Differential effects of homologous S4 mutations in human skeletal muscle sodium channels on deactivation gating from open and inactivated states

1. The outermost charged amino acid of S4 segments in the α subunit of human skeletal muscle sodium channels was mutated to cysteine in domains I (R219C), II (R669C), III (K1126C), and IV (R1448C). Double mutations in DIS4 and DIVS4 (R219C/R1448C), DIIS4 and DIVS4 (R669C/R1448C), and DIIIS4 and DIVS...

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Hlavní autoři: Groome, James R, Fujimoto, Esther, George, Alfred L, Ruben, Peter C
Médium: Artigo
Jazyk:Inglês
Vydáno: Blackwell Science Inc 1999
Témata:
Original Articles
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2269298/
https://ncbi.nlm.nih.gov/pubmed/10200418
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/j.1469-7793.1999.0687u.x
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