Evidence map›Paper›PMID 15516518›Full record

ArticleBiophysical journal2005

A ring of negative charges in the intracellular vestibule of Kir2.1 channel modulates K+ permeation.

Hsueh-Kai Chang, Shih-Hao Yeh, Ru-Chi Shieh

Abstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Activation of the CaPflugers Archiv : European journal of physiology · 2016
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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

3 authors.

Hsueh-Kai ChangInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, Republic of China.
Shih-Hao Yeh
Ru-Chi Shieh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glutamate at site 224 of a Kir2.1 channel plays an important role in K+ permeation. The single-channel inward current flickers with reduced conductance in an E224G mutant. We show that open-channel fluctuations can also be observed in E224C, E224K, and E224Q mutants. Yet, open-channel fluctuations were not observed in either the wild-type or an E224D mutant. Introducing a negatively charged methanethiosulfonate reagent to the E224C mutant irreversibly increased channel conductance and eliminated open-channel fluctuations. These results suggest that although the negatively charged residue 224 is located at the internal vestibule, it is important for smooth inward K+ conduction. We identified a substate in the E224G mutant and showed that open-channel fluctuations are mainly attributed to rapid transitions between the substate and the main state. Also, we characterized the voltage- and ion-dependence of the substate kinetics. The open-channel fluctuations decreased in internal NH4+ or Tl+ as compared to internal K+. These results suggest that NH4+ and Tl+ gate the E224G mutant in a more stable state. Based on an ion-conduction model, we propose that the appearance of the substate in the E224G mutant is due to changes of ion gating in association with variations of ion-ion interaction in the permeation pathway.

Indexed as

AnimalsBinding SitesCesiumCytoplasmElectrophysiologyGlutamic AcidIon Channel GatingIonsKineticsMesylatesMutationPotassiumPotassium Channels, Inwardly RectifyingProtein BindingProtein ConformationProtein Structure, TertiaryCesiumGlutamic AcidIonsKir2.1 channelMesylatesmethanethiosulfonatePotassiumPotassium Channels, Inwardly Rectifying

Identifiers

PMID15516518
PMCPMC1305002

What OpenQuestion holds

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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.