ArticleBiophysical journal2008
External Ba2+ block of human Kv1.5 at neutral and acidic pH: evidence for Ho+-induced constriction of the outer pore mouth at rest.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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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.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Regulation of human cardiac Kv1.5 channels by extracellular acidification.Pflugers Archiv : European journal of physiology · 2016Article
- Apoptosis of Corneal Epithelial Cells Caused by Ultraviolet B-induced Loss of K(+) is Inhibited by Ba(2.).The ocular surface · 2016Article
- ShakerIR and Kv1.5 mutant channels with enhanced slow inactivation also exhibit K⁺ o-dependent resting inactivation.Pflugers Archiv : European journal of physiology · 2013Article
- External Ba2+ block of the two-pore domain potassium channel TREK-1 defines conformational transition in its selectivity filter.The Journal of biological chemistry · 2011Article
- Kinetic analysis of the effects of H+ or Ni2+ on Kv1.5 current shows that both ions enhance slow inactivation and induce resting inactivation.The Journal of physiology · 2010Article
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have shown that low pHo accelerates depolarization-induced inactivation and decreases the macroscopic conductance by reducing channel availability. To test the hypothesis that outer pore constriction underlies the decreased conductance at low pHo, external Ba2+ was used to examine the accessibility of the channel pore at rest under neutral and acidic conditions. At pHo 7.4, Ba2+ block of closed channels follows a monoexponential time course and involves a low-affinity superficial site (KD congruent with 1 mM, -80 mV, 0 mM Ko(+)) and a high-affinity site (KD congruent with 4 microM) deeper in the pore. Depolarization promotes Ba2+ dissociation and an analytical model incorporating state-dependent changes of Ba2+ affinity is presented that replicates the frequency dependence of the time course and the extent of block. Open-channel block by Ba2+ is weak. At pHo 5.5, both the access to and exit from the deep site is inhibited. These results are consistent with a low-pHo-induced conformational change in the outer pore that prevents Ba2+ binding at rest or unbinding during depolarization. If a pore constriction is involved, similar to that proposed to occur during P/C-type inactivation, this would imply that closed-state inactivation in Kv1.5 occurs under acidic conditions.
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Registered trials
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.