Trial reportThe Journal of physiology1999
Characterization of a new sodium channel mutation at arginine 1448 associated with moderate Paramyotonia congenita in humans.
Trial report in The Journal of physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 50 citations in OpenAlex.
- Sodium channelopathies of skeletal muscle and brain.Physiological reviews · 2021Review
- Role of the voltage sensor module in NaChannels (Austin, Tex.) · 2019Review
- Hypokalaemic periodic paralysis and myotonia in a patient with homozygous mutation p.R1451L in NaScientific reports · 2018Article
- Substitutions of the S4DIV R2 residue (R1451) in NaScientific reports · 2018Article
- N1366S mutation of human skeletal muscle sodium channel causes paramyotonia congenita.The Journal of physiology · 2017Article
- A recessive Nav1.4 mutation underlies congenital myasthenic syndrome with periodic paralysis.Neurology · 2016Article
- Mutation analysis in exons 22 and 24 of SCN4A gene in Iranian patients with non-dystrophic myotonia.Iranian journal of neurology · 2015Article
- Physiological and Pathophysiological Insights of Nav1.4 and Nav1.5 Comparison.Frontiers in pharmacology · 2015Review
- Mechanisms underlying a life-threatening skeletal muscle Na+ channel disorder.The Journal of physiology · 2011Article
- Skeletal muscle na channel disorders.Frontiers in pharmacology · 2011Article
- The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation.Molecular pharmacology · 2010Article
- Sodium channel carboxyl-terminal residue regulates fast inactivation.The Journal of biological chemistry · 2010Article
- Functional characterization and cold sensitivity of T1313A, a new mutation of the skeletal muscle sodium channel causing paramyotonia congenita in humans.The Journal of physiology · 2004Article
- Different flecainide sensitivity of hNav1.4 channels and myotonic mutants explained by state-dependent block.The Journal of physiology · 2004Article
- Outer and central charged residues in DIVS4 of skeletal muscle sodium channels have differing roles in deactivation.Biophysical journal · 2002Article
- A missense mutation of the Na+ channel alpha II subunit gene Na(v)1.2 in a patient with febrile and afebrile seizures causes channel dysfunction.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Channelopathies: ion channel defects linked to heritable clinical disorders.Journal of medical genetics · 2000Review
- The delay in recovery from fast inactivation in skeletal muscle sodium channels is deactivation.Cellular and molecular neurobiology · 2000Article
- Open- and closed-state fast inactivation in sodium channels: differential effects of a site-3 anemone toxin.Channels (Austin, Tex.)Article
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 3 institutions in 2 countries.
Funding
Abstract
1. Paramyotonia congenita is a temperature-sensitive skeletal muscle disorder caused by missense mutations that occur in the adult skeletal muscle voltage-gated sodium channel. We report here the identification of a new genetic mutation in a family with the paramyotonia congenita phenotype. 2. Single-strand conformation polymorphism analysis and DNA sequencing showed that the defect was linked to a single nucleotide substitution causing an amino acid change from an arginine to a serine at position 1448 in the human sodium channel alpha-subunit. 3. Expression of the altered protein in human embryonic kidney (HEK) 293 cells revealed several defects in channel function: (i) the rate of fast inactivation was slower in the mutant channel compared with wild-type, (ii) steady-state fast inactivation was shifted towards hyperpolarizing potentials, (iii) the R1448S channels deactivated much more slowly, and (iv) the mutant channels recovered from the fast inactivated state more rapidly. 4. By contrast, the activation curve, steady-state slow inactivation and the rate of onset and recovery from slow inactivation were not altered by the R1448S mutation. 5. These data show that the defects observed in the sodium channel function could well explain the onset of the paramyotonia congenita in this family and emphasize the role of segment S4 of domain IV in sodium channel inactivation.
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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.