Evidence map›Paper›PMID 8868050›Full record

ArticleThe Journal of general physiology1996

Interaction of internal Ba2+ with a cloned Ca(2+)-dependent K+ (hslo) channel from smooth muscle.

F Diaz, M Wallner, E Stefani, L Toro, R Latorre

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 48 citations in OpenAlex.

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  8. Mg2+ enhances voltage sensor/gate coupling in BK channels.The Journal of general physiology · 2008
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  17. A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification.Proceedings of the National Academy of Sciences of the United States of America · 2003
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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 1 institution in 1 country.

F DiazCentro de Estudios Cientificos de Santiago, Universidad de Chile.
M Wallner
E Stefani
L Toro
R Latorre
Centro de Estudios Científicos · CL

Funding

STRUCTURAL DETERMINANTS OF K(CA) CHANNEL FUNCTIONR01HL054970 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORO DE STEFANI, LIGIA G. · 1995 to 2009
$3.2M
NHLBI NIH HHS HL54970NIGMS NIH HHS GM50550
6 · The paper itself

Abstract

We have studied potassium currents through a cloned Ca(2+)-dependent K+ channel (hslo) from human myometrium. Currents were recorded in inside-out macropatches from membranes of Xenopus laevis oocytes. In particular, the inactivation-like process that these channels show at high positive potentials was assessed in order to explore its molecular nature. This current inhibition conferred a bell shape to the current-voltage curves. The kinetic and voltage dependence of this process suggested the possibility of a Ba2+ block. There were the following similarities between the inactivation process observed at zero-added Ba2+ and the internal Ba2+ block of hslo channels: (a) in the steady state, the voltage dependence of the current inhibition observed at zero-added Ba2+ was the same as the voltage dependence of the Ba2+ block; (b) the time constant for recovery from current decay at zero-added Ba2+ was the same as the time constant for current recovery from Ba2+ blockade; and (c) current decay was largely suppressed in both cases by adding a Ba2+ chelator [(+)-18-crown-6-tetracarboxylic acid] to the internal solution. In our experimental conditions, we determined that the Kd for the complex chelator-Ba2+ is 1.6 x 10(-10) M. We conclude that the current decay observed at zero-added Ba2+ to the internal solution is due to contaminant Ba2+ present in our solutions (approximately 70 nM) and not to an intrinsic gating process. The Ba2+ blocking reaction in hslo channels is bimolecular. Ba2+ binds to a site (Kd = 0.36 +/- 0.05 mM at zero applied voltage) that senses 92 +/- 25% of the potential drop from the internal membrane surface.

Indexed as

AnimalsBariumCalciumChelating AgentsCloning, MolecularElectrophysiologyEthers, CyclicHumansLipid BilayersMembrane PotentialsMuscle, SmoothOocytesPatch-Clamp TechniquesPotassium ChannelsXenopus laevisBariumCalciumChelating AgentsEthers, CyclicLipid BilayersPotassium Channels

Identifiers

PMID8868050
PMCPMC2216995
OpenAlexW2109196366

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.