ArticleThe Journal of general physiology1997
Selectivity changes during activation of mutant Shaker potassium channels.
Article in The Journal of general physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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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
73 citing papers in PubMed, 127 citations in OpenAlex.
- Distinct functional open states of the polymodal nociceptor TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Barium senses subtle pore changes in a voltage-gated KScience advances · 2026Article
- Opening of capsaicin receptor TRPV1 is stabilized equally by its four subunits.The Journal of biological chemistry · 2023Article
- The Negative Allosteric Modulator EU1794-4 Reduces Single-Channel Conductance and CaMolecular pharmacology · 2021Article
- TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Shifts in the selectivity filter dynamics cause modal gating in KNature communications · 2019Article
- Polyamine-mediated channel block of ionotropic glutamate receptors and its regulation by auxiliary proteins.The Journal of biological chemistry · 2018Review
- The conformational wave in capsaicin activation of transient receptor potential vanilloid 1 ion channel.Nature communications · 2018Article
- The gating cycle of a KeLife · 2017Article
- Article
- A pain-inducing centipede toxin targets the heat activation machinery of nociceptor TRPV1.Nature communications · 2015Article
- Proton block of proton-activated TRPV1 current.The Journal of general physiology · 2015Article
- Hydrogen bonds as molecular timers for slow inactivation in voltage-gated potassium channels.eLife · 2013Article
- Single-channel basis for the slow activation of the repolarizing cardiac potassium current, I(Ks).Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Multiple pore conformations driven by asynchronous movements of voltage sensors in a eukaryotic sodium channel.Nature communications · 2013Article
- A linkage analysis toolkit for studying allosteric networks in ion channels.The Journal of general physiology · 2013Article
- Partial opening and subconductance gating of mechanosensitive ion channels in dystrophic skeletal muscle.The Journal of physiology · 2012Article
- Tetrameric assembly of KvLm K+ channels with defined numbers of voltage sensors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Being flexible: the voltage-controllable activation gate of kv channels.Frontiers in pharmacology · 2012Article
- On the structural basis of modal gating behavior in K(+) channels.Nature structural & molecular biology · 2011Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mutations of the pore-region residue T442 in Shaker channels result in large effects on channel kinetics. We studied mutations at this position in the backgrounds of NH2-terminal-truncated Shaker H4 and a Shaker -NGK2 chimeric channel having high conductance (Lopez, G.A., Y.N. Jan, and L.Y. Jan. 1994. Nature (Lond.). 367: 179-182). While mutations of T442 to C, D, H, V, or Y resulted in undetectable expression in Xenopus oocytes, S and G mutants yielded functional channels having deactivation time constants and channel open times two to three orders of magnitude longer than those of the parental channel. Activation time courses at depolarized potentials were unaffected by the mutations, as were first-latency distributions in the T442S chimeric channel. The mutant channels show two subconductance levels, 37 and 70% of full conductance. From single-channel analysis, we concluded that channels always pass through the larger subconductance state on the way to and from the open state. The smaller subconductance state is traversed in approximately 40% of activation time courses. These states apparently represent kinetic intermediates in channel gating having voltage-dependent transitions with apparent charge movements of approximately 1.6 e0. The fully open T442S chimeric channel has the conductance sequence Rb+ > NH4+ > K+. The opposite conductance sequence, K+ > NH4+ > Rb+, is observed in each of the subconductance states, with the smaller subconductance state discriminating most strongly against Rb+.
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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.