ArticlePflugers Archiv : European journal of physiology2005
Role of Domain IV/S4 outermost arginines in gating of T-type calcium channels.
Article in Pflugers Archiv : European journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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.
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
12 citing papers in PubMed, 17 citations in OpenAlex.
- Role of individual S4 segments in gating of CaChannels (Austin, Tex.) · 2018Article
- Contribution of S4 segments and S4-S5 linkers to the low-voltage activation properties of T-type CaV3.3 channels.PloS one · 2018Article
- Contrasting the roles of the I-II loop gating brake in CaV3.1 and CaV3.3 calcium channels.Pflugers Archiv : European journal of physiology · 2015Article
- A Recurrent Mutation in CACNA1G Alters Cav3.1 T-Type Calcium-Channel Conduction and Causes Autosomal-Dominant Cerebellar Ataxia.American journal of human genetics · 2015Article
- Ins and outs of T-channel structure function.Pflugers Archiv : European journal of physiology · 2014Review
- Inhibition of the activation pathway of the T-type calcium channel Ca(V)3.1 by ProTxII.Toxicon : official journal of the International Society on Toxinology · 2010Article
- I-II loop structural determinants in the gating and surface expression of low voltage-activated calcium channels.PloS one · 2008Article
- Characterization of the gating brake in the I-II loop of Ca(v)3.2 T-type Ca(2+) channels.The Journal of biological chemistry · 2008Article
- Defective protein folding and intracellular retention of thyroglobulin-R19K mutant as a cause of human congenital goiter.Molecular endocrinology (Baltimore, Md.) · 2008Article
- The effect of the outermost basic residues in the S4 segments of the Ca(V)3.1 T-type calcium channel on channel gating.Pflugers Archiv : European journal of physiology · 2007Article
- Evidence for common structural determinants of activation and inactivation in T-type Ca2+ channels.Pflugers Archiv : European journal of physiology · 2006Article
- Characterization of the gating brake in the I-II loop of CaV3 T-type calcium channels.Channels (Austin, Tex.)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The role of the outermost three charged residues of Domain IV/S4 in controlling gating of Ca(v)3.2 was investigated using single substitutions of each arginine with glutamine, cysteine, histidine, and lysine in a Flp-In-293 cell line, in which expression levels could be compared. Channel density, based on gating charge measurements, was ~125,000 channels/cell (10 fC/pF), except for R2Q and R3C, which expressed at lower levels. Channels substituted at Arg-1715 (R1C, R1Q, R1H) demonstrated such modest changes that a role in voltage sensing could not be determined. Arg-1718 (R2) made a contribution to activation voltage sensing, and the channel was sensitive to the geometry of side-chain substitutions at this position. Arg-1721 (R3) substitutions produced complex kinetic changes that together suggested that geometry made a larger contribution than charge. Current decay at positive potentials (O-->I) exponentially approached a constant value for all mutants except R2K channels, which were biphasically dependent on potential. R2K channels also displayed slowed deactivation with reduced voltage dependence despite near control values for conductance. Voltage-dependent accessibility of R to C mutants, evaluated with intracellularly and extracellularly applied methanthiosulfonate (MTS) reagents, showed that both R2 and R3 were exposed only when cells were depolarized, although it was not necessary for channels to open. Together, the data indicate that Domain IV/S4 is an activation domain and is not involved in inactivation from the open state.
Indexed as
Identifiers
What OpenQuestion holds
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.