The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Sodium channel mutations in paramyotonia congenita uncouple inactivation from activation
Open accessAbstract
Mutations in the adult human skeletal muscle Na+ channel alpha subunit cause the disease paramyotonia congenita. Two paramyotonia congenita mutations, R1448H and R1448C, substitute histidine and cysteine for arginine in the S4 segment of domain 4. These mutations, expressed in a cell line, have only small effects on the activation of Na+ currents, but mutant channels inactivate more slowly with less voltage dependence than wild-type channels and exhibit an enhanced rate of recovery from inactivation. Increase of extracellular pH made the rate of inactivation of R1448H similar to that of R1448C, suggesting that this residue has an extracellular location and that its charge is important for normal inactivation. Analysis of single-channel data reveals that mutant channels inactivate normally from closed states, but poorly from the open state. The data suggest a critical role for the S4 helix of domain 4 in coupling between activation and inactivation.
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Cites
Bootstrap methods: another look at the jackknife
Efron, B. (1979) · The Annals of Statistics · doi:10.1214/aos/1176344552 · Cited by 17,602
Ionic Blockage of Sodium Channels in Nerve
Woodhull, A. M. (1973) · The Journal of General Physiology · doi:10.1085/jgp.61.6.687 · Cited by 1,569
Biophysical and Molecular Mechanisms of Shaker Potassium Channel Inactivation
Hoshi, T., Zagotta, W. N., & Aldrich, R. W. (1990) · Science · doi:10.1126/science.2122519 · Cited by 1,538
Inactivation of the sodium channel. I. Sodium current experiments.
Bezanilla, F., & Armstrong, C. M. (1977) · The Journal of general physiology · doi:10.1085/jgp.70.5.549 · Cited by 1,500
Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence
Noda, M., Shimizu, S., Tanabe, T., Takai, T., Kayano, T., Ikeda, T., Takahashi, H., Nakayama, H., Kanaoka, Y., Minamino, N., et al. (1984) · Nature · doi:10.1038/312121a0 · Cited by 1,350
Structural parts involved in activation and inactivation of the sodium channel
Stühmer, W., Conti, F., Suzuki, H., Wang, X., Noda, M., Yahagi, N., Kubo, H., & Numa, S. (1989) · Nature · doi:10.1038/339597a0 · Cited by 1,215
Ashcroft, F. (1984) · Neuroscience · doi:10.1016/0306-4522(84)90114-3 · Cited by 982
Inactivation of the sodium channel. II. Gating current experiments.
Armstrong, C. M., & Bezanilla, F. (1977) · The Journal of general physiology · doi:10.1085/jgp.70.5.567 · Cited by 959
A cluster of hydrophobic amino acid residues required for fast Na(+)-channel inactivation.
West, J. W., Patton, D. E., Scheuer, T., Wang, Y., Goldin, A. L., & Catterall, W. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10910 · Cited by 830
Hoshi, T., Zagotta, W. N., & Aldrich, R. W. (1991) · Neuron · doi:10.1016/0896-6273(91)90367-9 · Cited by 694
Cited by
Rush, A. M., Dib‐Hajj, S. D., & Waxman, S. G. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.083089 · Cited by 278
Effects of temperature on slow and fast inactivation of rat skeletal muscle Na+channels
Ruff, R. L. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.277.5.c937 · Cited by 128
Genotype phenotype associations across the voltage-gated sodium channel family
Brunklaus, A., Ellis, R., Reavey, E., Semsarian, C., & Zuberi, S. M. (2014) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2014-102608 · Cited by 92
Metadata
- Authors
- Chahine, M., George, A. L., Zhou, M., Ji, S., Sun, W., Barchi, R. L., & Horn, R.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1994-02
- Volume
- 12
- Issue
- 2
- Pages
- 281-294
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1973420297
- Cited by
- 340
- References
- 50
- FWCI
- 9.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Chahine, M., George, A. L., Zhou, M., Ji, S., Sun, W., Barchi, R. L., & Horn, R. (1994). Sodium channel mutations in paramyotonia congenita uncouple inactivation from activation. Neuron. https://doi.org/10.1016/0896-6273(94)90271-2
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