ArticleMolecular pharmacology2010
Inhibition of large-conductance Ca2+-activated K+ channels by nanomolar concentrations of Ag+.
Article in Molecular pharmacology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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.
Who cites it
3 citing papers in PubMed.
- Closed state-coupled C-type inactivation in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The relationship of aluminium and silver to neural tube defects; a case control.Iranian journal of pediatrics · 2012Article
- Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating.The Journal of general physiology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Silver has been widely used in various medical products because of its antibacterial properties. However, there is only limited information concerning silver-related cytotoxicity. In this study we show that Ag(+) at low nanomolar concentrations (<10 nM) strongly inhibits the activity of large-conductance Ca(2+)-activated K(+) channels (BK) (Slo1), a widely expressed and physiologically important potassium channel. The Ag(+) inhibition is caused by irreversible modification on cytosolically accessible parts of the BK channel. At least four intracellular cysteines are involved in this process. In addition, at least one of these key cysteines is not accessible to the bulkier thiolate-active reagent [2-(trimethylammonium)ethyl] methanethiosulfonate bromide. One of the cysteine-less constructs generated in this study shows gating properties similar to wild-type BK channel but with much lower Ag(+) sensitivity, in which the Ag(+) modification rate was decreased by approximately 20-fold. The results from the present study suggest a possible contribution of BK channel inhibition to the cytotoxicity of Ag(+) in humans and other species.
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Registered trials
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