full record

ArticleCommunications biology2022

A selectivity filter mutation provides insights into gating regulation of a K

Theres Friesacher, Haritha P Reddy, Harald Bernsteiner, J Carlo Combista, Boris Shalomov, Amal K Bera, Eva-Maria Zangerl-Plessl, Nathan Dascal, Anna Stary-Weinzinger

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 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
0.3field-weighted citation impact, top 45% 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, 4 citations in OpenAlex.

  1. Article
  2. 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

9 authors at 3 institutions in 3 countries.

Theres Friesacher *Department of Pharmaceutical Sciences, Division of Pharmacology and Toxicology, University of Vienna, Josef-Holaubek-Platz 2, 1090, Vienna, Austria.ORCID http://orcid.org/0000-0001-5632-3472
Haritha P Reddy *Department of Physiology and Pharmacology, School of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.ORCID http://orcid.org/0000-0002-6280-6558
Harald BernsteinerDepartment of Pharmaceutical Sciences, Division of Pharmacology and Toxicology, University of Vienna, Josef-Holaubek-Platz 2, 1090, Vienna, Austria.
J Carlo CombistaDepartment of Physiology and Pharmacology, School of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Boris ShalomovDepartment of Physiology and Pharmacology, School of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Amal K BeraDepartment of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.
Eva-Maria Zangerl-PlesslDepartment of Pharmaceutical Sciences, Division of Pharmacology and Toxicology, University of Vienna, Josef-Holaubek-Platz 2, 1090, Vienna, Austria.
Nathan DascalDepartment of Physiology and Pharmacology, School of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel. dascaln@tauex.tau.ac.il.ORCID http://orcid.org/0000-0002-5397-4146
Anna Stary-WeinzingerDepartment of Pharmaceutical Sciences, Division of Pharmacology and Toxicology, University of Vienna, Josef-Holaubek-Platz 2, 1090, Vienna, Austria. anna.stary@univie.ac.at.ORCID http://orcid.org/0000-0002-9202-0484
Tel Aviv University · ILUniversity of Vienna · ATIndian Institute of Technology Madras · IN

Funding

Austrian Science Fund FWF W 1232
6 · The paper itself

Abstract

G-protein coupled inwardly rectifying potassium (GIRK) channels are key players in inhibitory neurotransmission in heart and brain. We conducted molecular dynamics simulations to investigate the effect of a selectivity filter (SF) mutation, G154S, on GIRK2 structure and function. We observe mutation-induced loss of selectivity, changes in ion occupancy and altered filter geometry. Unexpectedly, we reveal aberrant SF dynamics in the mutant to be correlated with motions in the binding site of the channel activator Gβγ. This coupling is corroborated by electrophysiological experiments, revealing that GIRK2

Indexed as

G Protein-Coupled Inwardly-Rectifying Potassium ChannelsIon Channel GatingBinding SitesHumansMutationPotassiumG Protein-Coupled Inwardly-Rectifying Potassium ChannelsPotassium

Identifiers

PMID35411015
PMCPMC9001731
OpenAlexW4226070838

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.