Evidence map›Paper›PMID 25483285›Full record

ArticleChannels (Austin, Tex.)2014

Insights into the structural nature of the transition state in the Kir channel gating pathway.

Philip W Fowler, Murali K Bollepalli, Markus Rapedius, Ehsan Nematian-Ardestani, Lijun Shang, Mark Sp Sansom, Stephen J Tucker, Thomas Baukrowitz

Abstract read
In one paragraph

Article in Channels (Austin, Tex.), 2014. 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
–field-weighted citation impact
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.

  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

8 authors.

Philip W Fowlera Department of Biochemistry ; University of Oxford , Oxford , UK.
Murali K Bollepalli
Markus Rapedius
Ehsan Nematian-Ardestani
Lijun Shang
Mark Sp Sansom
Stephen J Tucker
Thomas Baukrowitz

Funding

British Heart Foundation PG/09/016/26992Wellcome Trust 083547/Z/07/ZWellcome Trust 084655Wellcome Trust 092970/Z/10/Z
6 · The paper itself

Abstract

In a previous study we identified an extensive gating network within the inwardly rectifying Kir1.1 (ROMK) channel by combining systematic scanning mutagenesis and functional analysis with structural models of the channel in the closed, pre-open and open states. This extensive network appeared to stabilize the open and pre-open states, but the network fragmented upon channel closure. In this study we have analyzed the gating kinetics of different mutations within key parts of this gating network. These results suggest that the structure of the transition state (TS), which connects the pre-open and closed states of the channel, more closely resembles the structure of the pre-open state. Furthermore, the G-loop, which occurs at the center of this extensive gating network, appears to become unstructured in the TS because mutations within this region have a 'catalytic' effect upon the channel gating kinetics.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsMolecular Sequence DataPotassium Channels, Inwardly RectifyingRatsXenopusKcnj1 protein, ratPotassium Channels, Inwardly Rectifying

Identifiers

PMID25483285
PMCPMC4594414

What OpenQuestion holds

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LicenceCC BY
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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.