Evidence map›Paper›PMID 22552870›Full record

ReviewEuropean biophysics journal : EBJ2013

Insights into hERG K+ channel structure and function from NMR studies.

Chai Ann Ng, Allan M Torres, Guilhem Pagès, Philip W Kuchel, Jamie I Vandenberg

Abstract readReview
PubMed Publisher
In one paragraph

Review in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

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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

5 authors at 4 institutions in 2 countries.

Chai Ann NgMark Cowley Lidwill Research Programme in Cardiac Electrophysiology, Molecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, NSW, 2010, Australia. a.ng@victorchang.edu.au
Allan M Torres
Guilhem Pagès
Philip W Kuchel
Jamie I Vandenberg
Victor Chang Cardiac Research Institute · AUSingapore Bioimaging Consortium · SGUniversity of Sydney · AUWestern Sydney University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unique gating kinetics of hERG K(+) channels are critical for normal cardiac repolarization, and patients with mutations in hERG have a markedly increased risk of cardiac arrhythmias and sudden cardiac arrest. HERG K(+) channels are also remarkably promiscuous with respect to drug binding, which has been a very significant problem for the pharmaceutical industry. Here, we review the progress that has been made in understanding the structure and function of hERG K(+) channels with a particular focus on nuclear magnetic resonance studies of the domains of the hERG K(+) channel.

Indexed as

Amino Acid SequenceBinding SitesEther-A-Go-Go Potassium ChannelsHumansMagnetic Resonance SpectroscopyMolecular Docking SimulationMolecular Sequence DataProtein Structure, TertiaryEther-A-Go-Go Potassium ChannelsKCNH1 protein, human

Identifiers

PMID22552870
OpenAlexW1991985127

What OpenQuestion holds

Textmetadata
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.